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Q61245

- COBA1_MOUSE

UniProt

Q61245 - COBA1_MOUSE

Protein

Collagen alpha-1(XI) chain

Gene

Col11a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1623 – 16231CalciumBy similarity
    Metal bindingi1625 – 16251CalciumBy similarity
    Metal bindingi1626 – 16261Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1628 – 16281Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1631 – 16311CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cartilage condensation Source: MGI
    2. cartilage development Source: MGI
    3. chondrocyte development Source: MGI
    4. collagen fibril organization Source: MGI
    5. detection of mechanical stimulus involved in sensory perception of sound Source: Ensembl
    6. embryonic skeletal system morphogenesis Source: MGI
    7. heart morphogenesis Source: MGI
    8. inner ear morphogenesis Source: MGI
    9. proteoglycan metabolic process Source: MGI
    10. skeletal system morphogenesis Source: MGI
    11. tendon development Source: MGI
    12. ventricular cardiac muscle tissue morphogenesis Source: MGI
    13. visual perception Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XI) chain
    Gene namesi
    Name:Col11a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:88446. Col11a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Col11a1 are associated with chondrodysplasia, an autosomal recessive disease characterized by skeletal defects caused by abnormalities in the cartilage of limbs, ribs, mandibles and trachea.1 Publication

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Sequence AnalysisAdd
    BLAST
    Propeptidei35 – 511477N-terminal propeptideSequence AnalysisPRO_0000005777Add
    BLAST
    Chaini512 – 15611050Collagen alpha-1(XI) chainPRO_0000005778Add
    BLAST
    Propeptidei1562 – 1804243C-terminal propeptidePRO_0000005779Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi60 ↔ 242PROSITE-ProRule annotation
    Disulfide bondi181 ↔ 235PROSITE-ProRule annotation
    Modified residuei610 – 6101Allysine
    Modified residuei1450 – 14501Allysine
    Disulfide bondi1605 ↔ 1637PROSITE-ProRule annotation
    Disulfide bondi1628 – 1628InterchainPROSITE-ProRule annotation
    Glycosylationi1638 – 16381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1646 ↔ 1801PROSITE-ProRule annotation
    Disulfide bondi1712 ↔ 1755PROSITE-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.
    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ61245.
    PaxDbiQ61245.
    PRIDEiQ61245.

    PTM databases

    PhosphoSiteiQ61245.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61245.
    BgeeiQ61245.
    CleanExiMM_COL11A1.
    GenevestigatoriQ61245.

