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Entry version 151 (08 May 2019)
Sequence version 3 (30 May 2006)
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Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Type 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 bindingi1276CalciumBy similarity1
Metal bindingi1278CalciumBy similarity1
Metal bindingi1279Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1281Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1284CalciumBy 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-BTA-114604 GPVI-mediated activation cascade
R-BTA-1442490 Collagen degradation
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-202733 Cell surface interactions at the vascular wall
R-BTA-216083 Integrin cell surface interactions
R-BTA-2214320 Anchoring fibril formation
R-BTA-2243919 Crosslinking of collagen fibrils
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-3000178 ECM proteoglycans
R-BTA-430116 GP1b-IX-V activation signalling
R-BTA-75892 Platelet Adhesion to exposed collagen
R-BTA-8948216 Collagen chain trimerization

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-1(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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:27560 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_000023680423 – 161N-terminal propeptide1 PublicationAdd BLAST139
<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_0000059396162 – 1217Collagen alpha-1(I) chain1 PublicationAdd BLAST1056
PropeptideiPRO_00002368051218 – 1463C-terminal propeptide1 PublicationAdd BLAST246

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 residuei162Pyrrolidone carboxylic acid1 Publication1
Modified residuei170Allysine1 Publication1
Modified residuei171PhosphoserineBy similarity1
Modified residuei1894-hydroxyprolineBy similarity1
Modified residuei1924-hydroxyprolineBy similarity1
Modified residuei1954-hydroxyprolineBy similarity1
Modified residuei2044-hydroxyprolineBy similarity1
Modified residuei2074-hydroxyprolineBy similarity1
Modified residuei2104-hydroxyprolineBy similarity1
Modified residuei2254-hydroxyprolineBy similarity1
Modified residuei2404-hydroxyprolineBy similarity1
Modified residuei2464-hydroxyprolineBy similarity1
Modified residuei2554-hydroxyprolineBy similarity1
Modified residuei2614-hydroxyprolineBy similarity1
Modified residuei2645-hydroxylysine; alternate1 Publication1
<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>Glycosylationi264O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei270PhosphoserineBy similarity1
Modified residuei2765-hydroxylysineSequence analysis1
Modified residuei2855-hydroxylysineSequence analysis1
Modified residuei2884-hydroxyprolineBy similarity1
Modified residuei2914-hydroxyprolineBy similarity1
Modified residuei2974-hydroxyprolineBy similarity1
Modified residuei3064-hydroxyprolineBy similarity1
Modified residuei3124-hydroxyprolineBy similarity1
Modified residuei3334-hydroxyprolineBy similarity1
Modified residuei3424-hydroxyprolineBy similarity1
Modified residuei3454-hydroxyprolineBy similarity1
Modified residuei3724-hydroxyprolineBy similarity1
Modified residuei3754-hydroxyprolineBy similarity1
Modified residuei3874-hydroxyprolineBy similarity1
Modified residuei3934-hydroxyprolineBy similarity1
Modified residuei4024-hydroxyprolineBy similarity1
Modified residuei4084-hydroxyprolineBy similarity1
Modified residuei4114-hydroxyprolineBy similarity1
Modified residuei4264-hydroxyprolineBy similarity1
Modified residuei4295-hydroxylysineBy similarity1
Modified residuei4354-hydroxyprolineBy similarity1
Modified residuei4384-hydroxyprolineBy similarity1
Modified residuei4504-hydroxyprolineBy similarity1
Modified residuei4594-hydroxyprolineBy similarity1
Modified residuei4744-hydroxyprolineBy similarity1
Modified residuei4804-hydroxyprolineBy similarity1
Modified residuei4894-hydroxyprolineBy similarity1
Modified residuei4954-hydroxyprolineBy similarity1
Modified residuei5045-hydroxylysineBy similarity1
Modified residuei5134-hydroxyprolineBy similarity1
Modified residuei5224-hydroxyprolineBy similarity1
Modified residuei5284-hydroxyprolineBy similarity1
Modified residuei5344-hydroxyprolineBy similarity1
Modified residuei5434-hydroxyprolineBy similarity1
Modified residuei5464-hydroxyprolineBy similarity1
Modified residuei5554-hydroxyprolineBy similarity1
Modified residuei5644-hydroxyprolineBy similarity1
Modified residuei5704-hydroxyprolineBy similarity1
Modified residuei5824-hydroxyprolineBy similarity1
Modified residuei5914-hydroxyprolineBy similarity1
Modified residuei6004-hydroxyprolineBy similarity1
Modified residuei6034-hydroxyprolineBy similarity1
Modified residuei6214-hydroxyprolineBy similarity1
Modified residuei6394-hydroxyprolineBy similarity1
Modified residuei6454-hydroxyprolineBy similarity1
Modified residuei6514-hydroxyprolineBy similarity1
Modified residuei6574-hydroxyprolineBy similarity1
Modified residuei6634-hydroxyprolineBy similarity1
Modified residuei6694-hydroxyprolineBy similarity1
Modified residuei6814-hydroxyprolineBy similarity1
Modified residuei6904-hydroxyprolineBy similarity1
Modified residuei7024-hydroxyprolineBy similarity1
Modified residuei7144-hydroxyprolineBy similarity1
Modified residuei7174-hydroxyprolineBy similarity1
Modified residuei7234-hydroxyprolineBy similarity1
Modified residuei7294-hydroxyprolineBy similarity1
