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Protein

Collagen alpha-1(IV) chain

Gene

Col4a1

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 IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.1 Publication
Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.By similarity

<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

  • basement membrane organization Source: MGI
  • blood vessel morphogenesis Source: MGI
  • brain development Source: MGI
  • branching involved in blood vessel morphogenesis Source: MGI
  • cellular response to amino acid stimulus Source: MGI
  • collagen-activated tyrosine kinase receptor signaling pathway Source: MGI
  • epithelial cell differentiation Source: Ensembl
  • extracellular matrix organization Source: GO_Central
  • neuromuscular junction development Source: MGI
  • renal tubule morphogenesis Source: MGI
  • retinal blood vessel morphogenesis Source: MGI

<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

Biological processAngiogenesis

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-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000157 Laminin interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-419037 NCAM1 interactions
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-1(IV) chain
Cleaved into the following 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:Col4a1
<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 8

Organism-specific databases

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

More...
MGIi
MGI:88454 Col4a1

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice develop perinatal cerebral hemorrhage and porencephaly. The mutant protein inhibits the secretion of mutant and normal proteins into the basement membrane of embryonic origin. The mutation is semidominant.1 Publication

<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 – 27Add BLAST27
<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_000000575028 – 172N-terminal propeptide (7S domain)Add BLAST145
<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_0000005751173 – 1669Collagen alpha-1(IV) chainAdd BLAST1497
ChainiPRO_00003904831445 – 1669ArrestenAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei2043-hydroxyprolineBy similarity1
Modified residuei2073-hydroxyprolineBy similarity1
Modified residuei2103-hydroxyprolineBy similarity1
Modified residuei5873-hydroxyprolineBy similarity1
Modified residuei6023-hydroxyproline1 Publication1
Modified residuei6034-hydroxyproline1 Publication1
Modified residuei6053-hydroxyproline1 Publication1
Modified residuei6064-hydroxyproline1 Publication1
Modified residuei6234-hydroxyproline1 Publication1
Modified residuei6264-hydroxyproline1 Publication1
Modified residuei6294-hydroxyproline1 Publication1
Modified residuei6324-hydroxyproline1 Publication1
Modified residuei6473-hydroxyprolineBy similarity1
Modified residuei12143-hydroxyprolineBy similarity1
Modified residuei14243-hydroxyprolineBy similarity1
<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 bondi1460 ↔ 1551Or C-1460 with C-1548PROSITE-ProRule annotation
Disulfide bondi1493 ↔ 1548Or C-1493 with C-1551PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1511PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)By similarity
Disulfide bondi1570 ↔ 1665Or C-1570 with C-1662PROSITE-ProRule annotation
Disulfide bondi1604 ↔ 1662Or C-1604 with C-1665PROSITE-ProRule annotation
Disulfide bondi1616 ↔ 1622PROSITE-ProRule annotation
Cross-linki1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)By similarity

<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

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated.1 Publication
Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication
Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.2 Publications
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.By similarity
The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues. These cross-links are important for the mechanical stability of the basement membrane.1 Publication
Proteolytic processing produces the C-terminal NC1 peptide, arresten.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P02463

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

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PaxDbi
P02463

PeptideAtlas

More...
PeptideAtlasi
P02463

PRoteomics IDEntifications database

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PRIDEi
P02463

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02463

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

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PhosphoSitePlusi
P02463

<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

Detected in the basement membrane of the cornea (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000031502 Expressed in 351 organ(s), highest expression level in epithelium of lens

CleanEx database of gene expression profiles

More...
CleanExi
MM_COL4A1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02463 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02463 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

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198816, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2959 Collagen type IV trimer variant 1

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02463

Protein interaction database and analysis system

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IntActi
P02463, 1 interactor

Molecular INTeraction database

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MINTi
P02463

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000033898

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02463

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

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SMRi
P02463

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Domaini1445 – 1669Collagen IV NC1PROSITE-ProRule annotationAdd BLAST225

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>Regioni173 – 1440Triple-helical regionAdd BLAST1268

