Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 179 (18 Sep 2019)
Sequence version 1 (01 Oct 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Leucine-rich repeat transmembrane protein FLRT3

Gene

FLRT3

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

Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:26235030). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity). Promotes neurite outgrowth (in vitro) (PubMed:14706654). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length. Plays a role in the regulation of the density of glutamaergic synapses. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning. Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development. Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (By similarity).By similarity2 Publications

<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 functionDevelopmental protein
Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-376176 Signaling by ROBO receptors
R-HSA-5654687 Downstream signaling of activated FGFR1

<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:
Leucine-rich repeat transmembrane protein FLRT3
Alternative name(s):
Fibronectin-like domain-containing leucine-rich transmembrane protein 3
<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:FLRT3
Synonyms:KIAA1469
ORF Names:UNQ856/PRO1865
<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 20

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3762 FLRT3

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604808 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NZU0

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini29 – 528ExtracellularSequence analysisAdd BLAST500
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei529 – 549HelicalSequence analysisAdd BLAST21
Topological domaini550 – 649CytoplasmicSequence analysisAdd BLAST100

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Membrane, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypogonadotropic hypogonadism 21 with or without anosmia (HH21)1 Publication
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FLRT3 also have a mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17 (PubMed:23643382).1 Publication
Disease descriptionA disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH).
Related information in OMIM
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_06995069Q → K in HH21; rare variant associated with susceptibility to disease; the patient has a second mutation in the HH-associated gene FGFR1. 1 PublicationCorresponds to variant dbSNP:rs398124653EnsemblClinVar.1
Natural variantiVAR_06995197E → G in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17. 1 PublicationCorresponds to variant dbSNP:rs398124651EnsemblClinVar.1
Natural variantiVAR_069952144S → I in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17. 1 PublicationCorresponds to variant dbSNP:rs398124652EnsemblClinVar.1
Natural variantiVAR_069953339K → R in HH21. 1 PublicationCorresponds to variant dbSNP:rs398124654EnsemblClinVar.1

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>Mutagenesisi38D → A: Abolishes ADGRL3 binding; when associated with A-43; A-45 and A-47. 1 Publication1
Mutagenesisi43Y → A: Abolishes ADGRL3 binding; when associated with A-64. Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-47. 1 Publication1
Mutagenesisi45N → A: Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-47. 1 Publication1
Mutagenesisi47R → A: Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-45. 1 Publication1
Mutagenesisi64Y → A: Abolishes ADGRL3 binding; when associated with A-43. 1 Publication1
Mutagenesisi89Y → A: Abolishes ADGRL3 binding; when associated with A-91. 1 Publication1
Mutagenesisi91Y → A: Abolishes ADGRL3 binding; when associated with A-89. 1 Publication1
Mutagenesisi181R → A: No effect on homodimerization; when associated with A-183. 1 Publication1
Mutagenesisi181R → N: Adds a glycosylation site that strongly reduces homodimerization; when associated with T-183. 1 Publication1
Mutagenesisi183D → A: No effect on homodimerization; when associated with A-181. 1 Publication1
Mutagenesisi183D → T: Adds a glycosylation site that strongly reduces homodimerization; when associated with T-183. 1 Publication1

Keywords - Diseasei

Disease mutation, Hypogonadotropic hypogonadism, Kallmann syndrome

Organism-specific databases

DisGeNET

More...
DisGeNETi
23767

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
FLRT3

MalaCards human disease database

More...
MalaCardsi
FLRT3
MIMi615271 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000125848

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

More...
Orphaneti
478 Kallmann syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA28179

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FLRT3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
20138400

<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 – 28Sequence analysisAdd BLAST28
<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_000002128029 – 649Leucine-rich repeat transmembrane protein FLRT3Add BLAST621

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi31 ↔ 371 Publication
Disulfide bondi35 ↔ 441 Publication
<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>Glycosylationi226N-linked (GlcNAc...) asparagineSequence analysis1 Publication1
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi309 ↔ 3341 Publication

<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

N-glycosylated.By similarity
Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9NZU0

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9NZU0

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9NZU0

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9NZU0

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

More...
PaxDbi
Q9NZU0

PeptideAtlas

More...
PeptideAtlasi
Q9NZU0

PRoteomics IDEntifications database

More...
PRIDEi
Q9NZU0

ProteomicsDB human proteome resource

More...
ProteomicsDBi
83509

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1454

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9NZU0

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

More...
PhosphoSitePlusi
Q9NZU0

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in kidney, brain, pancreas, skeletal muscle, lung, liver, placenta, and heart.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000125848 Expressed in 203 organ(s), highest expression level in metanephros

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9NZU0 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB026166
HPA056033

<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

Monomer and homodimer. Self-associates (via leucine-rich repeats), giving rise to homooligomers (PubMed:26235030).

Interacts with FGFR1.

Interacts (via extracellular domain) with ADGRL1/LPHN1 and LPHN2 (via olfactomedin-like domain) (By similarity).

Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like domain); the interaction is direct (PubMed:26235030).