Modified residuei7384-hydroxyprolineBy similarity1
Modified residuei7505-hydroxylysineBy similarity1
Modified residuei7564-hydroxyprolineBy similarity1
Modified residuei7714-hydroxyprolineBy similarity1
Modified residuei7774-hydroxyprolineBy similarity1
Modified residuei786PhosphoserineBy similarity1
Modified residuei7984-hydroxyprolineBy similarity1
Modified residuei8044-hydroxyprolineBy similarity1
Modified residuei8074-hydroxyprolineBy similarity1
Modified residuei8164-hydroxyprolineBy similarity1
Modified residuei8224-hydroxyprolineBy similarity1
Modified residuei8404-hydroxyprolineBy similarity1
Modified residuei8494-hydroxyprolineBy similarity1
Modified residuei8584-hydroxyprolineBy similarity1
Modified residuei8615-hydroxylysineBy similarity1
Modified residuei8704-hydroxyprolineBy similarity1
Modified residuei8764-hydroxyprolineBy similarity1
Modified residuei8843-hydroxyprolineBy similarity1
Modified residuei8854-hydroxyprolineBy similarity1
Modified residuei8944-hydroxyprolineBy similarity1
Modified residuei8974-hydroxyprolineBy similarity1
Modified residuei9184-hydroxyprolineBy similarity1
Modified residuei9274-hydroxyprolineBy similarity1
Modified residuei9364-hydroxyprolineBy similarity1
Modified residuei9454-hydroxyprolineBy similarity1
Modified residuei9634-hydroxyprolineBy similarity1
Modified residuei9724-hydroxyprolineBy similarity1
Modified residuei9754-hydroxyprolineBy similarity1
Modified residuei9814-hydroxyprolineBy similarity1
Modified residuei9964-hydroxyprolineBy similarity1
Modified residuei10024-hydroxyprolineBy similarity1
Modified residuei10084-hydroxyprolineBy similarity1
Modified residuei10174-hydroxyprolineBy similarity1
Modified residuei10234-hydroxyprolineBy similarity1
Modified residuei10325-hydroxylysineBy similarity1
Modified residuei10444-hydroxyprolineBy similarity1
Modified residuei10474-hydroxyprolineBy similarity1
Modified residuei10504-hydroxyprolineBy similarity1
Modified residuei10955-hydroxylysineBy similarity1
Modified residuei11075-hydroxylysine; alternateBy similarity1
Glycosylationi1107O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei11194-hydroxyprolineBy similarity1
Modified residuei11224-hydroxyprolineBy similarity1
Modified residuei11254-hydroxyprolineBy similarity1
Modified residuei11434-hydroxyprolineBy similarity1
Modified residuei11584-hydroxyprolineBy similarity1
Modified residuei11633-hydroxyproline1 Publication1
Modified residuei11644-hydroxyprolineBy similarity1
Modified residuei11783-hydroxyproline1 Publication1
Modified residuei11794-hydroxyproline1 Publication1
Modified residuei11813-hydroxyproline1 Publication1
Modified residuei11824-hydroxyproline1 Publication1
Modified residuei11843-hydroxyprolineBy similarity1
Modified residuei11854-hydroxyproline1 Publication1
Modified residuei11884-hydroxyproline1 Publication1
Modified residuei11914-hydroxyprolineBy similarity1
Modified residuei1207Allysine1 Publication1
<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 bondi1258 ↔ 1290PROSITE-ProRule annotation
Disulfide bondi1264Interchain (with C-1281)PROSITE-ProRule annotation
Disulfide bondi1281Interchain (with C-1264)PROSITE-ProRule annotation
Disulfide bondi1298 ↔ 1461PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1414PROSITE-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.2 Publications
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.1 Publication
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.By similarity

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
P02453

PeptideAtlas

More...
PeptideAtlasi
P02453

PRoteomics IDEntifications database

More...
PRIDEi
P02453

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P02453

<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
ENSBTAG00000013103 Expressed in 9 organ(s), highest expression level in colon

<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 (By similarity). Interacts with TRAM2 (By similarity). Interacts with MFAP4 in a Ca (2+)-dependent manner (PubMed:26601954).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3101 Collagen type I trimer

Protein interaction database and analysis system

More...
IntActi
P02453, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000017420

<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
P02453

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 96VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1228 – 1463Fibrillar 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>Regioni162 – 177Nonhelical region (N-terminal)Add BLAST16
Regioni178 – 1191Triple-helical regionAdd BLAST1014
Regioni1192 – 1215Nonhelical region (C-terminal)Add BLAST24

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>Motifi744 – 746Cell attachment siteSequence analysis3
Motifi1092 – 1094Cell 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).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
P02453

KEGG Orthology (KO)

More...
KOi
K06236

Identification of Orthologs from Complete Genome Data

More...
OMAi
THGQEDI

Database of Orthologous Groups

More...
OrthoDBi
337699at2759

TreeFam database of animal gene trees

More...
TreeFami
TF344135

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 10 hits
PF00093 VWC, 1 hit

ProDom; a protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>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.

