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UniProtKB - P02466 (CO1A2_RAT)

Entry version 159 (25 May 2022)
Sequence version 3 (29 Aug 2001)
Previous versions | rss
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Protein

Collagen alpha-2(I) chain

Gene

Col1a2

Organism
Rattus norvegicus (Rat)
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 I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1187CalciumBy similarity1
Metal bindingi1189CalciumBy similarity1
Metal bindingi1190Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1192Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1195CalciumBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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-RNO-114604, GPVI-mediated activation cascade
R-RNO-1442490, Collagen degradation
R-RNO-1474244, Extracellular matrix organization
R-RNO-1650814, Collagen biosynthesis and modifying enzymes
R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures
R-RNO-202733, Cell surface interactions at the vascular wall
R-RNO-216083, Integrin cell surface interactions
R-RNO-2243919, Crosslinking of collagen fibrils
R-RNO-3000171, Non-integrin membrane-ECM interactions
R-RNO-3000178, ECM proteoglycans
R-RNO-430116, GP1b-IX-V activation signalling
R-RNO-75892, Platelet Adhesion to exposed collagen
R-RNO-76009, Platelet Aggregation (Plug Formation)
R-RNO-8874081, MET activates PTK2 signaling
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Col1a2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		621351, Col1a2

<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

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 – 221 PublicationAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000000581223 – 85N-terminal propeptideBy similarityAdd BLAST63
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000581386 – 1125Collagen alpha-2(I) chainAdd BLAST1040
PropeptideiPRO_00000058141126 – 1372C-terminal propeptideBy similarityAdd BLAST247

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 residuei23Pyrrolidone carboxylic acidBy similarity1
Modified residuei86Pyrrolidone carboxylic acid1 Publication1
Modified residuei90Allysine1 Publication1
Modified residuei1835-hydroxylysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi183O-linked (Gal...) hydroxylysine; alternateBy 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 bondi1169 ↔ 1201PROSITE-ProRule annotation
Disulfide bondi1209 ↔ 1370PROSITE-ProRule annotation
Glycosylationi1273N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1278 ↔ 1323PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

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

More...PaxDbi		P02466

PRoteomics IDEntifications database

More...PRIDEi		P02466

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P02466, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02466

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

More...PhosphoSitePlusi		P02466

<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

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. Expressed in flagella of epididymal sperm.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains.

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		249912, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3104, Collagen type I trimer

Database of interacting proteins

More...DIPi		DIP-37338N

Protein interaction database and analysis system

More...IntActi		P02466, 2 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000016423

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P02466

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

More...SMRi		P02466

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02466

<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%5Fand%5Fdomains%5Fsection">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>Domaini1139 – 1372Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

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>Regioni28 – 1135DisorderedSequence analysisAdd BLAST1108

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>Motifi783 – 785Cell attachment siteSequence analysis3
Motifi828 – 830Cell attachment siteSequence analysis3
Motifi1011 – 1013Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi58 – 78Pro residuesSequence analysisAdd BLAST21
Compositional biasi254 – 268Pro residuesSequence analysisAdd BLAST15
Compositional biasi1094 – 1108Pro residuesSequence analysisAdd BLAST15

<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

<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

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02466

Database of Orthologous Groups

More...OrthoDBi		1406711at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02466

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

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51461, NC1_FIB, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

P02466-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSFVDTRTL LLLAVTSCLA TCQSLQMGSV RKGPTGDRGP RGQRGPAGPR 
        60         70         80         90        100
GRDGVDGPVG PPGPPGAPGP PGPPGPPGLT GNFAAQYSDK GVSAGPGPMG 
       110        120        130        140        150
LMGPRGPPGA VGAPGPQGFQ GPAGEPGEPG QTGPAGSRGP AGPPGKAGED 
       160        170        180        190        200
GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP GFKGIRGHNG LDGLKGQPGA 
       210        220        230        240        250
QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR GSDGSVGPVG 
       260        270        280        290        300
PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE AGLPGLSGPV 
       310        320        330        340        350
GPPGNPGANG LTGAKGATGL PGVAGAPGLP GPRGIPGPVG AAGATGPRGL 
       360        370        380        390        400
VGEPGPAGSK GETGNKGEPG SAGAQGPPGP SGEEGKRGSP GEPGSAGPAG 
       410        420        430        440        450
PPGLRGSPGS RGLPGADGRA GVMGPPGNRG STGPAGVRGP NGDAGRPGEP 
       460        470        480        490        500
GLMGPRGLPG SPGNVGPAGK EGPVGLPGID GRPGPIGPAG PRGEAGNIGF 
       510        520        530        540        550
PGPKGPSGDP GKPGEKGHPG LAGARGAPGP DGNNGAQGPP GPQGVQGGKG 
       560        570        580        590        600
EQGPAGPPGF QGLPGPSGTA GEVGKPGERG LPGEFGLPGP AGPRGERGPP 
       610        620        630        640        650
GESGAAGPSG PIGIRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE 
       660        670        680        690        700
RGAAGIPGGK GEKGETGLRG EIGNPGRDGA RGAPGAIGAP GPAGASGDRG 
       710        720        730        740        750
EAGAAGPSGP AGPRGSPGER GEVGPAGPNG FAGPAGSAGQ PGAKGEKGTK 
       760        770        780        790        800
GPKGENGIVG PTGPVGAAGP SGPNGPPGPA GSRGDGGPPG MTGFPGAAGR 
       810        820        830        840        850
TGPPGPSGIT GPPGPPGAAG KEGIRGPRGD QGPVGRTGEI GASGPPGFAG 
       860        870        880        890        900
EKGPSGEPGT TGPPGTAGPQ GLLGAPGILG LPGSRGERGQ PGIAGALGEP 
       910        920        930        940        950
GPLGIAGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH 
       960        970        980        990       1000
KGERGYPGNI GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG 
      1010       1020       1030       1040       1050
PRGPSGPQGI RGDKGEPGDK GARGLPGLKG HNGLQGLPGL AGLHGDQGAP 
      1060       1070       1080       1090       1100
GPVGPAGPRG PAGPSGPIGK DGRSGHPGPV GPAGVRGSQG SQGPAGPPGP 
      1110       1120       1130       1140       1150
PGPPGPPGVS GGGYDFGFEG GFYRADQPRS QPSLRPKDYE VDATLKSLNN 
      1160       1170       1180       1190       1200
QIETLLTPEG SRKNPARTCR DLRLSHPEWK SDYYWIDPNQ GCTMDAIKVY 
      1210       1220       1230       1240       1250
CDFSTGETCI QAQPVNTPAK NAYSRAQANK HVWLGETING GSQFEYNAEG 
      1260       1270       1280       1290       1300
VSSKEMATQL AFMRLLANRA SQNITYHCKN SIAYLDEETG RLNKAVILQG 
      1310       1320       1330       1340       1350
SNDVELVAEG NSRFTYTVLV DGCSKKTNEW DKTVIEYKTN KPSRLPFLDI 
      1360       1370 
APLDIGGTNQ EFRVEVGPVC FK
Length:1,372
Mass (Da):129,564
Last modified:August 29, 2001 - v3
<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:iB069371A8DB20A72
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
F1LS40F1LS40_RAT
Collagen alpha-2(I) chain
Col1a2
1,372Annotation score:

