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Protein

Collagen alpha-3(IV) chain

Gene

Col4a3

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.By similarity1 Publication
Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms.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

Biological processCell adhesion

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-3(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:Col4a3Imported
<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)

More...
MGIi
MGI:104688 Col4a3

<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 exhibit normal pregnancy and wound healing, but consistent with the human hereditary disorder Alport syndrome they develop a progressive glomerulonephritis with microhematuria and proteinuria.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 – 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_000027969829 – 1669Collagen alpha-3(IV) chainSequence analysisAdd BLAST1641
ChainiPRO_00002796991424 – 1669Tumstatin1 PublicationAdd BLAST246

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
Glycosylationi253N-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 bondi1459 ↔ 1550Or C-1459 with C-1547PROSITE-ProRule annotationBy similarity
Disulfide bondi1492 ↔ 1547Or C-1492 with C-1550PROSITE-ProRule annotationBy similarity
Disulfide bondi1504 ↔ 1510PROSITE-ProRule annotationBy similarity
<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-linki1532S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1650)By similarity
Disulfide bondi1569 ↔ 1664Or C-1569 with C-1661PROSITE-ProRule annotationBy similarity
Disulfide bondi1603 ↔ 1661Or C-1603 with C-1664PROSITE-ProRule annotationBy similarity
Disulfide bondi1615 ↔ 1621PROSITE-ProRule annotationBy similarity
Cross-linki1650S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1532)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

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.PROSITE-ProRule annotationBy similarity
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.PROSITE-ProRule annotationBy similarity
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity
Phosphorylated by the Goodpasture antigen-binding protein/COL4A3BP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1424 – 1425Cleavage; by collagenaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9QZS0

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

More...
PaxDbi
Q9QZS0

PeptideAtlas

More...
PeptideAtlasi
Q9QZS0

PRoteomics IDEntifications database

More...
PRIDEi
Q9QZS0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9QZS0

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

More...
PhosphoSitePlusi
Q9QZS0

<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

Highly expressed in kidney and lung. Detected at lower levels in heart, muscle and skin.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000079465 Expressed in 93 organ(s), highest expression level in epithelium of lens

CleanEx database of gene expression profiles

More...
CleanExi
MM_COL4A3

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9QZS0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9QZS0 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. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite promoter, respectively. Interacts with COL4A3BP and ITGB3 (By similarity). Associates with LAMB2 at the neuromuscular junction and in GBM.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2961 Collagen type IV trimer variant 3

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000109084

<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

More...
ProteinModelPortali
Q9QZS0

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

More...
SMRi
Q9QZS0

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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>Domaini1444 – 1668Collagen 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>Regioni29 – 427S domainBy similarityAdd BLAST14
Regioni43 – 1436Triple-helical regionAdd BLAST1394
Regioni1425 – 1443Epitope recognized by Goodpasture antibodiesBy similarityAdd BLAST19
Regioni1478 – 1556Required for the anti-angiogenic activity of tumstatinBy similarityAdd BLAST79
Regioni1609 – 1627Required for the anti-tumor cell activity of tumstatinBy similarityAdd BLAST19

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>Motifi830 – 832Cell attachment siteSequence analysis3
Motifi994 – 996Cell attachment siteSequence analysis3
Motifi1152 – 1154Cell attachment siteSequence analysis3
Motifi1304 – 1306Cell 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

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.PROSITE-ProRule annotationBy 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 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
ENSGT00940000161675

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000085652

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004933

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9QZS0

KEGG Orthology (KO)

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KOi
K06237

Identification of Orthologs from Complete Genome Data

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OMAi
GCNGSKG

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0613

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9QZS0

TreeFam database of animal gene trees

More...
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

More...
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, 19 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

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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 2 potential isoforms that are computationally mapped.Show allAlign All

