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Entry version 219 (16 Oct 2019)
Sequence version 3 (01 Dec 1992)
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Protein

Interstitial collagenase

Gene

MMP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:2557822, PubMed:2153297, PubMed:1645757). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Can be activated without removal of the activation peptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi92Zinc 2; in inhibited formCombined sources1 Publication1
Metal bindingi124Calcium 1Combined sources1 Publication1
Metal bindingi158Calcium 2Combined sources3 Publications1
Metal bindingi168Zinc 1Combined sources6 Publications1
Metal bindingi170Zinc 1Combined sources6 Publications1
Metal bindingi175Calcium 3Combined sources5 Publications1
Metal bindingi176Calcium 3; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi178Calcium 3; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi180Calcium 3; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi183Zinc 1Combined sources6 Publications1
Metal bindingi190Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi192Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi194Calcium 2Combined sources3 Publications1
Metal bindingi196Zinc 1Combined sources6 Publications1
Metal bindingi198Calcium 3Combined sources5 Publications1
Metal bindingi199Calcium 1Combined sources2 Publications1
Metal bindingi201Calcium 3Combined sources6 Publications1
Metal bindingi218Zinc 2; catalyticCombined sources6 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2191
Metal bindingi222Zinc 2; catalyticCombined sources6 Publications1
Metal bindingi228Zinc 2; catalyticCombined sources6 Publications1
Metal bindingi285Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi329Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi378Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi427Calcium 4; via carbonyl oxygenCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation, Host-virus interaction
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.7 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-210991 Basigin interactions
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P03956

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M10.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Interstitial collagenase (EC:3.4.24.74 Publications)
Alternative name(s):
Fibroblast collagenase
Matrix metalloproteinase-1
Short name:
MMP-1
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MMP1
Synonyms:CLG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7155 MMP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
120353 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P03956

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi360Y → F: Partial reduction of tyrosine phosphorylation in the presence of PKDCC/VLK. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
4312

MalaCards human disease database

More...
MalaCardsi
MMP1

Open Targets

More...
OpenTargetsi
ENSG00000196611

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
79408 Severe generalized recessive dystrophic epidermolysis bullosa

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30867

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P03956

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL332

Drug and drug target database

More...
DrugBanki
DB08482 [[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE ETHYL ESTER
DB00786 Marimastat
DB08403 METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID
DB07926 N-[3-(N'-HYDROXYCARBOXAMIDO)-2-(2-METHYLPROPYL)-PROPANOYL]-O-TYROSINE-N-METHYLAMIDE
DB07556 N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE
DB08491 N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE

DrugCentral

More...
DrugCentrali
P03956

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1628

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MMP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116852

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Add BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002870320 – 99Activation peptide1 PublicationAdd BLAST80
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000028704100 – 469Interstitial collagenaseAdd BLAST370
ChainiPRO_0000028705100 – 26922 kDa interstitial collagenaseAdd BLAST170
ChainiPRO_0000028706270 – 46927 kDa interstitial collagenaseAdd BLAST200

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei57Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000105120N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei274Phosphothreonine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi278 ↔ 466By similarity
Modified residuei360Phosphotyrosine; by PKDCC1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.1 Publication
Tyrosine phosphorylated in platelets by PKDCC/VLK.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei143Not glycosylated1 Publication1
Sitei269 – 270Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P03956

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P03956

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P03956

PeptideAtlas

More...
PeptideAtlasi
P03956

PRoteomics IDEntifications database

More...
PRIDEi
P03956

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
51623

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
301

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P03956

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P03956

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P03956

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P03956

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000196611 Expressed in 121 organ(s), highest expression level in smooth muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P03956 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA004920

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

(Microbial infection) Interacts with HIV-1 Tat.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110456, 8 interactors

Database of interacting proteins

More...
DIPi
DIP-529N

Protein interaction database and analysis system

More...
IntActi
P03956, 3 interactors

Molecular INTeraction database

More...
MINTi
P03956

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000322788

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P03956

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P03956

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03956

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati275 – 324Hemopexin 1Add BLAST50
Repeati325 – 371Hemopexin 2Add BLAST47
Repeati374 – 422Hemopexin 3Add BLAST49
Repeati423 – 466Hemopexin 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni98 – 276MetalloproteaseAdd BLAST179

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi90 – 97Cysteine switch2 Publications8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1565 Eukaryota
ENOG410XQ5D LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154907

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000217927

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P03956

KEGG Orthology (KO)

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KOi
K01388

Identification of Orthologs from Complete Genome Data

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OMAi
DFPGIGH

Database of Orthologous Groups

More...
OrthoDBi
1023460at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P03956

