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P05539

- CO2A1_RAT

UniProt

P05539 - CO2A1_RAT

Protein

Collagen alpha-1(II) chain

Gene

Col2a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei113 – 1142Cleavage; by procollagen N-endopeptidaseBy similarity
    Sitei1173 – 11742Cleavage; by procollagen C-endopeptidaseBy similarity
    Metal bindingi1233 – 12331CalciumBy similarity
    Metal bindingi1235 – 12351CalciumBy similarity
    Metal bindingi1236 – 12361Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1238 – 12381Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1241 – 12411CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cartilage development Source: RGD
    2. cartilage development involved in endochondral bone morphogenesis Source: RGD
    3. cellular response to mechanical stimulus Source: RGD
    4. cellular response to nicotine Source: RGD
    5. cellular response to parathyroid hormone stimulus Source: RGD
    6. cellular response to peptide hormone stimulus Source: RGD
    7. cellular response to retinoic acid Source: RGD
    8. cellular response to tumor necrosis factor Source: RGD
    9. cellular response to vitamin E Source: RGD
    10. chondrocyte differentiation Source: RGD
    11. growth plate cartilage development Source: RGD
    12. response to fibroblast growth factor Source: RGD
    13. response to mechanical stimulus Source: RGD
    14. response to X-ray Source: RGD

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(II) chain
    Alternative name(s):
    Alpha-1 type II collagen
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Col2a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2375. Col2a1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type II trimer Source: RGD
    2. cytoplasm Source: RGD

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 11388N-terminal propeptideBy similarityPRO_0000005735Add
    BLAST
    Chaini114 – 11731060Collagen alpha-1(II) chainPRO_0000005736Add
    BLAST
    Chaini1174 – 1419246ChondrocalcinBy similarityPRO_0000043407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 12215-hydroxylysineBy similarity
    Glycosylationi122 – 1221O-linked (Gal...)By similarity
    Modified residuei219 – 21915-hydroxylysineBy similarity
    Glycosylationi219 – 2191O-linked (Gal...)By similarity
    Modified residuei231 – 23115-hydroxylysineBy similarity
    Glycosylationi231 – 2311O-linked (Gal...)By similarity
    Modified residuei240 – 24015-hydroxylysineBy similarity
    Glycosylationi240 – 2401O-linked (Gal...)By similarity
    Modified residuei306 – 30615-hydroxylysineBy similarity
    Glycosylationi306 – 3061O-linked (Gal...)By similarity
    Modified residuei540 – 54015-hydroxylysineBy similarity
    Glycosylationi540 – 5401O-linked (Gal...)By similarity
    Modified residuei552 – 55215-hydroxylysineBy similarity
    Glycosylationi552 – 5521O-linked (Gal...)By similarity
    Modified residuei602 – 60213-hydroxyproline; partial1 Publication
    Modified residuei839 – 83913-hydroxyproline; partial1 Publication
    Modified residuei1076 – 107613-hydroxyproline; partial1 Publication
    Modified residuei1118 – 111813-hydroxyproline1 Publication
    Modified residuei1133 – 113313-hydroxyproline; partial1 Publication
    Modified residuei1139 – 113913-hydroxyproline; partial1 Publication
    Modified residuei1145 – 114513-hydroxyproline; partial1 Publication
    Disulfide bondi1215 ↔ 1247PROSITE-ProRule annotation
    Disulfide bondi1221 – 1221Interchain (with C-1238)PROSITE-ProRule annotation
    Disulfide bondi1238 – 1238Interchain (with C-1221)PROSITE-ProRule annotation
    Disulfide bondi1255 ↔ 1417PROSITE-ProRule annotation
    Glycosylationi1320 – 13201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1325 ↔ 1370PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-602, Pro-839, Pro-1076, Pro-1133, Pro-1139 and Pro-1145 by LEPREL1.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP05539.
    PRIDEiP05539.

    Expressioni

    Tissue specificityi

    Expressed in chondrocytes.1 Publication

    Gene expression databases

    GenevestigatoriP05539.

    Interactioni

    Subunit structurei

    Homotrimers of alpha 1(II) chains.

    Protein-protein interaction databases

    IntActiP05539. 1 interaction.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1185 – 1419235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 11461014Triple-helical regionAdd
    BLAST
    Regioni1147 – 117327Nonhelical 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

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    KOiK06236.
    PhylomeDBiP05539.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 4 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.

