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Entry version 112 (08 May 2019)
Sequence version 1 (01 Nov 1999)
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Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 bindingi1273CalciumBy similarity1
Metal bindingi1275CalciumBy similarity1
Metal bindingi1276Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1278Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1281CalciumBy 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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Defects in COL1A1 are a cause of osteogenesis imperfecta (OI).

Keywords - Diseasei

Disease mutation

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3751652

<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 – 22By similarityAdd 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_000000571323 – 157N-terminal propeptideBy similarityAdd BLAST135
<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_0000005714158 – 1214Collagen alpha-1(I) chainBy similarityAdd BLAST1057
PropeptideiPRO_00000057151215 – 1460C-terminal propeptideBy similarityAdd 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 residuei166AllysineBy similarity1
Modified residuei167PhosphoserineBy similarity1
Modified residuei1864-hydroxyprolineBy similarity1
Modified residuei1894-hydroxyprolineBy similarity1
Modified residuei1924-hydroxyprolineBy similarity1
Modified residuei2014-hydroxyprolineBy similarity1
Modified residuei2044-hydroxyprolineBy similarity1
Modified residuei2074-hydroxyprolineBy similarity1
Modified residuei2224-hydroxyprolineBy similarity1
Modified residuei2374-hydroxyprolineBy similarity1
Modified residuei2434-hydroxyprolineBy similarity1
Modified residuei2524-hydroxyprolineBy similarity1
Modified residuei2584-hydroxyprolineBy similarity1
Modified residuei2615-hydroxylysine; alternateBy similarity1
<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>Glycosylationi261O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei267PhosphoserineBy similarity1
Modified residuei2854-hydroxyprolineBy similarity1
Modified residuei2884-hydroxyprolineBy similarity1
Modified residuei2944-hydroxyprolineBy similarity1
Modified residuei3034-hydroxyprolineBy similarity1
Modified residuei3094-hydroxyprolineBy similarity1
Modified residuei3304-hydroxyprolineBy similarity1
Modified residuei3394-hydroxyprolineBy similarity1
Modified residuei3424-hydroxyprolineBy similarity1
Modified residuei3694-hydroxyprolineBy similarity1
Modified residuei3724-hydroxyprolineBy similarity1
Modified residuei3844-hydroxyprolineBy similarity1
Modified residuei3904-hydroxyprolineBy similarity1
Modified residuei3994-hydroxyprolineBy similarity1
Modified residuei4054-hydroxyprolineBy similarity1
Modified residuei4084-hydroxyprolineBy similarity1
Modified residuei4234-hydroxyprolineBy similarity1
Modified residuei4265-hydroxylysineBy similarity1
Modified residuei4324-hydroxyprolineBy similarity1
Modified residuei4354-hydroxyprolineBy similarity1
Modified residuei4474-hydroxyprolineBy similarity1
Modified residuei4564-hydroxyprolineBy similarity1
Modified residuei4714-hydroxyprolineBy similarity1
Modified residuei4774-hydroxyprolineBy similarity1
Modified residuei4864-hydroxyprolineBy similarity1
Modified residuei4924-hydroxyprolineBy similarity1
Modified residuei5015-hydroxylysineBy similarity1
Modified residuei5104-hydroxyprolineBy similarity1
Modified residuei5194-hydroxyprolineBy similarity1
Modified residuei5254-hydroxyprolineBy similarity1
Modified residuei5314-hydroxyprolineBy similarity1
Modified residuei5404-hydroxyprolineBy similarity1
Modified residuei5434-hydroxyprolineBy similarity1
Modified residuei5524-hydroxyprolineBy similarity1
Modified residuei5614-hydroxyprolineBy similarity1
Modified residuei5674-hydroxyprolineBy similarity1
Modified residuei5794-hydroxyprolineBy similarity1
Modified residuei5884-hydroxyprolineBy similarity1
Modified residuei5974-hydroxyprolineBy similarity1
Modified residuei6004-hydroxyprolineBy similarity1
Modified residuei6184-hydroxyprolineBy similarity1
Modified residuei6364-hydroxyprolineBy similarity1
