Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01149

- CO1A2_MOUSE

UniProt

Q01149 - CO1A2_MOUSE

Protein

Collagen alpha-2(I) chain

Gene

Col1a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1187 – 11871CalciumBy similarity
    Metal bindingi1189 – 11891CalciumBy similarity
    Metal bindingi1190 – 11901Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1192 – 11921Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1195 – 11951CalciumBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: MGI
    4. SMAD binding Source: MGI

    GO - Biological processi

    1. blood vessel development Source: Ensembl
    2. cellular response to amino acid stimulus Source: MGI
    3. collagen fibril organization Source: Ensembl
    4. protein heterotrimerization Source: MGI
    5. regulation of blood pressure Source: Ensembl
    6. Rho protein signal transduction Source: Ensembl
    7. skeletal system development Source: Ensembl
    8. skin morphogenesis Source: Ensembl
    9. transforming growth factor beta receptor signaling pathway Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196515. Crosslinking of collagen fibrils.
    REACT_196581. Scavenging by Class A Receptors.
    REACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(I) chain
    Alternative name(s):
    Alpha-2 type I collagen
    Gene namesi
    Name:Col1a2
    Synonyms:Cola2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:88468. Col1a2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen trimer Source: MGI
    2. collagen type I trimer Source: MGI
    3. extracellular space Source: Ensembl
    4. extracellular vesicular exosome Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 8563N-terminal propeptideBy similarityPRO_0000005807Add
    BLAST
    Chaini86 – 11081023Collagen alpha-2(I) chainPRO_0000005808Add
    BLAST
    Propeptidei1109 – 1372264C-terminal propeptideBy similarityPRO_0000005809Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861Pyrrolidone carboxylic acidBy similarity
    Modified residuei90 – 901AllysineBy similarity
    Disulfide bondi1169 ↔ 1201PROSITE-ProRule annotation
    Disulfide bondi1209 ↔ 1370PROSITE-ProRule annotation
    Glycosylationi1273 – 12731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1278 ↔ 1323PROSITE-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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiQ01149.
    PaxDbiQ01149.
    PRIDEiQ01149.

    PTM databases

    PhosphoSiteiQ01149.

    Expressioni

    Tissue specificityi

    Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

    Gene expression databases

    ArrayExpressiQ01149.
    BgeeiQ01149.
    CleanExiMM_COL1A2.
    GenevestigatoriQ01149.

    Interactioni

    Subunit structurei

    Trimers of one alpha 2(I) and two alpha 1(I) chains.

    Protein-protein interaction databases

    IntActiQ01149. 1 interaction.
    MINTiMINT-4091346.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01149.
    SMRiQ01149. Positions 1158-1371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1139 – 1372234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    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

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    InParanoidiQ01149.
    KOiK06236.
    OMAiKNGDKGH.
    OrthoDBiEOG7TJ3HH.
    PhylomeDBiQ01149.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    [Graphical view]
    PROSITEiPS51461. NC1_FIB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q01149-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSFVDTRTL LLLAVTSCLA TCQYLQSGSV RKGPTGDRGP RGQRGPAGPR     50
    GRDGVDGPMG PPGPPGSPGP PGSPAPPGLT GNFAAQYSDK GVSSGPGPMG 100
    LMGPRGPPGA VGAPGPQGFQ GPAGEPGEPG QTGPAGPRGP AGSPGKAGED 150
    GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP GFKGVKGHSG MDGLKGQPGA 200
    QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR GSDGSVGPVG 250
    PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE VGLPGLSGPV 300
    GPPGNPGTNG LTGAKGATGL PGVAGAPGLP GPRGIPGPAG AAGATGARGL 350
    VGEPGPAGSK GESGNKGEPG SVGAQGPPGP SGEEGKRGSP GEAGSAGPAG 400
    PPGLRGSPGS RGLPGADGRA GVMGPPGNRG STGPAGIRGP NGDAGRPGEP 450
    GLMGPRGLPG SPGNVGPSGK EGPVGLPGID GRPGPIGPAG PRGEAGNIGF 500
    PGPKGPSGDP GKPGERGHPG LAGARGAPGP DGNNGAQGPP GPQGVQGGKG 550
    EQGPAGPPGF QGLPGPSGTT GEVGKPGERG LPGEFGLPGP AGPRGERGTP 600
    GESGAAGPSG PIGSRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE 650
    RGAAGIPGGK GEKGETGLRG DTGNTGRDGA RGIPGAVGAP GPAGASGDRG 700
    EAGAAGPSGP AGPRGSPGER GEVGPAGPNG FAGPAGAAGQ PGAKGEKGTK 750
    GPKGENGIVG PTGSVGAAGP SGPNGPPGPV GSRGDGGPPG MTGFPGAAGR 800
    TGPPGPSGIA GPPGPPGAAG KEGIRGPRGD QGPVGRTGET GASGPPGFVG 850
    EKGPSGEPGT AGAPGTAGPQ GLLGAPGILG LPGSRGERGL PGIAGALGEP 900
    GPLGISGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH 950
    KGERGYPGSI GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG 1000
    PRGPSGPQGI RGDKGEPGDK GHRGLPGLKG YSGLQGLPGL AGLHGDQGAP 1050
    GPVGPAGPRG PAGPSGPVGK DGRSGQPGPV GPAGVRGSQG SQGPAGPPGP 1100
    PGPPGPPGVS GGGYDFGFEG DFYRADQPRS QPSLRPKDYE VDATLKSLNN 1150
    QIETLLTPEG SRKNPARTCR DLRLSHPEWN SDYYWIDPNQ GCTMDAIKVY 1200
    CDFSTGETCI QAQPVNTPAK NSYSRAQANK HVWLGETING GSQFEYNVEG 1250
    VSSKEMATQL AFMRLLANRA SQNITYHCKN SIAYLDEETG SLNKAVLLQG 1300
    SNDVELVAEG NSRFTYSVLV DGCSKKTNEW GKTIIEYKTN KPSRLPFLDI 1350
    APLDIGGADQ EFRVEVGPVC FK 1372
    Length:1,372
    Mass (Da):129,557
    Last modified:August 29, 2001 - v2
    Checksum:i0D17DF5D6C1452D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151V → A in AAA37331. (PubMed:3039494)Curated
    Sequence conflicti1167 – 11671R → TT in CAA41205. (PubMed:1505972)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58251 mRNA. Translation: CAA41205.1.
    BC007158 mRNA. Translation: AAH07158.1.
    BC042503 mRNA. Translation: AAH42503.2.
    K01832 Genomic DNA. Translation: AAA37331.1.
    CCDSiCCDS39420.1.
    PIRiA43291.
    RefSeqiNP_031769.2. NM_007743.2.
    UniGeneiMm.277792.