<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

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.Curated

<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 type IV collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3544 Eukaryota
ENOG410XNMM LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157678

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004933

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02463

KEGG Orthology (KO)

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KOi
K06237

Database of Orthologous Groups

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OrthoDBi
63831at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P02463

TreeFam database of animal gene trees

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TreeFami
TF316865

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.170.240.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008160 Collagen
IPR001442 Collagen_IV_NC
IPR036954 Collagen_IV_NC_sf
IPR016187 CTDL_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01413 C4, 2 hits
PF01391 Collagen, 17 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00111 C4, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56436 SSF56436, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51403 NC1_IV, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P02463-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPRLSVWLL LLFAALLLHE ERSRAAAKGD CGGSGCGKCD CHGVKGQKGE
60 70 80 90 100
RGLPGLQGVI GFPGMQGPEG PHGPPGQKGD AGEPGLPGTK GTRGPPGAAG
110 120 130 140 150
YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPLGPPGL PGFSGNPGPP
160 170 180 190 200
GLPGMKGDPG EILGHVPGTL LKGERGFPGI PGMPGSPGLP GLQGPVGPPG
210 220 230 240 250
FTGPPGPPGP PGPPGEKGQM GSSFQGPKGD KGEQGVSGPP GVPGQAQVKE
260 270 280 290 300
KGDFAPTGEK GQKGEPGFPG VPGYGEKGEP GKQGPRGKPG KDGEKGERGS
310 320 330 340 350
PGIPGDSGYP GLPGRQGPQG EKGEAGLPGP PGTVIGTMPL GEKGDRGYPG
360 370 380 390 400
APGLRGEPGP KGFPGTPGQP GPPGFPTPGQ AGAPGFPGER GEKGDQGFPG
410 420 430 440 450
VSLPGPSGRD GAPGPPGPPG PPGQPGHTNG IVECQPGPPG DQGPPGTPGQ
460 470 480 490 500
PGLTGEVGQK GQKGESCLAC DTEGLRGPPG PQGPPGEIGF PGQPGAKGDR
510 520 530 540 550
GLPGRDGLEG LPGPQGSPGL IGQPGAKGEP GEIFFDMRLK GDKGDPGFPG
560 570 580 590 600
QPGMPGRAGT PGRDGHPGLP GPKGSPGSIG LKGERGPPGG VGFPGSRGDI
610 620 630 640 650
GPPGPPGVGP IGPVGEKGQA GFPGGPGSPG LPGPKGEAGK VVPLPGPPGA
660 670 680 690 700
AGLPGSPGFP GPQGDRGFPG TPGRPGIPGE KGAVGQPGIG FPGLPGPKGV
710 720 730 740 750
DGLPGEIGRP GSPGRPGFNG LPGNPGPQGQ KGEPGIGLPG LKGQPGLPGI
760 770 780 790 800
PGTPGEKGSI GGPGVPGEQG LTGPPGLQGI RGDPGPPGVQ GPAGPPGVPG
810 820 830 840 850
IGPPGAMGPP GGQGPPGSSG PPGIKGEKGF PGFPGLDMPG PKGDKGSQGL
860 870 880 890 900
PGLTGQSGLP GLPGQQGTPG VPGFPGSKGE MGVMGTPGQP GSPGPAGTPG
910 920 930 940 950
LPGEKGDHGL PGSSGPRGDP GFKGDKGDVG LPGMPGSMEH VDMGSMKGQK
960 970 980 990 1000
GDQGEKGQIG PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGLSGT
1010 1020 1030 1040 1050
PGSPGLPGPK GSVGGMGLPG SPGEKGVPGI PGSQGVPGSP GEKGAKGEKG
1060 1070 1080 1090 1100
QSGLPGIGIP GRPGDKGDQG LAGFPGSPGE KGEKGSAGTP GMPGSPGPRG
1110 1120 1130 1140 1150
SPGNIGHPGS PGLPGEKGDK GLPGLDGVPG VKGEAGLPGT PGPTGPAGQK
1160 1170 1180 1190 1200
GEPGSDGIPG SAGEKGEQGV PGRGFPGFPG SKGDKGSKGE VGFPGLAGSP
1210 1220 1230 1240 1250
GIPGVKGEQG FMGPPGPQGQ PGLPGTPGHP VEGPKGDRGP QGQPGLPGHP
1260 1270 1280 1290 1300
GPMGPPGFPG INGPKGDKGN QGWPGAPGVP GPKGDPGFQG MPGIGGSPGI
1310 1320 1330 1340 1350
TGSKGDMGLP GVPGFQGQKG LPGLQGVKGD QGDQGVPGPK GLQGPPGPPG
1360 1370 1380 1390 1400
PYDVIKGEPG LPGPEGPPGL KGLQGPPGPK GQQGVTGSVG LPGPPGVPGF
1410 1420 1430 1440 1450
DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR
1460 1470 1480 1490 1500
HSQTTDDPLC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
1510 1520 1530 1540 1550
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPISGDN IRPFISRCAV
1560 1570 1580 1590 1600
CEAPAMVMAV HSQTIQIPQC PNGWSSLWIG YSFVMHTSAG AEGSGQALAS
1610 1620 1630 1640 1650
PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL
1660
KAGELRTHVS RCQVCMRRT
Length:1,669
Mass (Da):160,679
Last modified:February 20, 2007 - v4
<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:iEFEEC72AF301E5CF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1B0GSI7A0A1B0GSI7_MOUSE
Collagen alpha-1(IV) chain
Col4a1
1,562Annotation score:

