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UniProtKB - P02459 (CO2A1_BOVIN)

Entry version 158 (13 Feb 2019)
Sequence version 4 (30 Nov 2010)
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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Bos taurus (Bovine)
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 II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1301CalciumBy similarity1
Metal bindingi1303CalciumBy similarity1
Metal bindingi1304Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1306Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1309CalciumBy similarity1

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-BTA-1442490 Collagen degradation
R-BTA-1474244 Extracellular matrix organization
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-186797 Signaling by PDGF
R-BTA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-216083 Integrin cell surface interactions
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-3000178 ECM proteoglycans
R-BTA-419037 NCAM1 interactions
R-BTA-8874081 MET activates PTK2 signaling
R-BTA-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(II) chainBy similarity
Alternative name(s):
Alpha-1 type II collagenBy similarity
<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:COL2A1By similarity
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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 5

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:27564 COL2A1

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

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<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_000040121026 – 181N-terminal propeptideBy similarityAdd BLAST156
<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_0000005725182 – 1487Collagen alpha-1(II) chainAdd BLAST1306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1905-hydroxylysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi190O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei212Hydroxyproline1 Publication1
Modified residuei218Hydroxyproline1 Publication1
Modified residuei230Hydroxyproline1 Publication1
Modified residuei233Hydroxyproline1 Publication1
Modified residuei245Hydroxyproline1 Publication1
Modified residuei248Hydroxyproline1 Publication1
Modified residuei251Hydroxyproline1 Publication1
Modified residuei260Hydroxyproline1 Publication1
Modified residuei269Hydroxyproline1 Publication1
Modified residuei278Hydroxyproline1 Publication1
Modified residuei281Hydroxyproline1 Publication1
Modified residuei284Hydroxyproline1 Publication1
Modified residuei2875-hydroxylysine1 Publication1
Glycosylationi287O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei293Hydroxyproline1 Publication1
Modified residuei2995-hydroxylysine1 Publication1
Glycosylationi299O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei305Hydroxyproline1 Publication1
Modified residuei3085-hydroxylysine1 Publication1
Glycosylationi308O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei314Hydroxyproline1 Publication1
Modified residuei320Hydroxyproline1 Publication1
Modified residuei329Hydroxyproline2 Publications1
Modified residuei350Hydroxyproline3 Publications1
Modified residuei356Hydroxyproline3 Publications1
Modified residuei365Hydroxyproline1 Publication1
Modified residuei368Hydroxyproline1 Publication1
Modified residuei371Hydroxyproline1 Publication1
Modified residuei3745-hydroxylysine1 Publication1
Glycosylationi374O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei395Hydroxyproline1 Publication1
Modified residuei398Hydroxyproline1 Publication1
Modified residuei401Hydroxyproline1 Publication1
Modified residuei410Hydroxyproline1 Publication1
Modified residuei416Hydroxyproline1 Publication1
Modified residuei4195-hydroxylysine1 Publication1
Modified residuei425Hydroxyproline1 Publication1
Modified residuei431Hydroxyproline1 Publication1
Modified residuei434Hydroxyproline1 Publication1
Modified residuei440Hydroxyproline1 Publication1
Modified residuei4525-hydroxylysine1 Publication1
Modified residuei458Hydroxyproline1 Publication1
Modified residuei4645-hydroxylysine1 Publication1
Modified residuei4705-hydroxylysine1 Publication1
Modified residuei473Hydroxyproline1 Publication1
Modified residuei482Hydroxyproline1 Publication1
Modified residuei497Hydroxyproline1 Publication1
Modified residuei506Hydroxyproline1 Publication1
Modified residuei512Hydroxyproline1 Publication1
Modified residuei518Hydroxyproline1 Publication1
Modified residuei5275-hydroxylysine1 Publication1
Modified residuei530Hydroxyproline1 Publication1
Modified residuei5425-hydroxylysine1 Publication1
Modified residuei551Hydroxyproline1 Publication1
Modified residuei557Hydroxyproline1 Publication1
Modified residuei566Hydroxyproline1 Publication1
Modified residuei581Hydroxyproline1 Publication1
Modified residuei587Hydroxyproline1 Publication1
Modified residuei590Hydroxyproline1 Publication1
Modified residuei599Hydroxyproline1 Publication1
Modified residuei605Hydroxyproline1 Publication1
Modified residuei6085-hydroxylysine1 Publication1
Glycosylationi608O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei614Hydroxyproline1 Publication1
Modified residuei6205-hydroxylysine1 Publication1
Glycosylationi620O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei623Hydroxyproline1 Publication1
Modified residuei626Hydroxyproline1 Publication1
Modified residuei632Hydroxyproline1 Publication1
Modified residuei644Hydroxyproline1 Publication1
Modified residuei659Hydroxyproline1 Publication1
Modified residuei668Hydroxyproline1 Publication1
Modified residuei6703-hydroxyprolineBy similarity1
Modified residuei671Hydroxyproline1 Publication1
Modified residuei674Hydroxyproline1 Publication1
Modified residuei9073-hydroxyprolineBy similarity1
Modified residuei9084-hydroxyprolineBy similarity1
Modified residuei9144-hydroxyprolineBy similarity1
Modified residuei9204-hydroxyprolineBy similarity1
Modified residuei11305-hydroxylysineBy similarity1
Glycosylationi1130O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei11443-hydroxyprolineBy similarity1
Modified residuei11814-hydroxyprolineBy similarity1
Modified residuei11863-hydroxyprolineBy similarity1
Modified residuei11874-hydroxyprolineBy similarity1
Modified residuei12013-hydroxyprolineBy similarity1
Modified residuei12024-hydroxyprolineBy similarity1
Modified residuei12054-hydroxyprolineBy similarity1
Modified residuei12073-hydroxyprolineBy similarity1
Modified residuei12084-hydroxyprolineBy similarity1
Modified residuei12114-hydroxyprolineBy similarity1
Modified residuei12133-hydroxyprolineBy similarity1
Modified residuei12144-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 bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1388N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

