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Entry version 169 (08 May 2019)
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 ‘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 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

GO - Biological processi

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

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-2214320 Anchoring fibril formation
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_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(I) chain
Alternative name(s):
Alpha-1 type I collagen
<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:Col1a1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 10

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

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 – 22Sequence analysisAdd BLAST22
<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_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.<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_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>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_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

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

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 10 organ(s), highest expression level in skeletal muscle tissue

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_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

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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MRC2Q9UBG02EBI-915744,EBI-1104992From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248045, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3104 Collagen type I trimer

Database of interacting proteins

More...
DIPi
DIP-36887N

Protein interaction database and analysis system

More...
IntActi
P02454, 4 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

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HQVfiber diffraction5.16A/C152-1207[»]
3HR2fiber diffraction5.16A/C152-1207[»]

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

More...
SMRi
P02454

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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_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>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
ENOG410XNMM LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156584

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000085654

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02454

KEGG Orthology (KO)

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KOi
K06236

Identification of Orthologs from Complete Genome Data

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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

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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

ProDom; a protein domain database

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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

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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>Sequencei

<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.

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

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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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HQVfiber diffraction5.16A/C152-1207[»]
3HR2fiber diffraction5.16A/C152-1207[»]
SMRiP02454
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248045, 1 interactor
ComplexPortaliCPX-3104 Collagen type I trimer
DIPiDIP-36887N
IntActiP02454, 4 interactors
STRINGi10116.ENSRNOP00000005311

PTM databases

iPTMnetiP02454
PhosphoSitePlusiP02454

Proteomic databases

jPOSTiP02454
PaxDbiP02454
PRIDEiP02454

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
ENOG410XNMM LUCA
GeneTreeiENSGT00940000156584
HOGENOMiHOG000085654
InParanoidiP02454
KOiK06236
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-2214320 Anchoring fibril formation
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 10 organ(s), highest expression level in skeletal muscle tissue
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
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 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_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: September 22, 2009
Last modified: May 8, 2019
This is version 169 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, Complete proteome, 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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