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Q91717

- CO2A1_XENLA

UniProt

Q91717 - CO2A1_XENLA

Protein

Collagen alpha-1(II) chain

Gene

col2a1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei183 – 1842Cleavage; by procollagen N-endopeptidaseBy similarity
    Sitei1243 – 12442Cleavage; by procollagen C-endopeptidaseBy similarity
    Metal bindingi1300 – 13001CalciumBy similarity
    Metal bindingi1302 – 13021CalciumBy similarity
    Metal bindingi1303 – 13031Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1305 – 13051Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1308 – 13081CalciumBy 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(II) chain
    Alternative name(s):
    Alpha-1 type II collagen
    Gene namesi
    Name:col2a1
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6252613. col2a1.

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Propeptidei27 – 183157N-terminal propeptideBy similarityPRO_0000286178Add
    BLAST
    Chaini184 – 12431060Collagen alpha-1(II) chainPRO_0000286179Add
    BLAST
    Propeptidei1244 – 1486243C-terminal propeptideBy similarityPRO_0000286180Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi1282 ↔ 1314PROSITE-ProRule annotation
    Disulfide bondi1288 – 1288Interchain (with C-1305)PROSITE-ProRule annotation
    Disulfide bondi1305 – 1305Interchain (with C-1288)PROSITE-ProRule annotation
    Disulfide bondi1322 ↔ 1484PROSITE-ProRule annotation
    Glycosylationi1387 – 13871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1392 ↔ 1437PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Expressioni

    Developmental stagei

    Initially, the transcripts are localized to notochord, somites, and the dorsal region of the lateral plate mesoderm. At later stages of development and parallel to increased mRNA accumulation, collagen expression becomes progressively more confined to chondrogenic regions of the tadpole.1 Publication

    Interactioni

    Subunit structurei

    Homotrimers of alpha 1(II) chains.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ91717.
    SMRiQ91717. Positions 34-101.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 9459VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1252 – 1486235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 12161014Triple-helical regionAdd
    BLAST
    Regioni1217 – 124327Nonhelical region (C-terminal)Add
    BLAST

    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

    HOVERGENiHBG004933.
    KOiK06236.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 9 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.

    Q91717-1 [UniParc]FASTAAdd to Basket

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    MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV     50
    WKPEPCQICV CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST 100
    SSGQGVLKGQ KGEPGDIKDV LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA 150
    PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN FAAQMTGGFD EKAGGAQMGV 200
    MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP MGPRGPPGPS 250
    GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA 300
    KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG 350
    LPGPAGPPGP VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP 400
    GSPGPAGASG NPGTDGIPGA KGSSGGPGIA GAPGFPGPRG PPGPQGATGP 450
    LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP QGAPGPAGEE GKRGARGEPG 500
    AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL GGPKGGNGDP 550
    GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ 600
    PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG 650
    PAGERGEQGP PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR 700
    GERGFPGERG SSGPQGLQGP RGLPGTPGTD GPKGASGPSG PNGAQGPPGL 750
    QGMPGERGAA GISGPKGDRG DTGEKGPEGA SGKDGSRGLT GPIGPPGPAG 800
    PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP PGADGQSGLK 850
    GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF 900
    PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG 950
    AAGAPGEKGE PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP 1000
    GPSGEPGKQG GPGSSGDRGP PGPVGPPGLT GPSGEPGREG NPGSDGPPGR 1050
    DGATGIKGDR GETGPLGAPG APGAPGAPGS VGPTGKQGDR GESGPQGPLG 1100
    PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL QGLPGPPGSA 1150
    GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP 1200
    SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL 1250
    PVDVEATLKS LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID 1300
    PNQGCTVDAI KVFCDMETGE TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE 1350
    TINGGFQFSY GDDSSAPNTA NIQMTFLRLL STDASQNITY HCKNSIAFMD 1400
    EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH TGKWSKTVIE 1450
    YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL 1486
    Length:1,486
    Mass (Da):142,263
    Last modified:May 1, 2007 - v2
    Checksum:i02C18E5F5807100E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti456 – 4561Q → E in AAA49678. (PubMed:1918153)Curated
    Sequence conflicti1287 – 12871L → I in AAA49678. (PubMed:1918153)Curated
    Sequence conflicti1315 – 13151D → N in AAA49678. (PubMed:1918153)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63595 mRNA. Translation: AAA49678.1.
    BC048221 mRNA. Translation: AAH48221.1.
    BC111515 mRNA. Translation: AAI11516.1.
    PIRiA40333.
    B40333.
    RefSeqiNP_001081258.1. NM_001087789.1.
    UniGeneiXl.606.

    Genome annotation databases

    GeneIDi397738.
    KEGGixla:397738.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63595 mRNA. Translation: AAA49678.1 .
    BC048221 mRNA. Translation: AAH48221.1 .
    BC111515 mRNA. Translation: AAI11516.1 .
    PIRi A40333.
    B40333.
    RefSeqi NP_001081258.1. NM_001087789.1.
    UniGenei Xl.606.

    3D structure databases

    ProteinModelPortali Q91717.
    SMRi Q91717. Positions 34-101.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397738.
    KEGGi xla:397738.

    Organism-specific databases

    CTDi 1280.
    Xenbasei XB-GENE-6252613. col2a1.

    Phylogenomic databases

    HOVERGENi HBG004933.
    KOi K06236.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 9 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. "Expression of two nonallelic type II procollagen genes during Xenopus laevis embryogenesis is characterized by stage-specific production of alternatively spliced transcripts."
      Su M.W., Suzuki H.R., Bieker J.J., Solursh M., Ramirez F.
      J. Cell Biol. 115:565-575(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiCO2A1_XENLA
    AccessioniPrimary (citable) accession number: Q91717
    Secondary accession number(s): Q7ZTI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3