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Entry version 106 (03 Jul 2019)
Sequence version 1 (11 Oct 2005)
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Protein

Collagen alpha-2(V) chain

Gene

Col5a2

Organism
Mus musculus (Mouse)
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

Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices.By similarity3 Publications

Miscellaneous

Mice homozygous for the targeted deletion of the N-terminal telopeptide segment of the COL5A2 chain show poor survival rates, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils.3 Publications
The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer makes a critical contribution to fibrillogenesis, basement membrane organization, and cell viability, and may play a possible role in the development of a functional skin matrix.1 Publication

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 bindingi1312CalciumBy similarity1
Metal bindingi1314CalciumBy similarity1
Metal bindingi1315Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1320CalciumBy similarity1

<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

LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-186797 Signaling by PDGF
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-419037 NCAM1 interactions
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8948216 Collagen chain trimerization

<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:
Collagen alpha-2(V) chain
<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:Col5a2Imported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:88458 Col5a2

<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 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 – 26Sequence analysisAdd BLAST26
<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_000028376827 – 1227Collagen alpha-2(V) chainSequence analysisAdd BLAST1201
<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_00002837691228 – 1497C-terminal propeptideSequence analysisAdd BLAST270

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 residuei2884-hydroxyprolineBy similarity1
Modified residuei2914-hydroxyprolineBy similarity1
Modified residuei2944-hydroxyprolineBy similarity1
Modified residuei6094-hydroxyprolineBy similarity1
Modified residuei6154-hydroxyprolineBy similarity1
<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>Glycosylationi1260N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi1294 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1334 ↔ 1495PROSITE-ProRule annotation
Glycosylationi1398N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1403 ↔ 1448PROSITE-ProRule annotation

<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

Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on prolines by LEPREL1.
Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
Q3U962

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

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PaxDbi
Q3U962

PeptideAtlas

More...
PeptideAtlasi
Q3U962

PRoteomics IDEntifications database

More...
PRIDEi
Q3U962

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q3U962

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

More...
PhosphoSitePlusi
Q3U962

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in embryos from 9 days of gestation onward. In 12.5 dpc embryos, low and diffuse level of expression was observed in the peritoneal membranes and intestinal and craniofacial mesenchymes. By 16.5 dpc, expression is higher and exhibits a more restricted accumulation in primary ossified regions, perichondrium, joints, tendon, atrioventricular valve of heart, and in selected portions of the head.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026042 Expressed in 303 organ(s), highest expression level in vault of skull

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q3U962 MM

<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

Trimers of two alpha 1(V) and one alpha 2(V) chains expressed in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains with a more limited distribution of expression.

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2962 Collagen type V trimer variant 1
CPX-2963 Collagen type V trimer variant 2
CPX-2976 Collagen type XI trimer variant 2
CPX-2977 Collagen type XI trimer variant 3

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000083620

<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

3D structure databases

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

More...
SMRi
Q3U962

Database of comparative protein structure models

More...
ModBasei
Search...

<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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 96VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1264 – 1497Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

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>Motifi141 – 143Cell attachment siteSequence analysis3
Motifi504 – 506Cell attachment siteSequence analysis3
Motifi942 – 944Cell attachment siteSequence analysis3
Motifi1065 – 1067Cell attachment siteSequence analysis3
Motifi1068 – 1070Cell attachment siteSequence analysis3
Motifi1125 – 1127Cell attachment siteSequence analysis3
Motifi1134 – 1136Cell attachment siteSequence analysis3

<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

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).By similarity

<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 fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3544 Eukaryota
ENOG4110XTV LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155675

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q3U962

KEGG Orthology (KO)

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KOi
K19721

Identification of Orthologs from Complete Genome Data

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OMAi
LCDKIEC

Database of Orthologous Groups

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OrthoDBi
1406711at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q3U962

TreeFam database of animal gene trees

More...
TreeFami
TF344135

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits
PF00093 VWC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 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.