Annotation score:1 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>
A0A140LHU8A0A140LHU8_MOUSE
Collagen alpha-1(IV) chain
Col4a1
133Annotation score:

Annotation score:1 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>
A0A1B0GRC0A0A1B0GRC0_MOUSE
Collagen alpha-1(IV) chain
Col4a1
328Annotation score:

Annotation score:1 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>
A0A1B0GT69A0A1B0GT69_MOUSE
Collagen alpha-1(IV) chain
Col4a1
126Annotation score:

Annotation score:1 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>

<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 AAH72650 differs from that shown. Insertion sequence.Curated
The sequence AAH72650 differs from that shown. Reason: Frameshift at position 1547.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 conflicti26A → P in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti186S → L in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti319Q → S in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti369Q → L in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti403L → F in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti481P → L in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti493Q → H in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti621G → S in BAE27208 (PubMed:16141072).Curated1
Sequence conflicti712S → I in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti813Q → E in AAA50292 (PubMed:2703490).Curated1
Sequence conflicti982Q → H in CAA29946 (PubMed:3338568).Curated1
Sequence conflicti1397V → S in AAA37342 (PubMed:3755692).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

More...
DDBJi
Links Updated
J04694 mRNA Translation: AAA50292.1
AK142097 mRNA Translation: BAE24936.1
AK146487 mRNA Translation: BAE27208.1
AK147284 mRNA Translation: BAE27820.1
AK147355 mRNA Translation: BAE27863.1
AK147661 mRNA Translation: BAE28055.1
BC002269 mRNA Translation: AAH02269.1
BC056620 mRNA Translation: AAH56620.1
BC072650 mRNA Translation: AAH72650.1 Sequence problems.
X06777 mRNA Translation: CAA29946.1
J03758 mRNA Translation: AAA37439.1
J03944 Genomic DNA Translation: AAA37442.1
J04448 Genomic DNA Translation: AAA37437.1
M23333 Genomic DNA Translation: AAA51625.1
M12879 Genomic DNA Translation: AAA37343.1
M13024 Genomic DNA No translation available.
M13025 Genomic DNA No translation available.
M13026 Genomic DNA Translation: AAA37344.1
M13027 Genomic DNA Translation: AAA37345.1
M13043 Genomic DNA Translation: AAA37346.1
M14042 mRNA Translation: AAA37342.1
X02201 mRNA Translation: CAA26132.1
M15832 mRNA Translation: AAA37340.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS40219.1

