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UniProtKB - P02454 (CO1A1_RAT)

Entry version 180 (07 Apr 2021)
Sequence version 5 (22 Sep 2009)
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Protein

Collagen alpha-1(I) chain

Gene

Col1a1

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 bindingi1266CalciumBy similarity1
Metal bindingi1268CalciumBy similarity1
Metal bindingi1269Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1271Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1274CalciumBy 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-1(I) chain
Alternative name(s):
Alpha-1 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:Col1a1
<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: Chromosome 10
  • UP000234681 Componentsi: Chromosome 10, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...RGDi		61817, Col1a1

<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 – 22Sequence analysisAdd 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_000004335823 – 151N-terminal propeptide1 PublicationAdd BLAST129
<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_0000043359152 – 1207Collagen alpha-1(I) chainAdd BLAST1056
PropeptideiPRO_00000433601208 – 1453C-terminal propeptideBy similarityAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi56N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei152Pyrrolidone carboxylic acid1 Publication1
Modified residuei160Allysine1 Publication1
Modified residuei161PhosphoserineCombined sources1
Modified residuei1794-hydroxyproline1 Publication1
Modified residuei1824-hydroxyproline1 Publication1
Modified residuei1854-hydroxyproline1 Publication1
Modified residuei1944-hydroxyproline1 Publication1
Modified residuei1974-hydroxyproline1 Publication1
Modified residuei2004-hydroxyproline1 Publication1
Modified residuei2154-hydroxyprolineBy similarity1
Modified residuei2304-hydroxyprolineBy similarity1
Modified residuei2364-hydroxyprolineBy similarity1
Modified residuei2454-hydroxyprolineBy similarity1
Modified residuei2514-hydroxyprolineBy similarity1
Modified residuei2545-hydroxylysine; alternate1 Publication1
Glycosylationi254O-linked (Gal...) hydroxylysine; alternate1 Publication1
Modified residuei260PhosphoserineCombined sources1
Modified residuei2784-hydroxyprolineBy similarity1
Modified residuei2814-hydroxyprolineBy similarity1
Modified residuei2874-hydroxyprolineBy similarity1
Modified residuei2964-hydroxyprolineBy similarity1
Modified residuei3024-hydroxyprolineBy similarity1
Modified residuei3234-hydroxyprolineBy similarity1
Modified residuei3324-hydroxyprolineBy similarity1
Modified residuei3354-hydroxyprolineBy similarity1
Modified residuei3624-hydroxyprolineBy similarity1
Modified residuei3654-hydroxyprolineBy similarity1
Modified residuei3774-hydroxyprolineBy similarity1
Modified residuei3834-hydroxyprolineBy similarity1
Modified residuei3924-hydroxyprolineBy similarity1
Modified residuei3984-hydroxyprolineBy similarity1
Modified residuei4014-hydroxyprolineBy similarity1
Modified residuei4164-hydroxyprolineBy similarity1
Modified residuei4195-hydroxylysineBy similarity1
Modified residuei4254-hydroxyprolineBy similarity1
Modified residuei4284-hydroxyprolineBy similarity1
Modified residuei4404-hydroxyprolineBy similarity1
Modified residuei4494-hydroxyprolineBy similarity1
Modified residuei4644-hydroxyprolineBy similarity1
Modified residuei4704-hydroxyprolineBy similarity1
Modified residuei4794-hydroxyprolineBy similarity1
Modified residuei4854-hydroxyprolineBy similarity1
Modified residuei4945-hydroxylysineBy similarity1
Modified residuei5034-hydroxyprolineBy similarity1
Modified residuei5124-hydroxyprolineBy similarity1
Modified residuei5184-hydroxyprolineBy similarity1
Modified residuei5244-hydroxyprolineBy similarity1
Modified residuei5334-hydroxyprolineBy similarity1
Modified residuei5364-hydroxyprolineBy similarity1
Modified residuei5454-hydroxyprolineBy similarity1
Modified residuei5544-hydroxyprolineBy similarity1
Modified residuei5604-hydroxyprolineBy similarity1
Modified residuei5724-hydroxyprolineBy similarity1
Modified residuei5814-hydroxyprolineBy similarity1