Interacts (via extracellular domain) with UNC5B and UNC5D (via extracellular domain); the interaction is direct (PubMed:26235030). Identified in complexes composed of FLRT3, ADGRL3 and UNC5B, respectively FLRT3, ADGRL3 and UNC5D (PubMed:26235030). May also interact (via extracellular domain) with UNC5A and UNC5C.

Interacts (via cytoplasmic domain) with ROBO1 (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
117267, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9NZU0

Database of interacting proteins

More...
DIPi
DIP-50407N

Protein interaction database and analysis system

More...
IntActi
Q9NZU0, 5 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000367292

<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

1649
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

More...
SMRi
Q9NZU0

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>Domaini29 – 58LRRNTSequence analysisAdd BLAST30
<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>Repeati59 – 80LRR 1Sequence analysisAdd BLAST22
Repeati84 – 104LRR 2Sequence analysisAdd BLAST21
Repeati105 – 126LRR 3Sequence analysisAdd BLAST22
Repeati129 – 150LRR 4Sequence analysisAdd BLAST22
Repeati155 – 175LRR 5Sequence analysisAdd BLAST21
Repeati176 – 197LRR 6Sequence analysisAdd BLAST22
Repeati200 – 220LRR 7Sequence analysisAdd BLAST21
Repeati226 – 247LRR 8Sequence analysisAdd BLAST22
Repeati248 – 269LRR 9Sequence analysisAdd BLAST22
Repeati272 – 293LRR 10Sequence analysisAdd BLAST22
Domaini305 – 357LRRCTSequence analysisAdd BLAST53
Domaini409 – 504Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST96

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>Regioni38 – 67Interaction with ADGRL31 PublicationAdd BLAST30

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IIEA Eukaryota
COG4886 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159704

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9NZU0

KEGG Orthology (KO)

More...
KOi
K16362

Identification of Orthologs from Complete Genome Data

More...
OMAi
SPYRVCM

Database of Orthologous Groups

More...
OrthoDBi
826997at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9NZU0

TreeFam database of animal gene trees

More...
TreeFami
TF331598

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000483 Cys-rich_flank_reg_C
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR000372 LRRNT

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13855 LRR_8, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00369 LRR_TYP, 7 hits
SM00082 LRRCT, 1 hit
SM00013 LRRNT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 1 hit
PS51450 LRR, 8 hits

<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.

Q9NZU0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MISAAWSIFL IGTKIGLFLQ VAPLSVMAKS CPSVCRCDAG FIYCNDRFLT
60 70 80 90 100
SIPTGIPEDA TTLYLQNNQI NNAGIPSDLK NLLKVERIYL YHNSLDEFPT
110 120 130 140 150
NLPKYVKELH LQENNIRTIT YDSLSKIPYL EELHLDDNSV SAVSIEEGAF
160 170 180 190 200
RDSNYLRLLF LSRNHLSTIP WGLPRTIEEL RLDDNRISTI SSPSLQGLTS
210 220 230 240 250
LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA PVNLPGTNLR
260 270 280 290 300
KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL
310 320 330 340 350
ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLNA
360 370 380 390 400
ELFDCKDSGI VSTIQITTAI PNTVYPAQGQ WPAPVTKQPD IKNPKLTKDH
410 420 430 440 450
QTTGSPSRKT ITITVKSVTS DTIHISWKLA LPMTALRLSW LKLGHSPAFG
460 470 480 490 500
SITETIVTGE RSEYLVTALE PDSPYKVCMV PMETSNLYLF DETPVCIETE
510 520 530 540 550
TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV TIALLALVCW
560 570 580 590 600
YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS
610 620 630 640
NEPISKEEFV IHTIFPPNGM NLYKNNHSES SSNRSYRDSG IPDSDHSHS
Length:649
Mass (Da):73,004
Last modified:October 1, 2000 - 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:i9EFF666C46181F08
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 BAA95993 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB55282 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB55303 differs from that shown. Reason: Erroneous initiation.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 conflicti198L → P in BAB55282 (PubMed:14702039).Curated1
Sequence conflicti307W → R in BAB55282 (PubMed:14702039).Curated1
Sequence conflicti519K → Q in BAB55023 (PubMed:14702039).Curated1
Sequence conflicti638D → G in BAB55282 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06995069Q → K in HH21; rare variant associated with susceptibility to disease; the patient has a second mutation in the HH-associated gene FGFR1. 1 PublicationCorresponds to variant dbSNP:rs398124653EnsemblClinVar.1
Natural variantiVAR_06995197E → G in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17. 1 PublicationCorresponds to variant dbSNP:rs398124651EnsemblClinVar.1
Natural variantiVAR_069952144S → I in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17. 1 PublicationCorresponds to variant dbSNP:rs398124652EnsemblClinVar.1
Natural variantiVAR_069953339K → R in HH21. 1 PublicationCorresponds to variant dbSNP:rs398124654EnsemblClinVar.1
Natural variantiVAR_050997377A → T. Corresponds to variant dbSNP:rs8120693EnsemblClinVar.1
Natural variantiVAR_017152400H → Q3 PublicationsCorresponds to variant dbSNP:rs6079391Ensembl.1
Natural variantiVAR_064714452I → V Found in a renal cell carcinoma case; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1393315241Ensembl.1
Natural variantiVAR_050998460E → D. Corresponds to variant dbSNP:rs35253731Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF169677 mRNA Translation: AAF28461.1
AB040902 mRNA Translation: BAA95993.1 Different initiation.
AK027297 mRNA Translation: BAB55023.1
AK027670 mRNA Translation: BAB55282.1 Different initiation.
AK027694 mRNA Translation: BAB55303.1 Different initiation.
AY358319 mRNA Translation: AAQ88685.1
AK074909 mRNA Translation: BAC11284.1
AL132826 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10300.1
CH471133 Genomic DNA Translation: EAX10301.1
BC020870 mRNA Translation: AAH20870.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13121.1

