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Q9XSJ7

- CO1A1_CANFA

UniProt

Q9XSJ7 - CO1A1_CANFA

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

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

    Sites

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

    GO - Molecular functioni

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

    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

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

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

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By 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 acidBy similarity
    Modified residuei166 – 1661AllysineBy similarity
    Modified residuei261 – 26115-hydroxylysine; alternateBy similarity
    Glycosylationi261 – 2611O-linked (Gal...); alternateBy similarity
    Modified residuei1160 – 116013-hydroxyprolineBy similarity
    Disulfide bondi1255 ↔ 1287PROSITE-ProRule annotation
    Disulfide bondi1261 – 1261Interchain (with C-1278)PROSITE-ProRule annotation
    Disulfide bondi1278 – 1278Interchain (with C-1261)PROSITE-ProRule annotation
    Disulfide bondi1295 ↔ 1458PROSITE-ProRule annotation
    Glycosylationi1361 – 13611N-linked (GlcNAc...)By similarity
    Disulfide bondi1366 ↔ 1411PROSITE-ProRule annotation

    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.By similarity

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 9259VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1225 – 1460236Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    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 siteSequence Analysis
    Motifi1089 – 10913Cell attachment siteSequence Analysis

    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

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    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: October 1, 2014
    This is version 91 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