Q9QZS0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHSKTAPRFL VFLLLTLLLL LAASPVASKG CVCKGKGQCL CAGTKGEKGE
60 70 80 90 100
KGVPGSPGFP GQKGFPGPEG LPGPQGPKGS PGLPGLTGPK GIRGITGLPG
110 120 130 140 150
FAGPPGLPGL PGHPGPRGLA GLPGCNGSKG EQGFPGFPGT PGYAGLPGPD
160 170 180 190 200
GLKGQKGEPA QGEDRGFNGK GDPGPPGVPG FQGFPGLPGF PGPAGPPGPP
210 220 230 240 250
GFFGLPGAMG PRGPKGHMGD SVIGQKGERG MKGLTGPPGP PGTVIFTLTQ
260 270 280 290 300
PYNKSDFKGE KGDEGERGEP GPPGPSGPPG DSYGSEKGAP GEPGPRGKPG
310 320 330 340 350
KDGAPGFPGT EGAKGNRGFP GLRGEAGIKG RKGDIGPPGF PGPTEYYDAY
360 370 380 390 400
LEKGERGMPG LPGPKGARGP QGPSGPPGVP GSPGLSRPGL RGPIGWPGLK
410 420 430 440 450
GSKGERGPPG KDTVGPPGPL GCPGSPGPPG PPGPPGCPGD IVFKCSPGEH
460 470 480 490 500
GMPGDTGPPG VPGLDGPKGE PGSPCTECHC FPGPPGVPGF PGLDGIKGIP
510 520 530 540 550
GGRGVPGLKG NPGSPGSAGL PGFAGFPGDQ GHPGLKGDKG DTPLPWGQVG
560 570 580 590 600
NPGDPGLRGL PGRKGFDGTP GGPGAKGPPG PQGEPALSGR KGDQGPPGPP
610 620 630 640 650
GFPGPPGPAG PAGPPGYGPQ GEPGPKGAQG VPGVLGPPGE AGLKGEPSTS
660 670 680 690 700
TPDLGPPGPP GPPGQAGPRG LPGLPGPVGK CDPGLPGPDG EPGIPEAGCP
710 720 730 740 750
GPPGPKGNQG FPGTKGSPGC PGEMGKPGRP GEPGIPGAKG EPSVGRPGKP
760 770 780 790 800
GKPGFPGERG NAGENGDIGL PGLPGLPGTP GRGGLDGPPG DPGQPGSPGA
810 820 830 840 850
KGSPGRCIPG PRGTQGLPGL NGLKGQPGRR GDTGPKGDPG IPGMDRSGVP
860 870 880 890 900
GDPGPPGTPG CPGEMGPPGQ KGYPGAPGFP GPPGEKGEVG MMGYPGTTGP
910 920 930 940 950
PGLPGKPGSQ GQRGSLGIPG MKGEKGRPGA KGERGEKGKP GPSQTTLLKG
960 970 980 990 1000
DKGEPGLKGF VGNPGEKGNR GNPGLPGPKG LEGLPGLPGP PGPRGDTGSR
1010 1020 1030 1040 1050
GNPGRPGPHG MPGSMGIMGV PGPKGRKGTS GLPGLAGRPG LTGIHGPQGD
1060 1070 1080 1090 1100
KGEPGYSEGA RPGPPGPKGD PGLPGDKGKK GERGVPGPPG QSGPAGPDGA
1110 1120 1130 1140 1150
PGSPGSPGHP GKPGPAGDLG LKGQKGFPGP PGSTGPPGPP GLPGLPGPMG
1160 1170 1180 1190 1200
MRGDQGRDGI PGPPGEKGET GLLGAYPGPK GSPGVPGAKG DRGVPGLSGL
1210 1220 1230 1240 1250
PGRKGVMGDV GPQGPPGTAG LPGPPGLPGA IIPGPKGDRG LPGLRGNPGE
1260 1270 1280 1290 1300
PGPPGPPGPI GKGIKGDKGF MGPPGPKGLP GTVGDMGPPG FPGAPGTPGL
1310 1320 1330 1340 1350
PGVRGDPGFP GFPGIKGEKG NPGFLGPIGH PGPVGPKGPP GPRGKPGTLK
1360 1370 1380 1390 1400
VISLPGSPGP PGVPGQPGMK GDPGPLGLPG IPGPCGPRGK PGKDGKPGTP
1410 1420 1430 1440 1450
GPAGTKGNKG LKGQQGPPGL DGLPGLKGNP GDRGTPATGT RMRGFIFTRH
1460 1470 1480 1490 1500
SQTTAIPSCP EGTQPLYSGF SLLFVQGNKR AHGQDLGTLG SCLQRFTTMP
1510 1520 1530 1540 1550
FLFCNINNVC NFASRNDYSY WLSTPALMPM DMAPISGRAL EPYISRCTVC
1560 1570 1580 1590 1600
EGPAMAIAVH SQTTAIPPCP QDWVSLWKGF SFIMFTSAGS EGAGQALASP
1610 1620 1630 1640 1650
GSCLEEFRAS PFIECHGRGT CNYYSNSYSF WLASLNPERM FRKPIPSTVK
1660
AGDLEKIISR CQVCMKKRH
Length:1,669
Mass (Da):161,726
Last modified:March 6, 2007 - v2
<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:i2E976B2F2E66D28E
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6RIS8F6RIS8_MOUSE
Collagen alpha-3(IV) chain
Col4a3
197Annotation 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>
M0QWQ2M0QWQ2_MOUSE
Collagen alpha-3(IV) chain
Col4a3
61Annotation 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>