Q3U962-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR
60 70 80 90 100
DIWKPSPCQI CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG
110 120 130 140 150
GDTSFGRGRK GQKGEPGLVP VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP
160 170 180 190 200
GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP GPDGMSRPFS AQMAGLDEKS
210 220 230 240 250
GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP GEPGPMGPIG
260 270 280 290 300
SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR
310 320 330 340 350
GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA
360 370 380 390 400
PGKRGAHGMP GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG
410 420 430 440 450
QRGETGPPGP AGSQGLPGAV GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP
460 470 480 490 500
GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK GEPGPHGIQG PIGPPGEEGK
510 520 530 540 550
RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ GERGPVGSSG
560 570 580 590 600
PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP
610 620 630 640 650
GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP
660 670 680 690 700
SGPVGPPGLA GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG
710 720 730 740 750
AVGPLGPRGE RGNPGERGEP GITGLPGEKG MAGGHGPDGP KGNPGPTGTI
760 770 780 790 800
GDTGPPGLQG MPGERGIAGT PGPKGDRGGI GEKGAEGTAG NDGARGLPGP
810 820 830 840 850
LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT GAVGFAGPQG
860 870 880 890 900
PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ
910 920 930 940 950
GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR
960 970 980 990 1000
VGDRGPAGPP GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG
1010 1020 1030 1040 1050
ERGMPGLPGP AGTPGKVGPT GATGDKGPPG PVGPPGSNGP VGEPGPEGPA
1060 1070 1080 1090 1100
GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ GAPGTPGPVG APGDAGQRGE
1110 1120 1130 1140 1150
PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK GHRGFTGLQG
1160 1170 1180 1190 1200
LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR
1210 1220 1230 1240 1250
GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT
1260 1270 1280 1290 1300
EDQAAPDDTN KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC
1310 1320 1330 1340 1350
HPTKQSGEYW IDPNQGSAED AIKVYCNMET GETCISANPA SVPRKTWWAS
1360 1370 1380 1390 1400
KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT AITQMTFLRL LSKEASQNLT
1410 1420 1430 1440 1450
YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR YTVLQDTCSK
1460 1470 1480 1490
RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM
Length:1,497
Mass (Da):145,018
Last modified:October 11, 2005 - v1
<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:iCAAE15514984DB41
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAE23896 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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 conflicti20Y → D in BAE23896 (PubMed:16141072).Curated1
Sequence conflicti88T → P in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti160G → R in BAE27850 (PubMed:16141072).Curated1
Sequence conflicti164V → M in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti222Q → V in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti231V → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti387A → R in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti390T → H in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti428A → R in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti431P → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti614L → V in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti614L → V in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti666Q → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti809 – 813PTGEK → LLGAP in AAA37440 (PubMed:1297453).Curated5
Sequence conflicti851P → S in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti1001 – 1002ER → VT in AAA37440 (PubMed:1297453).Curated2
Sequence conflicti1013T → A in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti1063G → V in BAE21154 (PubMed:16141072).Curated1
Sequence conflicti1181P → S in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti1337A → T in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti1388L → F in AAA37440 (PubMed:1297453).Curated1

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
L02918 mRNA Translation: AAA37440.1
AK132413 mRNA Translation: BAE21154.1
AK139130 mRNA Translation: BAE23896.1 Different initiation.
AK147220 mRNA Translation: BAE27775.1
AK147328 mRNA Translation: BAE27850.1
AK151929 mRNA Translation: BAE30805.1
AK160008 mRNA Translation: BAE35556.1
BC043696 mRNA Translation: AAH43696.1
BC055077 mRNA Translation: AAH55077.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS35555.1

Protein sequence database of the Protein Information Resource

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PIRi
I49607

NCBI Reference Sequences

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RefSeqi
NP_031763.2, NM_007737.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042

Database of genes from NCBI RefSeq genomes

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GeneIDi
12832

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12832

UCSC genome browser

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UCSCi
uc007awr.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02918 mRNA Translation: AAA37440.1
AK132413 mRNA Translation: BAE21154.1
AK139130 mRNA Translation: BAE23896.1 Different initiation.
AK147220 mRNA Translation: BAE27775.1
AK147328 mRNA Translation: BAE27850.1
AK151929 mRNA Translation: BAE30805.1
AK160008 mRNA Translation: BAE35556.1
BC043696 mRNA Translation: AAH43696.1
BC055077 mRNA Translation: AAH55077.1
CCDSiCCDS35555.1
PIRiI49607
RefSeqiNP_031763.2, NM_007737.2

3D structure databases

SMRiQ3U962
ModBaseiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2962 Collagen type V trimer variant 1
CPX-2963 Collagen type V trimer variant 2
CPX-2976 Collagen type XI trimer variant 2
CPX-2977 Collagen type XI trimer variant 3
STRINGi10090.ENSMUSP00000083620

PTM databases

iPTMnetiQ3U962
PhosphoSitePlusiQ3U962

Proteomic databases

MaxQBiQ3U962
PaxDbiQ3U962
PeptideAtlasiQ3U962
PRIDEiQ3U962

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042
GeneIDi12832
KEGGimmu:12832
UCSCiuc007awr.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1290
MGIiMGI:88458 Col5a2

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG4110XTV LUCA
GeneTreeiENSGT00940000155675
InParanoidiQ3U962
KOiK19721
OMAiLCDKIEC
OrthoDBi1406711at2759
PhylomeDBiQ3U962
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-186797 Signaling by PDGF
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-419037 NCAM1 interactions
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

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

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ChiTaRSi
Col5a2 mouse

Protein Ontology

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PROi
PR:Q3U962

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026042 Expressed in 303 organ(s), highest expression level in vault of skull
GenevisibleiQ3U962 MM

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits
PF00093 VWC, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 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 nameiCO5A2_MOUSE
<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: Q3U962
Secondary accession number(s): Q3TVR2
, Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
<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: April 3, 2007
Last sequence update: October 11, 2005
Last modified: July 3, 2019
This is version 106 of the entry and version 1 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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