NCBI Reference Sequences

More...
RefSeqi
NP_037413.1, NM_013281.3
NP_938205.1, NM_198391.2
XP_005260739.1, XM_005260682.4
XP_011527506.1, XM_011529204.2
XP_011527507.1, XM_011529205.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000341420; ENSP00000339912; ENSG00000125848
ENST00000378053; ENSP00000367292; ENSG00000125848

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23767

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23767

UCSC genome browser

More...
UCSCi
uc002wov.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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169677 mRNA Translation: AAF28461.1
AB040902 mRNA Translation: BAA95993.1 Different initiation.
AK027297 mRNA Translation: BAB55023.1
AK027670 mRNA Translation: BAB55282.1 Different initiation.
AK027694 mRNA Translation: BAB55303.1 Different initiation.
AY358319 mRNA Translation: AAQ88685.1
AK074909 mRNA Translation: BAC11284.1
AL132826 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10300.1
CH471133 Genomic DNA Translation: EAX10301.1
BC020870 mRNA Translation: AAH20870.1
CCDSiCCDS13121.1
RefSeqiNP_037413.1, NM_013281.3
NP_938205.1, NM_198391.2
XP_005260739.1, XM_005260682.4
XP_011527506.1, XM_011529204.2
XP_011527507.1, XM_011529205.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5CMNX-ray3.61A/B/C/D29-357[»]
5CMPX-ray2.60A/B/C/D29-357[»]
SMRiQ9NZU0
ModBaseiSearch...

Protein-protein interaction databases

BioGridi117267, 3 interactors
CORUMiQ9NZU0
DIPiDIP-50407N
IntActiQ9NZU0, 5 interactors
STRINGi9606.ENSP00000367292

PTM databases

GlyConnecti1454
iPTMnetiQ9NZU0
PhosphoSitePlusiQ9NZU0

Polymorphism and mutation databases

BioMutaiFLRT3
DMDMi20138400

Proteomic databases

EPDiQ9NZU0
jPOSTiQ9NZU0
MassIVEiQ9NZU0
MaxQBiQ9NZU0
PaxDbiQ9NZU0
PeptideAtlasiQ9NZU0
PRIDEiQ9NZU0
ProteomicsDBi83509

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
23767
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341420; ENSP00000339912; ENSG00000125848
ENST00000378053; ENSP00000367292; ENSG00000125848
GeneIDi23767
KEGGihsa:23767
UCSCiuc002wov.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23767
DisGeNETi23767

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FLRT3
GeneReviewsiFLRT3
HGNCiHGNC:3762 FLRT3
HPAiCAB026166
HPA056033
MalaCardsiFLRT3
MIMi604808 gene
615271 phenotype
neXtProtiNX_Q9NZU0
OpenTargetsiENSG00000125848
Orphaneti478 Kallmann syndrome
PharmGKBiPA28179

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IIEA Eukaryota
COG4886 LUCA
GeneTreeiENSGT00940000159704
InParanoidiQ9NZU0
KOiK16362
OMAiSPYRVCM
OrthoDBi826997at2759
PhylomeDBiQ9NZU0
TreeFamiTF331598

Enzyme and pathway databases

ReactomeiR-HSA-376176 Signaling by ROBO receptors
R-HSA-5654687 Downstream signaling of activated FGFR1

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
FLRT3

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

More...
GenomeRNAii
23767

Pharos

More...
Pharosi
Q9NZU0

Protein Ontology

More...
PROi
PR:Q9NZU0

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000125848 Expressed in 203 organ(s), highest expression level in metanephros
GenevisibleiQ9NZU0 HS

Family and domain databases

Gene3Di2.60.40.10, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR000483 Cys-rich_flank_reg_C
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR000372 LRRNT
PfamiView protein in Pfam
PF13855 LRR_8, 2 hits
SMARTiView protein in SMART
SM00369 LRR_TYP, 7 hits
SM00082 LRRCT, 1 hit
SM00013 LRRNT, 1 hit
SUPFAMiSSF49265 SSF49265, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 1 hit
PS51450 LRR, 8 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiFLRT3_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: Q9NZU0
Secondary accession number(s): D3DW20
, Q542Z9, Q96K39, Q96K42, Q96KB1, Q9P259
<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: March 27, 2002
Last sequence update: October 1, 2000
Last modified: September 18, 2019
This is version 179 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
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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again