Modified residuei6424-hydroxyprolineBy similarity1
Modified residuei6484-hydroxyprolineBy similarity1
Modified residuei6544-hydroxyprolineBy similarity1
Modified residuei6604-hydroxyprolineBy similarity1
Modified residuei6664-hydroxyprolineBy similarity1
Modified residuei6784-hydroxyprolineBy similarity1
Modified residuei6874-hydroxyprolineBy similarity1
Modified residuei6994-hydroxyprolineBy similarity1
Modified residuei7114-hydroxyprolineBy similarity1
Modified residuei7144-hydroxyprolineBy similarity1
Modified residuei7204-hydroxyprolineBy similarity1
Modified residuei7264-hydroxyprolineBy similarity1
Modified residuei7354-hydroxyprolineBy similarity1
Modified residuei7475-hydroxylysineBy similarity1
Modified residuei7534-hydroxyprolineBy similarity1
Modified residuei7684-hydroxyprolineBy similarity1
Modified residuei7744-hydroxyprolineBy similarity1
Modified residuei783PhosphoserineBy similarity1
Modified residuei7954-hydroxyprolineBy similarity1
Modified residuei8014-hydroxyprolineBy similarity1
Modified residuei8044-hydroxyprolineBy similarity1
Modified residuei8134-hydroxyprolineBy similarity1
Modified residuei8194-hydroxyprolineBy similarity1
Modified residuei8374-hydroxyprolineBy similarity1
Modified residuei8464-hydroxyprolineBy similarity1
Modified residuei8554-hydroxyprolineBy similarity1
Modified residuei8585-hydroxylysineBy similarity1
Modified residuei8674-hydroxyprolineBy similarity1
Modified residuei8734-hydroxyprolineBy similarity1
Modified residuei8813-hydroxyprolineBy similarity1
Modified residuei8824-hydroxyprolineBy similarity1
Modified residuei8914-hydroxyprolineBy similarity1
Modified residuei8944-hydroxyprolineBy similarity1
Modified residuei9154-hydroxyprolineBy similarity1
Modified residuei9244-hydroxyprolineBy similarity1
Modified residuei9334-hydroxyprolineBy similarity1
Modified residuei9424-hydroxyprolineBy similarity1
Modified residuei9604-hydroxyprolineBy similarity1
Modified residuei9694-hydroxyprolineBy similarity1
Modified residuei9724-hydroxyprolineBy similarity1
Modified residuei9784-hydroxyprolineBy similarity1
Modified residuei9934-hydroxyprolineBy similarity1
Modified residuei9994-hydroxyprolineBy similarity1
Modified residuei10054-hydroxyprolineBy similarity1
Modified residuei10144-hydroxyprolineBy similarity1
Modified residuei10204-hydroxyprolineBy similarity1
Modified residuei10295-hydroxylysineBy similarity1
Modified residuei10414-hydroxyprolineBy similarity1
Modified residuei10444-hydroxyprolineBy similarity1
Modified residuei10474-hydroxyprolineBy similarity1
Modified residuei10925-hydroxylysineBy similarity1
Modified residuei11045-hydroxylysine; alternateBy similarity1
Glycosylationi1104O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei11164-hydroxyprolineBy similarity1
Modified residuei11194-hydroxyprolineBy similarity1
Modified residuei11224-hydroxyprolineBy similarity1
Modified residuei11404-hydroxyprolineBy similarity1
Modified residuei11554-hydroxyprolineBy similarity1
Modified residuei11603-hydroxyprolineBy similarity1
Modified residuei11614-hydroxyprolineBy similarity1
Modified residuei11753-hydroxyprolineBy similarity1
Modified residuei11764-hydroxyprolineBy similarity1
Modified residuei11783-hydroxyprolineBy similarity1
Modified residuei11794-hydroxyprolineBy similarity1
Modified residuei11813-hydroxyprolineBy similarity1
Modified residuei11824-hydroxyprolineBy similarity1
Modified residuei11854-hydroxyprolineBy similarity1
Modified residuei11884-hydroxyprolineBy similarity1
Modified residuei1204AllysineBy 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 bondi1255 ↔ 1287PROSITE-ProRule annotation
Disulfide bondi1261Interchain (with C-1278)PROSITE-ProRule annotation
Disulfide bondi1278Interchain (with C-1261)PROSITE-ProRule annotation
Disulfide bondi1295 ↔ 1458PROSITE-ProRule annotation
Glycosylationi1361N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi1366 ↔ 1411PROSITE-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.By similarity
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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q9XSJ7