Modified residuei5904-hydroxyprolineBy similarity1
Modified residuei5934-hydroxyprolineBy similarity1
Modified residuei6114-hydroxyprolineBy similarity1
Modified residuei6294-hydroxyprolineBy similarity1
Modified residuei6354-hydroxyprolineBy similarity1
Modified residuei6414-hydroxyprolineBy similarity1
Modified residuei6474-hydroxyprolineBy similarity1
Modified residuei6534-hydroxyprolineBy similarity1
Modified residuei6594-hydroxyprolineBy similarity1
Modified residuei6714-hydroxyprolineBy similarity1
Modified residuei6804-hydroxyprolineBy similarity1
Modified residuei6924-hydroxyprolineBy similarity1
Modified residuei7044-hydroxyprolineBy similarity1
Modified residuei7074-hydroxyprolineBy similarity1
Modified residuei7134-hydroxyprolineBy similarity1
Modified residuei7194-hydroxyprolineBy similarity1
Modified residuei7284-hydroxyprolineBy similarity1
Modified residuei7405-hydroxylysineBy similarity1
Modified residuei7464-hydroxyprolineBy similarity1
Modified residuei7614-hydroxyprolineBy similarity1
Modified residuei7674-hydroxyprolineBy similarity1
Modified residuei776PhosphoserineCombined sources1
Modified residuei7884-hydroxyprolineBy similarity1
Modified residuei7944-hydroxyprolineBy similarity1
Modified residuei7974-hydroxyprolineBy similarity1
Modified residuei8064-hydroxyprolineBy similarity1
Modified residuei8124-hydroxyprolineBy similarity1
Modified residuei8304-hydroxyprolineBy similarity1
Modified residuei8394-hydroxyprolineBy similarity1
Modified residuei8484-hydroxyprolineBy similarity1
Modified residuei8515-hydroxylysineBy similarity1
Modified residuei8604-hydroxyprolineBy similarity1
Modified residuei8664-hydroxyprolineBy similarity1
Modified residuei8743-hydroxyprolineBy similarity1
Modified residuei8754-hydroxyprolineBy similarity1
Modified residuei8844-hydroxyprolineBy similarity1
Modified residuei8874-hydroxyprolineBy similarity1
Modified residuei9084-hydroxyprolineBy similarity1
Modified residuei9174-hydroxyprolineBy similarity1
Modified residuei9264-hydroxyprolineBy similarity1
Modified residuei9354-hydroxyprolineBy similarity1
Modified residuei9534-hydroxyprolineBy similarity1
Modified residuei9624-hydroxyprolineBy similarity1
Modified residuei9654-hydroxyprolineBy similarity1
Modified residuei9714-hydroxyprolineBy similarity1
Modified residuei9864-hydroxyprolineBy similarity1
Modified residuei9924-hydroxyprolineBy similarity1
Modified residuei9984-hydroxyprolineBy similarity1
Modified residuei10074-hydroxyprolineBy similarity1
Modified residuei10134-hydroxyprolineBy similarity1
Modified residuei10225-hydroxylysineBy similarity1
Modified residuei10344-hydroxyprolineBy similarity1
Modified residuei10374-hydroxyprolineBy similarity1
Modified residuei10404-hydroxyprolineBy similarity1
Modified residuei10855-hydroxylysineBy similarity1
Modified residuei10975-hydroxylysine; alternateBy similarity1
Glycosylationi1097O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei11094-hydroxyprolineBy similarity1
Modified residuei11124-hydroxyprolineBy similarity1
Modified residuei11154-hydroxyprolineBy similarity1
Modified residuei11334-hydroxyprolineBy similarity1
Modified residuei11484-hydroxyprolineBy similarity1
Modified residuei11533-hydroxyprolineBy similarity1
Modified residuei11544-hydroxyprolineBy similarity1
Modified residuei11683-hydroxyprolineBy similarity1
Modified residuei11694-hydroxyprolineBy similarity1
Modified residuei11713-hydroxyprolineBy similarity1
Modified residuei11724-hydroxyprolineBy similarity1
Modified residuei11743-hydroxyprolineBy similarity1
Modified residuei11754-hydroxyprolineBy similarity1
Modified residuei11784-hydroxyprolineBy similarity1
Modified residuei11814-hydroxyprolineBy similarity1
Modified residuei1197AllysineBy 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 bondi1248 ↔ 1280PROSITE-ProRule annotation
Disulfide bondi1254Interchain (with C-1271)PROSITE-ProRule annotation
Disulfide bondi1271Interchain (with C-1254)PROSITE-ProRule annotation
Disulfide bondi1288 ↔ 1451PROSITE-ProRule annotation
Glycosylationi1354N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1359 ↔ 1404PROSITE-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