P02453-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR
60 70 80 90 100
DVWKPVPCQI CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE
110 120 130 140 150
SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP
160 170 180 190 200
GPPGLGGNFA PQLSYGYDEK STGISVPGPM GPSGPRGLPG PPGAPGPQGF
210 220 230 240 250
QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG
260 270 280 290 300
ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM
310 320 330 340 350
GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA
360 370 380 390 400
KGEGGPQGPR GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG
410 420 430 440 450
APGIAGAPGF PGARGPSGPQ GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP
460 470 480 490 500
GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP GPPGERGGPG SRGFPGADGV
510 520 530 540 550
AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
560 570 580 590 600
KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP
610 620 630 640 650
GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP
660 670 680 690 700
PGEAGKPGEQ GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG
710 720 730 740 750
APGNDGAKGD AGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK
760 770 780 790 800
GADGAPGKDG VRGLTGPIGP PGPAGAPGDK GEAGPSGPAG PTGARGAPGD
810 820 830 840 850
RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP GPAGPAGPPG
860 870 880 890 900
PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA
910 920 930 940 950
GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP
960 970 980 990 1000
QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG
1010 1020 1030 1040 1050
PPGLAGPPGE SGREGAPGAE GSPGRDGSPG AKGDRGETGP AGPPGAPGAP
1060 1070 1080 1090 1100
GAPGPVGPAG KSGDRGETGP AGPAGPIGPV GARGPAGPQG PRGDKGETGE
1110 1120 1130 1140 1150
QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR GPPGSAGSPG
1160 1170 1180 1190 1200
KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL
1210 1220 1230 1240 1250
PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS
1260 1270 1280 1290 1300
RKNPARTCRD LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY
1310 1320 1330 1340 1350
PTQPSVAQKN WYISKNPKEK RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ
1360 1370 1380 1390 1400
LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKALLLQ GSNEIEIRAE
1410 1420 1430 1440 1450
GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID VAPLDVGAPD
1460
QEFGFDVGPA CFL
Length:1,463
Mass (Da):138,938
Last modified:May 30, 2006 - 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:i8A6E17F276C4C6FA
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 conflicti687Q → E AA sequence (PubMed:4673951).Curated1
Sequence conflicti790 – 792Missing AA sequence (PubMed:4359390).Curated3
Sequence conflicti794A → T AA sequence (PubMed:4359390).Curated1
Sequence conflicti1043P → A AA sequence (PubMed:4343808).Curated1
Sequence conflicti1046A → P AA sequence (PubMed:4343808).Curated1
Sequence conflicti1074A → I AA sequence (PubMed:4343808).Curated1
Sequence conflicti1077I → V AA sequence (PubMed:4343808).Curated1
Sequence conflicti1080V → A AA sequence (PubMed:4343808).Curated1
Sequence conflicti1206E → QZ AA sequence (PubMed:11946479).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC105184 mRNA Translation: AAI05185.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A91193 CGBO1S

NCBI Reference Sequences

More...
RefSeqi
NP_001029211.1, NM_001034039.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
282187

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:282187

<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
BC105184 mRNA Translation: AAI05185.1
PIRiA91193 CGBO1S
RefSeqiNP_001029211.1, NM_001034039.2

3D structure databases

SMRiP02453
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-3101 Collagen type I trimer
IntActiP02453, 1 interactor
STRINGi9913.ENSBTAP00000017420

Proteomic databases

PaxDbiP02453
PeptideAtlasiP02453
PRIDEiP02453

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103
GeneIDi282187
KEGGibta:282187

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1277
VGNCiVGNC:27560 COL1A1

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000156584
HOGENOMiHOG000085654
InParanoidiP02453
KOiK06236
OMAiTHGQEDI
OrthoDBi337699at2759
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-BTA-114604 GPVI-mediated activation cascade
R-BTA-1442490 Collagen degradation
R-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-BTA-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-202733 Cell surface interactions at the vascular wall
R-BTA-216083 Integrin cell surface interactions
R-BTA-2214320 Anchoring fibril formation
R-BTA-2243919 Crosslinking of collagen fibrils
R-BTA-3000171 Non-integrin membrane-ECM interactions
R-BTA-3000178 ECM proteoglycans
R-BTA-430116 GP1b-IX-V activation signalling
R-BTA-75892 Platelet Adhesion to exposed collagen
R-BTA-8948216 Collagen chain trimerization

Miscellaneous databases

PMAP-CutDBiP02453

Gene expression databases

BgeeiENSBTAG00000013103 Expressed in 9 organ(s), highest expression level in colon

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, 10 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_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02453
Secondary accession number(s): Q3MHM2
<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: May 30, 2006
Last modified: May 8, 2019
This is version 151 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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