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

Probably 3-hydroxylated on prolines by LEPREL1 (By similarity). Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.By similarity4 Publications
O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.3 Publications
Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains.4 Publications
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.By similarity
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.By similarity
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.3 Publications

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>Sitei181 – 182Cleavage; by procollagen N-endopeptidaseBy similarity2
Sitei1241 – 1242Cleavage; by procollagen C-endopeptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

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

More...PaxDbi		P02459

PRoteomics IDEntifications database

More...PRIDEi		P02459

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P02459

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000013155 Expressed in 6 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P02459 baseline

<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

Homotrimers of alpha 1(II) chains.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3105 Collagen type II trimer
CPX-3108 Collagen type XI trimer variant 1

Protein interaction database and analysis system

More...IntActi		P02459, 1 interactor

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000017505

<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		P02459

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

More...SMRi		P02459

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>Domaini32 – 90VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1253 – 1487Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

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>Regioni201 – 1214Triple-helical regionBy similarityAdd BLAST1014
Regioni1215 – 1241Nonhelical region (C-terminal)By similarityAdd BLAST27

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

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

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

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3544 Eukaryota
ENOG410XNMM LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155224

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000085654

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004933

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02459

KEGG Orthology (KO)

More...KOi		K19719

Identification of Orthologs from Complete Genome Data

More...OMAi		VQKAGSC

Database of Orthologous Groups

More...OrthoDBi		337699at2759

TreeFam database of animal gene trees

More...TreeFami		TF344135

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 7 hits
PF00093 VWC, 1 hit

ProDom; a protein domain database

More...ProDomi		View protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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 1 potential isoform that is computationally mapped.Show allAlign All