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication
Contains 3-hydroxyproline 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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02454

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

More...PaxDbi		P02454

PRoteomics IDEntifications database

More...PRIDEi		P02454

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P02454, 4 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02454

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

More...PhosphoSitePlusi		P02454

<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.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000003897, Expressed in skeletal muscle tissue and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02454, RN

<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.

Interacts with MRC2 (PubMed:15817460).

Interacts with TRAM2.

Interacts with MFAP4 in a Ca (2+)-dependent manner.

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		248045, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-36887N

Protein interaction database and analysis system

More...IntActi		P02454, 5 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000005311

<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

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

More...SMRi		P02454

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		P02454

<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>Domaini29 – 87VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1218 – 1453Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST236

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>Regioni152 – 167Nonhelical region (N-terminal)Add BLAST16
Regioni168 – 1181Triple-helical regionAdd BLAST1014
Regioni1176 – 1186Major antigenic determinant (of neutral salt-extracted rat skin collagen)Add BLAST11
Regioni1182 – 1207Nonhelical region (C-terminal)Add BLAST26

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>Motifi734 – 736Cell attachment siteSequence analysis3
Motifi1082 – 1084Cell 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

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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156584

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001074_2_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02454

Identification of Orthologs from Complete Genome Data

More...OMAi		THGQEDI

Database of Orthologous Groups

More...OrthoDBi		337699at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02454

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, 12 hits
PF00093, VWC, 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%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>Sequencei

<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.

P02454-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL 
        60         70         80         90        100
ICICHNGTAV CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV 
       110        120        130        140        150
EGPKGDPGPQ GPRGPVGPPG QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA 
       160        170        180        190        200
SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP 
       210        220        230        240        250
GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL 
       260        270        280        290        300
PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 
       310        320        330        340        350
RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR 
       360        370        380        390        400
GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF 
       410        420        430        440        450
PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG 
       460        470        480        490        500
PAGEEGKRGA RGEPGPSGLP GPPGERGGPG SRGFPGADGV AGPKGPAGER 
       510        520        530        540        550
GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ 
       560        570        580        590        600
DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG 
       610        620        630        640        650
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ 
       660        670        680        690        700
GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD 
       710        720        730        740        750
TGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGSPGKDG 
       760        770        780        790        800
VRGLTGPIGP PGPAGAPGDK GETGPSGPAG PTGARGAPGD RGEPGPPGPA 
       810        820        830        840        850
GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG PIGNVGAPGP 
       860        870        880        890        900
KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG 
       910        920        930        940        950
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV 
       960        970        980        990       1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE 
      1010       1020       1030       1040       1050
SGREGSPGAE GSPGRDGAPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG 
      1060       1070       1080       1090       1100
KNGDRGETGP AGPAGPIGPA GARGPAGPQG PRGDKGETGE QGDRGIKGHR 
      1110       1120       1130       1140       1150
GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP 
      1160       1170       1180       1190       1200
IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD 
      1210       1220       1230       1240       1250
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD 
      1260       1270       1280       1290       1300
LKMCHSDWKS GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN 
      1310       1320       1330       1340       1350
WYISPNPKEK KHVWFGESMT DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE 
      1360       1370       1380       1390       1400
ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ GSNEIELRGE GNSRFTYSTL 
      1410       1420       1430       1440       1450
VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD QEFGMDIGPA 