Protein sequence database of the Protein Information Resource

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PIRi
A33525 CGMS4B

NCBI Reference Sequences

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RefSeqi
NP_034061.2, NM_009931.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.738

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000033898; ENSMUSP00000033898; ENSMUSG00000031502

Database of genes from NCBI RefSeq genomes

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GeneIDi
12826

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12826

UCSC genome browser

More...
UCSCi
uc009kvb.2 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
J04694 mRNA Translation: AAA50292.1
AK142097 mRNA Translation: BAE24936.1
AK146487 mRNA Translation: BAE27208.1
AK147284 mRNA Translation: BAE27820.1
AK147355 mRNA Translation: BAE27863.1
AK147661 mRNA Translation: BAE28055.1
BC002269 mRNA Translation: AAH02269.1
BC056620 mRNA Translation: AAH56620.1
BC072650 mRNA Translation: AAH72650.1 Sequence problems.
X06777 mRNA Translation: CAA29946.1
J03758 mRNA Translation: AAA37439.1
J03944 Genomic DNA Translation: AAA37442.1
J04448 Genomic DNA Translation: AAA37437.1
M23333 Genomic DNA Translation: AAA51625.1
M12879 Genomic DNA Translation: AAA37343.1
M13024 Genomic DNA No translation available.
M13025 Genomic DNA No translation available.
M13026 Genomic DNA Translation: AAA37344.1
M13027 Genomic DNA Translation: AAA37345.1
M13043 Genomic DNA Translation: AAA37346.1
M14042 mRNA Translation: AAA37342.1
X02201 mRNA Translation: CAA26132.1
M15832 mRNA Translation: AAA37340.1
CCDSiCCDS40219.1
PIRiA33525 CGMS4B
RefSeqiNP_034061.2, NM_009931.2
UniGeneiMm.738

3D structure databases

ProteinModelPortaliP02463
SMRiP02463
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198816, 1 interactor
ComplexPortaliCPX-2959 Collagen type IV trimer variant 1
CORUMiP02463
IntActiP02463, 1 interactor
MINTiP02463
STRINGi10090.ENSMUSP00000033898

PTM databases

iPTMnetiP02463
PhosphoSitePlusiP02463

Proteomic databases

MaxQBiP02463
PaxDbiP02463
PeptideAtlasiP02463
PRIDEiP02463

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033898; ENSMUSP00000033898; ENSMUSG00000031502
GeneIDi12826
KEGGimmu:12826
UCSCiuc009kvb.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1282
MGIiMGI:88454 Col4a1

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000157678
HOVERGENiHBG004933
InParanoidiP02463
KOiK06237
OrthoDBi63831at2759
PhylomeDBiP02463
TreeFamiTF316865

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-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000157 Laminin interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-419037 NCAM1 interactions
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

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

More...
ChiTaRSi
Col4a1 mouse

Protein Ontology

More...
PROi
PR:P02463

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031502 Expressed in 351 organ(s), highest expression level in epithelium of lens
CleanExiMM_COL4A1
ExpressionAtlasiP02463 baseline and differential
GenevisibleiP02463 MM

Family and domain databases

Gene3Di2.170.240.10, 1 hit
InterProiView protein in InterPro
IPR008160 Collagen
IPR001442 Collagen_IV_NC
IPR036954 Collagen_IV_NC_sf
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF01413 C4, 2 hits
PF01391 Collagen, 17 hits
SMARTiView protein in SMART
SM00111 C4, 2 hits
SUPFAMiSSF56436 SSF56436, 2 hits
PROSITEiView protein in PROSITE
PS51403 NC1_IV, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCO4A1_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: P02463
Secondary accession number(s): Q3UHJ4
, Q3UJE7, Q3UQV2, Q53X35, Q6GQS7, Q6PHB5, Q99LQ8
<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: July 21, 1986
Last sequence update: February 20, 2007
Last modified: January 16, 2019
This is version 179 of the entry and version 4 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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