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 conflicti1041L → R in AAD50449 (PubMed:10534397).Curated1
Sequence conflicti1594G → R in CAA57689 (PubMed:7962065).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
AF169387 mRNA Translation: AAD50449.1
AC123746 Genomic DNA No translation available.
AC138214 Genomic DNA No translation available.
Z35166 mRNA Translation: CAA84529.1
X82205 mRNA Translation: CAA57689.1
AK033387 mRNA Translation: BAC28260.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS35631.1

Protein sequence database of the Protein Information Resource

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PIRi
I48302
S49488

NCBI Reference Sequences

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RefSeqi
NP_031760.2, NM_007734.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.389135

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000113457; ENSMUSP00000109084; ENSMUSG00000079465

Database of genes from NCBI RefSeq genomes

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GeneIDi
12828

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12828

UCSC genome browser

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UCSCi
uc007brv.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
AF169387 mRNA Translation: AAD50449.1
AC123746 Genomic DNA No translation available.
AC138214 Genomic DNA No translation available.
Z35166 mRNA Translation: CAA84529.1
X82205 mRNA Translation: CAA57689.1
AK033387 mRNA Translation: BAC28260.1
CCDSiCCDS35631.1
PIRiI48302
S49488
RefSeqiNP_031760.2, NM_007734.2
UniGeneiMm.389135

3D structure databases

ProteinModelPortaliQ9QZS0
SMRiQ9QZS0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2961 Collagen type IV trimer variant 3
STRINGi10090.ENSMUSP00000109084

PTM databases

iPTMnetiQ9QZS0
PhosphoSitePlusiQ9QZS0

Proteomic databases

MaxQBiQ9QZS0
PaxDbiQ9QZS0
PeptideAtlasiQ9QZS0
PRIDEiQ9QZS0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113457; ENSMUSP00000109084; ENSMUSG00000079465
GeneIDi12828
KEGGimmu:12828
UCSCiuc007brv.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1285
MGIiMGI:104688 Col4a3

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000161675
HOGENOMiHOG000085652
HOVERGENiHBG004933
InParanoidiQ9QZS0
KOiK06237
OMAiGCNGSKG
OrthoDBiEOG091G0613
PhylomeDBiQ9QZS0
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
Col4a3 mouse

Protein Ontology

More...
PROi
PR:Q9QZS0

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000079465 Expressed in 93 organ(s), highest expression level in epithelium of lens
CleanExiMM_COL4A3
ExpressionAtlasiQ9QZS0 baseline and differential
GenevisibleiQ9QZS0 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, 19 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 nameiCO4A3_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: Q9QZS0
Secondary accession number(s): Q61430, Q61435, Q8CCD6
<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 6, 2007
Last sequence update: March 6, 2007
Last modified: December 5, 2018
This is version 137 of the entry and version 2 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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