CFV
Length:1,453
Mass (Da):137,953
Last modified:September 22, 2009 - v5
<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:iBCDDC40C3167AE59
GO

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 conflicti143P → L in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti202A → G in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti209R → P in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti232E → Q AA sequence (PubMed:4327399).Curated1
Sequence conflicti268D → N AA sequence (PubMed:5411206).Curated1
Sequence conflicti286A → T in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti307S → T in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti313N → D AA sequence (PubMed:4335087).Curated1
Sequence conflicti421N → T in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti497A → S in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti773T → A in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti794P → A in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti958E → K in CAB01633 (PubMed:10065941).Curated1
Sequence conflicti1111S → P AA sequence (PubMed:4126850).Curated1
Sequence conflicti1163S → A AA sequence (PubMed:4126850).Curated1
Sequence conflicti1166A → S AA sequence (PubMed:4126850).Curated1
Sequence conflicti1187F → L AA sequence (PubMed:4636751).Curated1
Sequence conflicti1190L → F AA sequence (PubMed:4636751).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
Z78279 mRNA Translation: CAB01633.1
CH473948 Genomic DNA Translation: EDM05727.1
BC133728 mRNA Translation: AAI33729.1
M11432 mRNA Translation: AAA40832.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...PIRi		A90559, CGRT1S

NCBI Reference Sequences

More...RefSeqi		NP_445756.1, NM_053304.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897

Database of genes from NCBI RefSeq genomes

More...GeneIDi		29393

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:29393

UCSC genome browser

More...UCSCi		RGD:61817, 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
Z78279 mRNA Translation: CAB01633.1
CH473948 Genomic DNA Translation: EDM05727.1
BC133728 mRNA Translation: AAI33729.1
M11432 mRNA Translation: AAA40832.1 Sequence problems.
PIRiA90559, CGRT1S
RefSeqiNP_445756.1, NM_053304.1

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 diffraction5.16A/C152-1207[»]
3HR2fiber diffraction5.16A/C152-1207[»]
SMRiP02454
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi248045, 3 interactors
ComplexPortaliCPX-3104, Collagen type I trimer
DIPiDIP-36887N
IntActiP02454, 5 interactors
STRINGi10116.ENSRNOP00000005311

PTM databases

GlyGeniP02454, 4 sites
iPTMnetiP02454
PhosphoSitePlusiP02454

Proteomic databases

jPOSTiP02454
PaxDbiP02454
PRIDEiP02454

Genome annotation databases

EnsembliENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897
GeneIDi29393
KEGGirno:29393
UCSCiRGD:61817, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1277
RGDi61817, Col1a1

Phylogenomic databases

eggNOGiKOG3544, Eukaryota
GeneTreeiENSGT00940000156584
HOGENOMiCLU_001074_2_3_1
InParanoidiP02454
OMAiTHGQEDI
OrthoDBi337699at2759
PhylomeDBiP02454
TreeFamiTF344135

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

EvolutionaryTraceiP02454

Protein Ontology

More...PROi		PR:P02454

Gene expression databases

BgeeiENSRNOG00000003897, Expressed in skeletal muscle tissue and 21 other tissues
GenevisibleiP02454, RN

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, 12 hits
PF00093, VWC, 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...

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 nameiCO1A1_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: P02454
Secondary accession number(s): A3KNA1, P02455, Q63079
<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: September 22, 2009
Last modified: April 7, 2021
This is version 180 of the entry and version 5 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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