P02459-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE 
        60         70         80         90        100
PCRICVCDTG TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP 
       110        120        130        140        150
GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG 
       160        170        180        190        200
RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQMGVMQ 
       210        220        230        240        250
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK 
       260        270        280        290        300
PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 
       310        320        330        340        350
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP 
       360        370        380        390        400
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS 
       410        420        430        440        450
PGPAGAAGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG 
       460        470        480        490        500
PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGA 
       510        520        530        540        550
GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR 
       560        570        580        590        600
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 
       610        620        630        640        650
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA 
       660        670        680        690        700
GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE 
       710        720        730        740        750
RGFPGERGSP GSQGLQGARG LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG 
       760        770        780        790        800
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN 
       810        820        830        840        850
GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE 
       860        870        880        890        900
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 
       910        920        930        940        950
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA 
       960        970        980        990       1000
GPPGEKGEPG DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP 
      1010       1020       1030       1040       1050
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG 
      1060       1070       1080       1090       1100
AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PIGKQGDRGE AGAQGPMGPA 
      1110       1120       1130       1140       1150
GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG LPGPPGPSGD 
      1160       1170       1180       1190       1200
QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 
      1210       1220       1230       1240       1250
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ 
      1260       1270       1280       1290       1300
HDAEVDATLK SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI 
      1310       1320       1330       1340       1350
DPNQGCTLDA MKVFCNMETG ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG 
      1360       1370       1380       1390       1400
ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL 
      1410       1420       1430       1440       1450
DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK HTGKWGKTMI 
      1460       1470       1480 
EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
Length:1,487
Mass (Da):141,828
Last modified:November 30, 2010 - 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:iF99891F6FD1E47F9
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1MSR8F1MSR8_BOVIN
Collagen alpha-1(II) chain
COL2A1
1,418Annotation 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 conflicti202P → V AA sequence (PubMed:782511).Curated1
Sequence conflicti380T → Q AA sequence (PubMed:2714276).Curated1
Sequence conflicti400S → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti412T → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti436P → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti443Q → T AA sequence (PubMed:2714276).Curated1
Sequence conflicti446T → S AA sequence (PubMed:2714276).Curated1
Sequence conflicti476A → T in AAA30436 (PubMed:7511638).Curated1
Sequence conflicti478P → V AA sequence (PubMed:2714276).Curated1
Sequence conflicti514N → S AA sequence (PubMed:2714276).Curated1
Sequence conflicti518P → S in AAA30436 (PubMed:7511638).Curated1
Sequence conflicti523L → I AA sequence (PubMed:2714276).Curated1
Sequence conflicti529A → P AA sequence (PubMed:2714276).Curated1
Sequence conflicti535 – 539PSGLA → SPGAV AA sequence (PubMed:2714276).Curated5
Sequence conflicti544 – 548ANGDP → SPGEA AA sequence (PubMed:2714276).Curated5
Sequence conflicti554P → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti560R → K AA sequence (PubMed:2714276).Curated1
Sequence conflicti677G → P AA sequence (PubMed:4857180).Curated1
Sequence conflicti712S → A in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti718A → P in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti734A → S in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti1372N → D in CAA26269 (PubMed:2582365).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti349Q → L1 Publication1

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
AAFC03017082 Genomic DNA No translation available.
AAFC03017085 Genomic DNA No translation available.
AAFC03056593 Genomic DNA No translation available.
L28918 mRNA Translation: AAA30436.2
AF138883 mRNA Translation: AAD42346.1
AF138957 mRNA Translation: AAD42347.1
X02420 mRNA Translation: CAA26269.1

Protein sequence database of the Protein Information Resource

More...PIRi		A90369 CGBO6C
I45876

NCBI Reference Sequences

More...RefSeqi		NP_001001135.2, NM_001001135.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Bt.21390

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155

Database of genes from NCBI RefSeq genomes

More...GeneIDi		407142

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:407142

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
AAFC03017082 Genomic DNA No translation available.
AAFC03017085 Genomic DNA No translation available.
AAFC03056593 Genomic DNA No translation available.
L28918 mRNA Translation: AAA30436.2
AF138883 mRNA Translation: AAD42346.1
AF138957 mRNA Translation: AAD42347.1
X02420 mRNA Translation: CAA26269.1
PIRiA90369 CGBO6C
I45876
RefSeqiNP_001001135.2, NM_001001135.3
UniGeneiBt.21390

3D structure databases

ProteinModelPortaliP02459
SMRiP02459
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-3105 Collagen type II trimer
CPX-3108 Collagen type XI trimer variant 1
IntActiP02459, 1 interactor
STRINGi9913.ENSBTAP00000017505

Proteomic databases

PaxDbiP02459
PRIDEiP02459

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155
GeneIDi407142
KEGGibta:407142

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1280
VGNCiVGNC:27564 COL2A1

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000155224
HOGENOMiHOG000085654
HOVERGENiHBG004933
InParanoidiP02459
KOiK19719
OMAiVQKAGSC
OrthoDBi337699at2759
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-BTA-1442490 Collagen degradation
R-BTA-1474244 Extracellular matrix organization
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-186797 Signaling by PDGF
R-BTA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-216083 Integrin cell surface interactions
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-3000178 ECM proteoglycans
R-BTA-419037 NCAM1 interactions
R-BTA-8874081 MET activates PTK2 signaling
R-BTA-8948216 Collagen chain trimerization

Miscellaneous databases

PMAP-CutDBiP02459

Gene expression databases

BgeeiENSBTAG00000013155 Expressed in 6 organ(s), highest expression level in testis
ExpressionAtlasiP02459 baseline

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 7 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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 nameiCO2A1_BOVIN
<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: P02459
Secondary accession number(s): Q28070, Q9XT24, Q9XT25
<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: November 30, 2010
Last modified: February 13, 2019
This is version 158 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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