    Interactioni

    Subunit structurei

    Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ61245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini70 – 242173Laminin G-likeAdd
    BLAST
    Domaini440 – 48849Collagen-like 1Add
    BLAST
    Domaini527 – 58458Collagen-like 2Add
    BLAST
    Domaini567 – 62357Collagen-like 3Add
    BLAST
    Domaini728 – 78154Collagen-like 4Add
    BLAST
    Domaini1427 – 148256Collagen-like 5Add
    BLAST
    Domaini1481 – 153959Collagen-like 6Add
    BLAST
    Domaini1575 – 1803229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 417189Nonhelical regionAdd
    BLAST
    Regioni418 – 50689Triple-helical region (interrupted)Add
    BLAST
    Regioni507 – 5093Short nonhelical segment
    Regioni510 – 52718TelopeptideAdd
    BLAST
    Regioni528 – 15401013Triple-helical regionAdd
    BLAST
    Regioni1541 – 156121Nonhelical 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 6 collagen-like domains.Curated
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00710000106385.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    KOiK06236.
    OMAiHPGKEGQ.
    OrthoDBiEOG7XPZ4W.
    TreeFamiTF323987.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51461. NC1_FIB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q61245-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPWSRWKTK RWIWDLTIST LALTFLFQAR EVRGAAPVDI LKALDFHNSP     50
    VGISKTTGFC TNRKNSKDPD VAYRVTEEAQ ISAPTKQLFP GGIFPQDFSI 100
    LFTIKPKKGT QAFLLSLYNE HGIQQLGVEV GRSPVFLFED HTGKPTPENY 150
    PLFSTVNIAD GKWHRVAISV EKKTVTMIVD CKKKITKPLD RSERSIVDTN 200
    GIMVFGTRIL ETDVFQGDIQ QFLITGDPKA AYDYCDHYSP DCDLTSKAAQ 250
    AQEPHIDEYA PEDIIEYDYE YGETDYKEAE SVTEMPTFTE ETVAQTEANI 300
    VDDFQDYNYG TMEPYQTETP RRVSGSNEPN PVEEGFTEEY LTGEDYDVQR 350
    NTSEDILYGN KGVDGRDSDL LVDGDLGEYD FYEYKEYEER TTTSPNEEFG 400
    PGVPAETDFT ETSINGHGAY GEKGQKGEPA VVEPGMLVEG PPGPAGPAGL 450
    MGPPGLQGPS GLPGDPGDRG PPGRPGLPGA DGLPGPPGTM LMLPFRYGGD 500
    GSKGPTISAQ EAQAQAILQQ ARIALRGPPG PMGLTGRPGP VGGPGSAGAK 550
    GESGDPGPQG PRGVQGPPGP TGKPGKRGRP GADGGRGMPG ESGSKGDRGF 600
    DGLPGLPGDK GHRGERGPQG PPGLPGDDGM RGEDGEIGPR GLPGEAGPRG 650
    LLGPRGTPGP PGQPGIGGID GPQGPKGNMG PQGEPGPPGQ QGNPGPQGLP 700
    GPQGPIGPPG EKGPQGKPGL AGLPGADGPP GHPGKEGQSG EKGALGPPGP 750
    QGPIGYPGPR GVKGADGVRG LKGSKGEKGE DGFPGFKGDM GLKGDRGEVG 800
    QVGPRGEDGP EGPKGRAGPT GDPGPSGQAG EKGKLGVPGL PGYPGRQGPK 850
    GSTGFPGFPG ANGEKGARGI AGKPGPRGQR GPTGPRGSRG ARGPTGKPGP 900
    KGTSGGDGPP GPPGERGPQG PQGPVGFPGP KGPPGPAGKD GLPGHPGQRG 950
    ETGFQGKTGP PGPGGVVGPQ GPTGETGPIG ERGHPGPPGP PGEQGLPGAA 1000
    GKEGAKGDPG PQGISGKDGP AGIRGFPGER GLPGAQGAPG LKGGEGPQGP 1050
    QGPVGSPGER GSAGTAGPIG LPGRPGPQGP PGPAGEKGAP GEKGPQGPAG 1100
    RDGVQGPVGL PGPAGPAGSP GEDGDKGEIG EPGQKGSKGD KGENGPPGPP 1150
    GLQGPVGAPG IAGGDGEPGP RGQQGMFGQK GDEGARGFPG LPGPIGLQGL 1200
    PGPPGEKGEN GDVGPMGPPG PPGPRGPQGP NGADGPQGPP GSIGSVGVVG 1250
    DKGEPGEAGN PGPPGEAGSG GLKGERGEKG EAGPPGAAGP AGIKGPPGDD 1300
    GPKGNPGPVG FPGDPGPPGE PGPAGQDGVG GDKGEDGDPG QPGPPGPSGE 1350
    AGPPGPPGKR GPPGASGSEG RQGEKGAKGE AGAEGPPGKT GPVGPQGPSG 1400
    KPGPEGLRGI PGPVGEQGLP GAAGQDGPPG PLGPPGLPGL KGDPGSKGEK 1450
    GHPGLIGLIG PPGEQGEKGD RGLPGTQGSP GAKGDGGIPG PAGPIGPPGP 1500
    PGLPGPAGPK GNKGSSGPTG QKGDSGMPGP PGPPGPPGEV IQPLPILSPK 1550
    KTRRHTESIQ GDAGDNILDY SDGMEEIFGS LNSLKQDIEH MKFPMGTQTN 1600
    PARTCKDLQL SHPDFPDGEY WIDPNQGCSG DSFKVYCNFT AGGETCIYPD 1650
    KKSEGVRISS WPKEKPGSWY SEFKRGKLLS YLDVEGNSIN MVQMTFLKLL 1700
    TASARQNFTY NCHQSAAWYD VLSGSYDKAL RFLGSNDEEM SYENNPHIKA 1750
    LYDGCASRKG YEKTVIEINT PKIDQVPIID VMINDFGDQN QKFGFEVGPA 1800
    CFLG 1804
    Length:1,804
    Mass (Da):181,032
    Last modified:July 27, 2011 - v2
    Checksum:i918C3D4B8C964470
    GO
    Isoform Short (identifier: Q61245-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-413: Missing.