    Genome annotation databases

    EnsembliENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661.
    GeneIDi12843.
    KEGGimmu:12843.
    UCSCiuc009avm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58251 mRNA. Translation: CAA41205.1 .
    BC007158 mRNA. Translation: AAH07158.1 .
    BC042503 mRNA. Translation: AAH42503.2 .
    K01832 Genomic DNA. Translation: AAA37331.1 .
    CCDSi CCDS39420.1.
    PIRi A43291.
    RefSeqi NP_031769.2. NM_007743.2.
    UniGenei Mm.277792.

    3D structure databases

    ProteinModelPortali Q01149.
    SMRi Q01149. Positions 1158-1371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q01149. 1 interaction.
    MINTi MINT-4091346.

    PTM databases

    PhosphoSitei Q01149.

    Proteomic databases

    MaxQBi Q01149.
    PaxDbi Q01149.
    PRIDEi Q01149.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031668 ; ENSMUSP00000031668 ; ENSMUSG00000029661 .
    GeneIDi 12843.
    KEGGi mmu:12843.
    UCSCi uc009avm.1. mouse.

    Organism-specific databases

    CTDi 1278.
    MGIi MGI:88468. Col1a2.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    InParanoidi Q01149.
    KOi K06236.
    OMAi KNGDKGH.
    OrthoDBi EOG7TJ3HH.
    PhylomeDBi Q01149.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_196515. Crosslinking of collagen fibrils.
    REACT_196581. Scavenging by Class A Receptors.
    REACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    ChiTaRSi COL1A2. mouse.
    NextBioi 282380.
    PROi Q01149.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01149.
    Bgeei Q01149.
    CleanExi MM_COL1A2.
    Genevestigatori Q01149.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    [Graphical view ]
    PROSITEi PS51461. NC1_FIB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a full-length cDNA for the murine pro alpha 2(I) collagen chain: comparison of the derived primary structure with human pro alpha 2(I) collagen."
      Phillips C.L., Morgan A.L., Lever L.W., Wenstrup R.J.
      Genomics 13:1345-1346(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Calvaria.
    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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    3. "Construction of a full-length murine pro alpha 2(I) collagen cDNA by the polymerase chain reaction."
      Phillips C.L., Lever L.W., Pinnell S.R., Quarles L.D., Wenstrup R.J.
      J. Invest. Dermatol. 97:980-984(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-110.
      Tissue: Calvaria.
    4. "Identification of a cell-specific transcriptional enhancer in the first intron of the mouse alpha 2 (type I) collagen gene."
      Rossi P., de Crombrugghe B.
      Proc. Natl. Acad. Sci. U.S.A. 84:5590-5594(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.

    Entry informationi

    Entry nameiCO1A2_MOUSE
    AccessioniPrimary (citable) accession number: Q01149
    Secondary accession number(s): Q8CGA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 128 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