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Entry version 116 (08 May 2019)
Sequence version 3 (10 Jul 2007)
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Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Gallus gallus (Chicken)
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

  • extracellular matrix structural constituent Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

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

<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <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: Unplaced

<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 – 22Add 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_000000571623 – 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_0000005717152 – 1207Collagen alpha-1(I) chain1 PublicationAdd BLAST1056
PropeptideiPRO_00000057181208 – 1453C-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 residuei152Pyrrolidone carboxylic acid1 Publication1
Modified residuei160AllysineBy similarity1
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-hydroxyproline1 Publication1
Modified residuei2304-hydroxyproline1 Publication1
Modified residuei2364-hydroxyproline1 Publication1
Modified residuei2454-hydroxyproline1 Publication1
Modified residuei2514-hydroxyproline1 Publication1
Modified residuei2545-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>Glycosylationi254O-linked (Gal...) hydroxylysine; partial1 Publication1
Modified residuei2694-hydroxyproline1 Publication1
Modified residuei2784-hydroxyproline1 Publication1
Modified residuei2814-hydroxyproline1 Publication1
Modified residuei2874-hydroxyproline1 Publication1
Modified residuei2964-hydroxyproline1 Publication1
Modified residuei3024-hydroxyproline1 Publication1
Modified residuei3174-hydroxyproline1 Publication1
Modified residuei3234-hydroxyproline1 Publication1
Modified residuei3324-hydroxyproline1 Publication1
Modified residuei3354-hydroxyproline1 Publication1
Modified residuei3624-hydroxyproline1 Publication1
Modified residuei3654-hydroxyproline1 Publication1
Modified residuei3774-hydroxyproline1 Publication1
Modified residuei3834-hydroxyproline1 Publication1
Modified residuei3924-hydroxyproline1 Publication1
Modified residuei3984-hydroxyproline1 Publication1
Modified residuei4014-hydroxyproline1 Publication1
Modified residuei4164-hydroxyproline1 Publication1
Modified residuei4195-hydroxylysine1 Publication1
Modified residuei4254-hydroxyproline1 Publication1
Modified residuei4284-hydroxyproline1 Publication1
Modified residuei4404-hydroxyproline1 Publication1
Modified residuei4494-hydroxyproline1 Publication1
Modified residuei4644-hydroxyproline1 Publication1
Modified residuei4704-hydroxyproline1 Publication1
Modified residuei4794-hydroxyproline1 Publication1
Modified residuei4854-hydroxyproline1 Publication1
Modified residuei4945-hydroxylysine1 Publication1
Modified residuei4974-hydroxyproline1 Publication1
Modified residuei5034-hydroxyproline1 Publication1
Modified residuei5124-hydroxyproline1 Publication1
Modified residuei5184-hydroxyproline1 Publication1
Modified residuei5244-hydroxyproline1 Publication1
Modified residuei5334-hydroxyproline1 Publication1
Modified residuei5364-hydroxyproline1 Publication1
Modified residuei5454-hydroxyproline1 Publication1
Modified residuei5544-hydroxyproline1 Publication1
Modified residuei5604-hydroxyproline1 Publication1
Modified residuei5724-hydroxyproline1 Publication1
Modified residuei5814-hydroxyproline1 Publication1
Modified residuei5844-hydroxyproline1 Publication1
Modified residuei5904-hydroxyproline1 Publication1
Modified residuei5934-hydroxyproline1 Publication1
Modified residuei6114-hydroxyproline1 Publication1
Modified residuei6294-hydroxyproline1 Publication1
Modified residuei6354-hydroxyproline1 Publication1
Modified residuei6414-hydroxyproline1 Publication1
Modified residuei6474-hydroxyproline1 Publication1
Modified residuei6534-hydroxyproline1 Publication1
Modified residuei6594-hydroxyproline1 Publication1
Modified residuei6714-hydroxyproline1 Publication1
Modified residuei6804-hydroxyproline1 Publication1
Modified residuei6924-hydroxyproline1 Publication1
Modified residuei7044-hydroxyproline1 Publication1
Modified residuei7074-hydroxyproline1 Publication1
Modified residuei7134-hydroxyproline1 Publication1
Modified residuei7194-hydroxyproline1 Publication1
Modified residuei7284-hydroxyproline1 Publication1
Modified residuei7374-hydroxyproline1 Publication1
Modified residuei7405-hydroxylysine1 Publication1
Modified residuei7464-hydroxyproline1 Publication1
Modified residuei7614-hydroxyproline1 Publication1
Modified residuei7674-hydroxyproline1 Publication1
Modified residuei7764-hydroxyproline1 Publication1
Modified residuei7884-hydroxyproline1 Publication1
Modified residuei7944-hydroxyproline1 Publication1
Modified residuei7974-hydroxyproline1 Publication1
Modified residuei8064-hydroxyproline1 Publication1
Modified residuei8124-hydroxyproline1 Publication1
Modified residuei8304-hydroxyproline1 Publication1
Modified residuei8394-hydroxyproline1 Publication1
Modified residuei8484-hydroxyproline1 Publication1
Modified residuei8515-hydroxylysine1 Publication1
Modified residuei8604-hydroxyproline1 Publication1
Modified residuei8664-hydroxyproline1 Publication1
Modified residuei8743-hydroxyprolineBy similarity1
Modified residuei8754-hydroxyproline1 Publication1
Modified residuei8844-hydroxyproline1 Publication1
Modified residuei8874-hydroxyproline1 Publication1
Modified residuei9084-hydroxyproline1 Publication1
Modified residuei9114-hydroxyproline1 Publication1
Modified residuei9174-hydroxyproline1 Publication1
Modified residuei9204-hydroxyproline1 Publication1
Modified residuei9264-hydroxyproline1 Publication1
Modified residuei9354-hydroxyproline1 Publication1
Modified residuei9534-hydroxyproline1 Publication1
Modified residuei9624-hydroxyproline1 Publication1
Modified residuei9654-hydroxyproline1 Publication1
Modified residuei9714-hydroxyproline1 Publication1
Modified residuei9864-hydroxyproline1 Publication1
Modified residuei9924-hydroxyproline1 Publication1
Modified residuei9984-hydroxyproline1 Publication1
Modified residuei10074-hydroxyproline1 Publication1
Modified residuei10134-hydroxyproline1 Publication1
Modified residuei10225-hydroxylysine; partial1 Publication1
Modified residuei10344-hydroxyproline1 Publication1
Modified residuei10374-hydroxyproline1 Publication1
Modified residuei10404-hydroxyproline1 Publication1
Modified residuei10674-hydroxyproline1 Publication1
Modified residuei10855-hydroxylysine; partial1 Publication1
Modified residuei10975-hydroxylysine; alternate1 Publication1
Glycosylationi1097O-linked (Gal...) hydroxylysine; partial1 Publication1
Modified residuei11094-hydroxyproline1 Publication1
Modified residuei11124-hydroxyproline1 Publication1
Modified residuei11154-hydroxyproline1 Publication1
Modified residuei11334-hydroxyproline1 Publication1
Modified residuei11484-hydroxyproline1 Publication1
Modified residuei11533-hydroxyproline1 Publication1
Modified residuei11544-hydroxyproline1 Publication1
Modified residuei11683-hydroxyprolineBy similarity1
Modified residuei11694-hydroxyproline1 Publication1
Modified residuei11713-hydroxyprolineBy similarity1
Modified residuei11724-hydroxyproline1 Publication1
Modified residuei11743-hydroxyprolineBy similarity1
Modified residuei11754-hydroxyproline1 Publication1
Modified residuei11784-hydroxyproline1 Publication1
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...) asparagineBy similarity1
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 4-hydroxylated in some or all of the chains.5 Publications
Contains 3-hydroxyproline. 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.3 Publications
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1022Not glycosylated1 Publication1
Sitei1085Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P02457