    Show »
    Length:1,719
    Mass (Da):171,401
    Checksum:i82E461C5F6246038
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121T → A in BAA07367. (PubMed:8530046)Curated
    Sequence conflicti370 – 3701L → V in BAA07367. (PubMed:8530046)Curated
    Sequence conflicti547 – 5471A → T in BAA07367. (PubMed:8530046)Curated
    Sequence conflicti696 – 6961P → S in BAA07367. (PubMed:8530046)Curated
    Sequence conflicti1065 – 10651T → A in BAA07367. (PubMed:8530046)Curated
    Sequence conflicti1476 – 14761T → S in BAA07367. (PubMed:8530046)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei329 – 41385Missing in isoform Short. CuratedVSP_001147Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38162 mRNA. Translation: BAA07367.1.
    BC052161 mRNA. Translation: AAH52161.1.
    S74574 mRNA. Translation: AAB33439.1.
    CCDSiCCDS17778.1. [Q61245-1]
    PIRiA55648.
    RefSeqiNP_031755.2. NM_007729.2. [Q61245-1]
    UniGeneiMm.209715.

    Genome annotation databases

    EnsembliENSMUST00000092155; ENSMUSP00000089793; ENSMUSG00000027966. [Q61245-1]
    GeneIDi12814.
    KEGGimmu:12814.
    UCSCiuc008rbk.1. mouse. [Q61245-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38162 mRNA. Translation: BAA07367.1 .
    BC052161 mRNA. Translation: AAH52161.1 .
    S74574 mRNA. Translation: AAB33439.1 .
    CCDSi CCDS17778.1. [Q61245-1 ]
    PIRi A55648.
    RefSeqi NP_031755.2. NM_007729.2. [Q61245-1 ]
    UniGenei Mm.209715.

    3D structure databases

    ProteinModelPortali Q61245.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q61245.

    Proteomic databases

    MaxQBi Q61245.
    PaxDbi Q61245.
    PRIDEi Q61245.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092155 ; ENSMUSP00000089793 ; ENSMUSG00000027966 . [Q61245-1 ]
    GeneIDi 12814.
    KEGGi mmu:12814.
    UCSCi uc008rbk.1. mouse. [Q61245-1 ]

    Organism-specific databases

    CTDi 1301.
    MGIi MGI:88446. Col11a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00710000106385.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    KOi K06236.
    OMAi HPGKEGQ.
    OrthoDBi EOG7XPZ4W.
    TreeFami TF323987.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    NextBioi 282270.
    PROi Q61245.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61245.
    Bgeei Q61245.
    CleanExi MM_COL11A1.
    Genevestigatori Q61245.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51461. NC1_FIB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coding sequence and alternative splicing of the mouse alpha 1(XI) collagen gene (Col11a1)."
      Yoshioka H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Andrikopoulos K., Ramirez F.
      Genomics 28:337-340(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING.
      Tissue: Embryo.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Embryo.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-198, DISEASE.
      Strain: C57BL/6.

    Entry informationi

    Entry nameiCOBA1_MOUSE
    AccessioniPrimary (citable) accession number: Q61245
    Secondary accession number(s): Q64047, Q80WR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3