PRoteomics IDEntifications database

More...
PRIDEi
Q9XSJ7

<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. Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)-dependent manner.By similarity

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3103 Collagen type I trimer

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000025056

<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
Q9XSJ7

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>Domaini34 – 92VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1225 – 1460Fibrillar 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>Regioni158 – 174Nonhelical region (N-terminal)Add BLAST17
Regioni175 – 1188Triple-helical regionAdd BLAST1014
Regioni1189 – 1214Nonhelical 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>Motifi741 – 743Cell attachment siteSequence analysis3
Motifi1089 – 1091Cell 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000085654

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9XSJ7

KEGG Orthology (KO)

More...
KOi
K06236

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, 12 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.

Q9XSJ7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSFVDLRLL LLLAATALLT HGQEEGQEED IPPVTCVQNG LRYYDRDVWK
60 70 80 90 100
PEACRICVCD NGNVLCDDVI CDETKNCPGA QVPPGECCPV CPDGEASPTD
110 120 130 140 150
QETTGVEGPK GDTGPRGPRG PAGPPGRDGI PGQPGLPGPP GPPGPPGPPG
160 170 180 190 200
LGGNFAPQMS YGYDEKSTGG ISVPGPMGPS GPRGLPGPPG APGPQGFQGP
210 220 230 240 250
PGEPGEPGAS GPMGPRGPPG PPGKNGDDGE AGKPGRPGER GPPGPQGARG
260 270 280 290 300
LPGTAGLPGM KGHRGFSGLD GAKGDAGPAG PKGEPGSPGE NGAPGQMGPR
310 320 330 340 350
GLPGERGRPG APGPAGARGN DGATGAAGPP GPTGPAGPPG FPGAVGAKGE
360 370 380 390 400
AGPQGARGSE GPQGVRGEPG PPGPAGAAGP AGNPGADGQP GAKGANGAPG
410 420 430 440 450
IAGAPGFPGA RGPSGPQGPS GPPGPKGNSG EPGAPGNKGD TGAKGEPGPT
460 470 480 490 500
GIQGPPGPAG EEGKRGARGE PGPTGLPGPP GERGGPGSRG FPGADGVAGP
510 520 530 540 550
KGPAGERGSP GPAGPKGSPG EAGRPGEAGL PGAKGLTGSP GSPGPDGKTG
560 570 580 590 600
PPGPAGQDGR PGPPGPPGAR GQAGVMGFPG PKGAAGEPGK AGERGVPGPP
610 620 630 640 650
GAVGPAGKDG EAGAQGPPGP AGPAGERGEQ GPAGSPGFQG LPGPAGPPGE
660 670 680 690 700
AGKPGEQGVP GDLGAPGPSG ARGERGFPGE RGVQGPPGPA GPRGANGAPG
710 720 730 740 750
NDGAKGDAGA PGAPGSQGAP GLQGMPGERG AAGLPGPKGD RGDAGPKGAD
760 770 780 790 800
GSPGKDGVRG LTGPIGPPGP AGAPGDKGEA GPSGPAGPTG ARGAPGDRGE
810 820 830 840 850
PGPPGPAGFA GPPGADGQPG AKGEPGDAGA KGDAGPPGPA GPTGPPGPIG
860 870 880 890 900
NVGAPGPKGA RGSAGPPGAT GFPGAAGRVG PPGPSGNAGP PGPPGPAGKE
910 920 930 940 950
GGKGARGETG PAGRPGEVGP PGPPGPAGEK GSPGADGPAG APGTPGPQGI
960 970 980 990 1000
AGQRGVVGLP GQRGERGFPG LPGPSGEPGK QGPSGTSGER GPPGPMGPPG
1010 1020 1030 1040 1050
LAGPPGESGR EGSPGAEGSP GRDGSPGPKG DRGETGPAGP PGAPGAPGAP
1060 1070 1080 1090 1100
GPVGPAGKNG DRGETGPAGP AGPIGPVGAR GPAGPQGPRG DKGETGEQGD
1110 1120 1130 1140 1150
RGIKGHRGFS GLQGPPGPPG SPGEQGPSGA SGPAGPRGPP GSAGSPGKDG
1160 1170 1180 1190 1200
LNGLPGPIGP PGPRGRTGDA GPVGPPGPPG PPGPPGPPSG GFDFSFLPQP
1210 1220 1230 1240 1250
PQEKAHDGGR YYRADDANVV RDRDLEVDTT LKSLSQQIEN IRSPEGSRKN
1260 1270 1280 1290 1300
PARTCRDLKM CHSDWKSGEY WIDPNQGCNL DAIKVFCNME TGETCVYPTQ
1310 1320 1330 1340 1350
PQVAQKNWYI SKNPKEKRHV WYGESMTDGF QFEYGGQGSD PADVAIQLTF
1360 1370 1380 1390 1400
LRLMSTEASQ NITYHCKNSV AYMDQQTGNL KKALLLQGSN EIEIRAEGNS
1410 1420 1430 1440 1450
RFTYSVTYDG CTSHTGAWGK TVIEYKTTKT SRLPIIDVAP LDVGAPDQEF
1460
GMDIGPVCFL
Length:1,460
Mass (Da):138,762
Last modified:November 1, 1999 - v1
<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:i58E3674D2B570697
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti208G → A in OI; severe. 1 Publication1

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
AF153062 mRNA Translation: AAD34619.1

NCBI Reference Sequences

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RefSeqi
NP_001003090.1, NM_001003090.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
403651

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cfa:403651

<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
AF153062 mRNA Translation: AAD34619.1
RefSeqiNP_001003090.1, NM_001003090.1

3D structure databases

SMRiQ9XSJ7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-3103 Collagen type I trimer
STRINGi9612.ENSCAFP00000025056

Chemistry databases

ChEMBLiCHEMBL3751652

Proteomic databases

PaxDbiQ9XSJ7
PRIDEiQ9XSJ7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403651
KEGGicfa:403651

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1277

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
HOGENOMiHOG000085654
InParanoidiQ9XSJ7
KOiK06236
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, 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

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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_CANLF
<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: Q9XSJ7
<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: May 30, 2000
Last sequence update: November 1, 1999
Last modified: May 8, 2019
This is version 112 of the entry and version 1 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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