TreeFam database of animal gene trees

More...
TreeFami
TF315428

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.110.10.10, 1 hit
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001191 Peptidase_M10A_matrix, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00138 MATRIXIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P03956-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ
60 70 80 90 100
VEKRRNSGPV VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF
110 120 130 140 150
VLTEGNPRWE QTHLTYRIEN YTPDLPRADV DHAIEKAFQL WSNVTPLTFT
160 170 180 190 200
KVSEGQADIM ISFVRGDHRD NSPFDGPGGN LAHAFQPGPG IGGDAHFDED
210 220 230 240 250
ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY TFSGDVQLAQ
260 270 280 290 300
DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR
310 320 330 340 350
FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA
360 370 380 390 400
VQGQNVLHGY PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY
410 420 430 440 450
DEYKRSMDPG YPKMIAHDFP GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK
460
TKRILTLQKA NSWFNCRKN
Length:469
Mass (Da):54,007
Last modified:December 1, 1992 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4B1361DCF4C54B20
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti43N → K in AAA35700 (PubMed:3027129).Curated1
Sequence conflicti64Missing in AAA35700 (PubMed:3027129).Curated1
Sequence conflicti115T → R in AAA35699 (PubMed:3009463).Curated1
Sequence conflicti200D → H in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti208R → T in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti317I → T in CAA28858 (PubMed:3030290).Curated1
Sequence conflicti410G → S in AAA35699 (PubMed:3009463).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01196929Q → P. Corresponds to variant dbSNP:rs554499Ensembl.1
Natural variantiVAR_021024191I → V1 PublicationCorresponds to variant dbSNP:rs17879973Ensembl.1
Natural variantiVAR_011970252D → G. Corresponds to variant dbSNP:rs513964Ensembl.1
Natural variantiVAR_054005262R → S. Corresponds to variant dbSNP:rs12282811Ensembl.1
Natural variantiVAR_021025405R → Q1 PublicationCorresponds to variant dbSNP:rs17879165Ensembl.1
Natural variantiVAR_021026406S → T1 PublicationCorresponds to variant dbSNP:rs17884120Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X54925 mRNA Translation: CAA38691.1
X05231 mRNA Translation: CAA28858.1
M13509 mRNA Translation: AAA35699.1
U78045 Genomic DNA Translation: AAB36941.1
BT006874 mRNA Translation: AAP35520.1
AY769434 Genomic DNA Translation: AAV28732.1
BC013875 mRNA Translation: AAH13875.1
M16567 Genomic DNA Translation: AAA52033.1
M15996 mRNA Translation: AAA35700.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8322.1

Protein sequence database of the Protein Information Resource

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PIRi
A37308 KCHUI

NCBI Reference Sequences

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RefSeqi
NP_002412.1, NM_002421.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000315274; ENSP00000322788; ENSG00000196611

Database of genes from NCBI RefSeq genomes

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GeneIDi
4312

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4312

UCSC genome browser

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UCSCi
uc001phi.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Wikipedia

Collagenase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54925 mRNA Translation: CAA38691.1
X05231 mRNA Translation: CAA28858.1
M13509 mRNA Translation: AAA35699.1
U78045 Genomic DNA Translation: AAB36941.1
BT006874 mRNA Translation: AAP35520.1
AY769434 Genomic DNA Translation: AAV28732.1
BC013875 mRNA Translation: AAH13875.1
M16567 Genomic DNA Translation: AAA52033.1
M15996 mRNA Translation: AAA35700.1
CCDSiCCDS8322.1
PIRiA37308 KCHUI
RefSeqiNP_002412.1, NM_002421.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYKNMR-A101-269[»]
1CGEX-ray1.90A102-269[»]
1CGFX-ray2.10A/B102-263[»]
1CGLX-ray2.40A/B101-269[»]
1HFCX-ray1.50A101-269[»]
1SU3X-ray2.20A/B20-469[»]
2AYKNMR-A101-269[»]
2CLTX-ray2.67A/B100-466[»]
2J0TX-ray2.54A/B/C101-269[»]
2TCLX-ray2.20A101-269[»]
3AYKNMR-A101-269[»]
3SHIX-ray2.20A/G/M106-261[»]
4AUOX-ray3.00A/B100-466[»]
4AYKNMR-A101-269[»]
966CX-ray1.90A108-264[»]
SMRiP03956
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110456, 8 interactors
DIPiDIP-529N
IntActiP03956, 3 interactors
MINTiP03956
STRINGi9606.ENSP00000322788

Chemistry databases

BindingDBiP03956
ChEMBLiCHEMBL332
DrugBankiDB08482 [[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE ETHYL ESTER
DB00786 Marimastat
DB08403 METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID
DB07926 N-[3-(N'-HYDROXYCARBOXAMIDO)-2-(2-METHYLPROPYL)-PROPANOYL]-O-TYROSINE-N-METHYLAMIDE
DB07556 N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE
DB08491 N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE
DrugCentraliP03956
GuidetoPHARMACOLOGYi1628

Protein family/group databases

MEROPSiM10.001

PTM databases

GlyConnecti301
iPTMnetiP03956
PhosphoSitePlusiP03956
UniCarbKBiP03956

Polymorphism and mutation databases

BioMutaiMMP1
DMDMi116852

Proteomic databases

jPOSTiP03956
MassIVEiP03956
PaxDbiP03956
PeptideAtlasiP03956
PRIDEiP03956
ProteomicsDBi51623

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4312

Genome annotation databases

EnsembliENST00000315274; ENSP00000322788; ENSG00000196611
GeneIDi4312
KEGGihsa:4312
UCSCiuc001phi.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4312
DisGeNETi4312

GeneCards: human genes, protein and diseases

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GeneCardsi
MMP1
HGNCiHGNC:7155 MMP1
HPAiHPA004920
MalaCardsiMMP1
MIMi120353 gene
neXtProtiNX_P03956
OpenTargetsiENSG00000196611
Orphaneti79408 Severe generalized recessive dystrophic epidermolysis bullosa
PharmGKBiPA30867

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00940000154907
HOGENOMiHOG000217927
InParanoidiP03956
KOiK01388
OMAiDFPGIGH
OrthoDBi1023460at2759
PhylomeDBiP03956
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.7 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-210991 Basigin interactions
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SIGNORiP03956

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MMP1 human
EvolutionaryTraceiP03956

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MMP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4312
PharosiP03956
PMAP-CutDBiP03956

Protein Ontology

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PROi
PR:P03956

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196611 Expressed in 121 organ(s), highest expression level in smooth muscle tissue
GenevisibleiP03956 HS

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
PfamiView protein in Pfam
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03956
Secondary accession number(s): P08156
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: December 1, 1992
Last modified: October 16, 2019
This is version 219 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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