<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.

<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.

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3102 Collagen type I trimer

Protein interaction database and analysis system

More...
IntActi
P02457, 1 interactor

<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>Domaini31 – 89VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1218 – 1453Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST236

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02457

Database of Orthologous Groups

More...
OrthoDBi
337699at2759

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.

P02457-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP
60 70 80 90 100
CQICVCDSGN ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES
110 120 130 140 150
AGVEGPKGDT GPRGDRGLPG PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA
160 170 180 190 200
PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG PPGAPGPQGF QGPPGEPGEP
210 220 230 240 250
GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG ARGLPGTAGL
260 270 280 290 300
PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
310 320 330 340 350
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR
360 370 380 390 400
GSEGPQGSRG EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF
410 420 430 440 450
PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG
460 470 480 490 500
PAGEEGKRGA RGEPGPAGLP GPAGERGAPG SRGFPGADGI AGPKGPPGER
510 520 530 540 550
GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ
560 570 580 590 600
DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG
610 620 630 640 650
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ
660 670 680 690 700
GVPGNAGAPG PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD
710 720 730 740 750
AGAPGAPGNE GPPGLEGMPG ERGAAGLPGA KGDRGDPGPK GADGAPGKDG
760 770 780 790 800
LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG PTGARGAPGD RGEPGPPGPA
810 820 830 840 850
GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG PAGZVGAPGP
860 870 880 890 900
KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG
910 920 930 940 950
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV
960 970 980 990 1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE
1010 1020 1030 1040 1050
AGREGAPGAE GAPGRDGAAG PKGDRGETGP AGPPGAPGAP GAPGPVGPAG
1060 1070 1080 1090 1100
KNGDRGETGP AGPAGPPGPA GARGPAGPQG PRGDKGETGE QGDRGMKGHR
1110 1120 1130 1140 1150
GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG KDGLNGLPGP
1160 1170 1180 1190 1200
IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD
1210 1220 1230 1240 1250
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD
1260 1270 1280 1290 1300
LKMCHGDWKS GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN
1310 1320 1330 1340 1350
WYLSKNPKEK KHVWFGETMS DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE
1360 1370 1380 1390 1400
ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ GANEIEIRAE GNSRFTYGVT
1410 1420 1430 1440 1450
EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD QEFGIDIGPV

CFL
Length:1,453
Mass (Da):137,755
Last modified:July 10, 2007 - 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:i61C617239E271A82
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 conflicti1441Q → H in AAA48671 (PubMed:6987088).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

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DDBJi
Links Updated
M17839, M17838 Genomic DNA Translation: AAA48704.1
V00401 mRNA Translation: CAA23695.1
M10571 mRNA Translation: AAA48671.1 Sequence problems.
M17607 mRNA Translation: AAA48672.1

Protein sequence database of the Protein Information Resource

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PIRi
A27179
A90458 CGCH1S
I50629
S07234

<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
M17839, M17838 Genomic DNA Translation: AAA48704.1
V00401 mRNA Translation: CAA23695.1
M10571 mRNA Translation: AAA48671.1 Sequence problems.
M17607 mRNA Translation: AAA48672.1
PIRiA27179
A90458 CGCH1S
I50629
S07234

3D structure databases

Database of comparative protein structure models

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ModBasei
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

ComplexPortaliCPX-3102 Collagen type I trimer
IntActiP02457, 1 interactor

Proteomic databases

PRIDEiP02457

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiP02457
OrthoDBi337699at2759

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

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ProtoNeti
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<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_CHICK
<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: P02457
<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: July 10, 2007
Last modified: May 8, 2019
This is version 116 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
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