Annotation score:3 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>
A0A0G2K5E8A0A0G2K5E8_RAT
Collagen alpha-2(I) chain
NEWGENE_621351 Col1a2
1,288Annotation 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 conflicti132T → P AA sequence (PubMed:4636752).Curated1
Sequence conflicti137S → P AA sequence (PubMed:4636752).Curated1
Sequence conflicti431 – 432ST → TS AA sequence (PubMed:5544653).Curated2
Sequence conflicti494E → Z AA sequence (PubMed:4435743).Curated1
Sequence conflicti497N → A AA sequence (PubMed:4435743).Curated1
Sequence conflicti825R → K AA sequence (PubMed:4763308).Curated1

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
AF121217 mRNA Translation: AAD41775.1

NCBI Reference Sequences

More...RefSeqi		NP_445808.1, NM_053356.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		84352

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:84352

UCSC genome browser

More...UCSCi		RGD:621351, rat

<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
AF121217 mRNA Translation: AAD41775.1
RefSeqiNP_445808.1, NM_053356.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HQVfiber diffraction5.16B86-1113[»]
3HR2fiber diffraction5.16B86-1113[»]
AlphaFoldDBiP02466
SMRiP02466
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi249912, 2 interactors
ComplexPortaliCPX-3104, Collagen type I trimer
DIPiDIP-37338N
IntActiP02466, 2 interactors
STRINGi10116.ENSRNOP00000016423

PTM databases

GlyGeniP02466, 2 sites
iPTMnetiP02466
PhosphoSitePlusiP02466

Proteomic databases

PaxDbiP02466
PRIDEiP02466

Genome annotation databases

GeneIDi84352
KEGGirno:84352
UCSCiRGD:621351, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1278
RGDi621351, Col1a2

Phylogenomic databases

eggNOGiKOG3544, Eukaryota
InParanoidiP02466
OrthoDBi1406711at2759
PhylomeDBiP02466

Enzyme and pathway databases

ReactomeiR-RNO-114604, GPVI-mediated activation cascade
R-RNO-1442490, Collagen degradation
R-RNO-1474244, Extracellular matrix organization
R-RNO-1650814, Collagen biosynthesis and modifying enzymes
R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures
R-RNO-202733, Cell surface interactions at the vascular wall
R-RNO-216083, Integrin cell surface interactions
R-RNO-2243919, Crosslinking of collagen fibrils
R-RNO-3000171, Non-integrin membrane-ECM interactions
R-RNO-3000178, ECM proteoglycans
R-RNO-430116, GP1b-IX-V activation signalling
R-RNO-75892, Platelet Adhesion to exposed collagen
R-RNO-76009, Platelet Aggregation (Plug Formation)
R-RNO-8874081, MET activates PTK2 signaling
R-RNO-8948216, Collagen chain trimerization

Miscellaneous databases

EvolutionaryTraceiP02466

Protein Ontology

More...PROi		PR:P02466

Family and domain databases

InterProiView protein in InterPro
IPR008160, Collagen
IPR000885, Fib_collagen_C
PfamiView protein in Pfam
PF01410, COLFI, 1 hit
PF01391, Collagen, 7 hits
SMARTiView protein in SMART
SM00038, COLFI, 1 hit
PROSITEiView protein in PROSITE
PS51461, NC1_FIB, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO1A2_RAT
<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: P02466
Secondary accession number(s): Q9R1E8
<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%5Fand%5Fisoforms">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: August 29, 2001
Last modified: May 25, 2022
This is version 159 of the entry and version 3 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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