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Q9XSJ7

- CO1A1_CANFA

UniProt

Q9XSJ7 - CO1A1_CANFA

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Protein

Collagen alpha-1(I) chain

Gene
COL1A1
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1273 – 12731Calcium By similarity
Metal bindingi1275 – 12751Calcium By similarity
Metal bindingi1276 – 12761Calcium; via carbonyl oxygen By similarity
Metal bindingi1278 – 12781Calcium; via carbonyl oxygen By similarity
Metal bindingi1281 – 12811Calcium By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene namesi
Name:COL1A1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in COL1A1 are a cause of osteogenesis imperfecta (OI).1 Publication

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 By similarityAdd
BLAST
Propeptidei23 – 157135N-terminal propeptidePRO_0000005713Add
BLAST
Chaini158 – 12141057Collagen alpha-1(I) chainPRO_0000005714Add
BLAST
Propeptidei1215 – 1460246C-terminal propeptidePRO_0000005715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei158 – 1581Pyrrolidone carboxylic acid By similarity
Modified residuei166 – 1661Allysine By similarity
Modified residuei261 – 26115-hydroxylysine; alternate By similarity
Glycosylationi261 – 2611O-linked (Gal...); alternate By similarity
Modified residuei1160 – 116013-hydroxyproline By similarity
Disulfide bondi1255 ↔ 1287 By similarity
Disulfide bondi1261 – 1261Interchain (with C-1278) By similarity
Disulfide bondi1278 – 1278Interchain (with C-1261) By similarity
Disulfide bondi1295 ↔ 1458 By similarity
Glycosylationi1361 – 13611N-linked (GlcNAc...) By similarity
Disulfide bondi1366 ↔ 1411 By similarity

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ9XSJ7.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 By similarity. Interacts with TRAM2 By similarity.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 9259VWFCAdd
BLAST
Domaini1225 – 1460236Fibrillar collagen NC1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 17417Nonhelical region (N-terminal)Add
BLAST
Regioni175 – 11881014Triple-helical regionAdd
BLAST
Regioni1189 – 121426Nonhelical region (C-terminal)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi741 – 7433Cell attachment site Reviewed prediction
Motifi1089 – 10913Cell attachment site Reviewed prediction

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.

Sequence similaritiesi

Contains 1 VWFC domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ9XSJ7.
KOiK06236.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 12 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XSJ7-1 [UniParc]FASTAAdd to Basket

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MFSFVDLRLL LLLAATALLT HGQEEGQEED IPPVTCVQNG LRYYDRDVWK     50
PEACRICVCD NGNVLCDDVI CDETKNCPGA QVPPGECCPV CPDGEASPTD 100
QETTGVEGPK GDTGPRGPRG PAGPPGRDGI PGQPGLPGPP GPPGPPGPPG 150
LGGNFAPQMS YGYDEKSTGG ISVPGPMGPS GPRGLPGPPG APGPQGFQGP 200
PGEPGEPGAS GPMGPRGPPG PPGKNGDDGE AGKPGRPGER GPPGPQGARG 250
LPGTAGLPGM KGHRGFSGLD GAKGDAGPAG PKGEPGSPGE NGAPGQMGPR 300
GLPGERGRPG APGPAGARGN DGATGAAGPP GPTGPAGPPG FPGAVGAKGE 350
AGPQGARGSE GPQGVRGEPG PPGPAGAAGP AGNPGADGQP GAKGANGAPG 400
IAGAPGFPGA RGPSGPQGPS GPPGPKGNSG EPGAPGNKGD TGAKGEPGPT 450
GIQGPPGPAG EEGKRGARGE PGPTGLPGPP GERGGPGSRG FPGADGVAGP 500
KGPAGERGSP GPAGPKGSPG EAGRPGEAGL PGAKGLTGSP GSPGPDGKTG 550
PPGPAGQDGR PGPPGPPGAR GQAGVMGFPG PKGAAGEPGK AGERGVPGPP 600
GAVGPAGKDG EAGAQGPPGP AGPAGERGEQ GPAGSPGFQG LPGPAGPPGE 650
AGKPGEQGVP GDLGAPGPSG ARGERGFPGE RGVQGPPGPA GPRGANGAPG 700
NDGAKGDAGA PGAPGSQGAP GLQGMPGERG AAGLPGPKGD RGDAGPKGAD 750
GSPGKDGVRG LTGPIGPPGP AGAPGDKGEA GPSGPAGPTG ARGAPGDRGE 800
PGPPGPAGFA GPPGADGQPG AKGEPGDAGA KGDAGPPGPA GPTGPPGPIG 850
NVGAPGPKGA RGSAGPPGAT GFPGAAGRVG PPGPSGNAGP PGPPGPAGKE 900
GGKGARGETG PAGRPGEVGP PGPPGPAGEK GSPGADGPAG APGTPGPQGI 950
AGQRGVVGLP GQRGERGFPG LPGPSGEPGK QGPSGTSGER GPPGPMGPPG 1000
LAGPPGESGR EGSPGAEGSP GRDGSPGPKG DRGETGPAGP PGAPGAPGAP 1050
GPVGPAGKNG DRGETGPAGP AGPIGPVGAR GPAGPQGPRG DKGETGEQGD 1100
RGIKGHRGFS GLQGPPGPPG SPGEQGPSGA SGPAGPRGPP GSAGSPGKDG 1150
LNGLPGPIGP PGPRGRTGDA GPVGPPGPPG PPGPPGPPSG GFDFSFLPQP 1200
PQEKAHDGGR YYRADDANVV RDRDLEVDTT LKSLSQQIEN IRSPEGSRKN 1250
PARTCRDLKM CHSDWKSGEY WIDPNQGCNL DAIKVFCNME TGETCVYPTQ 1300
PQVAQKNWYI SKNPKEKRHV WYGESMTDGF QFEYGGQGSD PADVAIQLTF 1350
LRLMSTEASQ NITYHCKNSV AYMDQQTGNL KKALLLQGSN EIEIRAEGNS 1400
RFTYSVTYDG CTSHTGAWGK TVIEYKTTKT SRLPIIDVAP LDVGAPDQEF 1450
GMDIGPVCFL 1460
Length:1,460
Mass (Da):138,762
Last modified:November 1, 1999 - v1
Checksum:i58E3674D2B570697
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti208 – 2081G → A in OI; severe. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF153062 mRNA. Translation: AAD34619.1.
RefSeqiNP_001003090.1. NM_001003090.1.
UniGeneiCfa.100.

Genome annotation databases

GeneIDi403651.
KEGGicfa:403651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF153062 mRNA. Translation: AAD34619.1 .
RefSeqi NP_001003090.1. NM_001003090.1.
UniGenei Cfa.100.

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9XSJ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403651.
KEGGi cfa:403651.

Organism-specific databases

CTDi 1277.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi Q9XSJ7.
KOi K06236.

Miscellaneous databases

NextBioi 20817156.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 12 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence of normal canine COL1A1 cDNA and identification of a heterozygous alpha1(I) collagen Gly208Ala mutation in a severe case of canine osteogenesis imperfecta."
    Campbell B.G., Wootton J.A.M., MacLeod J.N., Minor R.R.
    Arch. Biochem. Biophys. 384:37-46(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT OI ALA-208.
    Tissue: Skin.

Entry informationi

Entry nameiCO1A1_CANFA
AccessioniPrimary (citable) accession number: Q9XSJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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