    P05539-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIRLGAPQSL VLLTLLIATV LQCQGQDARK LGPKGQKGEP GDIKDIIGPK     50
    GPPGPQGPAG EQGPRGDRGD KGERGAPGPR GRDGEPGTPG NPGPPGPPGP 100
    PGPPGLGGGN FAAQMAGGFD EKAGGAQMGV MQGPMGPMGP RGPPGPAGAP 150
    GPQGFQGNPG EPGEPGVSGP IGPRGPPGPA GKPGDDGEAG KPGKAGERGL 200
    PGPQGARGFP GTPGLPGVKG HRGYPGLDGA KGEAGAPGVK GESGSPGENG 250
    SPGPMGPRGL PGERGRTGPA GAAGARGNDG QPGPAGPPGP VGPAGGPGFL 300
    GAPGAKGEAG PTGARGPEGA QGSRGEPGNP GSPGPAGASG NPGTDGIPGA 350
    KGSAGAPGIA GAPGFPGPRG PPGPQGATGP LGPKGQTGEP GIAGFKGEQG 400
    PKGETGPAGP QGAPGPAGEE GKRGARGEPG GAGPIGPPGE RGAPGNRGFP 450
    GQDGLAGPKG APGERGPSGL AGPKGANGDP GRPGEPGLPG ARGLTGRPGD 500
    AGPQGKVGPS GAPGEDGRPG PPGPQGARGQ PGVMGFPGPK GANGEPGKAG 550
    EKGLAGAPGL RGLPGKDGET GAAGPPGPSG PAGERGEQGA PGPSGFQGLP 600
    GPPGPPGEGG KQGDQGIPGE AGAPGLVGPR GERGFPGERG SPGAQGLQGP 650
    RGLPGTPGTD GPKGAAGPDG PPGAQGPPGL QGMPGERGAA GIAGPKGDRG 700
    DVGEKGPEGA PGKDGGRGLT GPIGPPGPAG ANGEKGEVGP PGPSGSTGAR 750
    GAPGERGETG PPGPAGFAGP PGADGQPGAK GDQGEAGQKG DAGAPGPQGP 800
    SGAPGPQGPT GVTGPKGARG AQGPPGATGF PGAAGRVGPP GSNGNPGPAG 850
    PPGPAGKDGP KGARGDTGAP GRAGDPGLQG PAGAPGEKGE PGDDGPSGSD 900
    GPPGPQGLAG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG APGASGDRGP 950
    PGPVGPPGLT GPAGEPGREG SPGADGPPGR DGAAGVKGDR GETGALGAPG 1000
    APGPPGSPGP AGPTGKQGDR GEAGAQGPMG PSGPAGARGI AGPQGPRGDK 1050
    GEAGEPGERG LKGHRGFTGL QGLPGPPGPS GDQGTSGPAG PSGPRGPPGP 1100
    VGPSGKDGSN GIPGPIGPPG PRGRSGETGP AGPPGNPGPP GPPGPPGPGI 1150
    DMSAFAGLGQ REKGPDPLQY MRADEADSTL RQHDVEVDAT LKSLNNQIES 1200
    IRSPDGSRKN PARTCQDLKL CHPEWKSGDY WIDPNQGCTL DAMKVFCNME 1250
    TGESCVYPNP ATVPRKNWWS SKSKEKKHIW FGETMNGGFH FSYGDGNLAP 1300
    NTANVQMTFL RLLSTEGSQN ITYHCKNSIA YLDEAAGNLK KALLIQGSND 1350
    VEMRAEGNSR FTYTALKDGC TKHTGKWGKT IIEYRSQKTS RLPIVDIAPM 1400
    DIGGPDQEFG VDIGPVCFL 1419
    Length:1,419
    Mass (Da):134,570
    Last modified:December 6, 2005 - v2
    Checksum:iB7C63B77819CE50B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211E → Q in AAA40919. (PubMed:6094525)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L48440 mRNA. Translation: AAA79780.1.
    K02804 mRNA. Translation: AAA40919.1.
    M10613 Genomic DNA. Translation: AAA40920.1.
    X79816 mRNA. Translation: CAA56213.1.
    PIRiA05152.
    I60384.
    RefSeqiNP_037061.1. NM_012929.1.
    UniGeneiRn.10124.

    Genome annotation databases

    GeneIDi25412.
    KEGGirno:25412.
    UCSCiRGD:2375. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L48440 mRNA. Translation: AAA79780.1 .
    K02804 mRNA. Translation: AAA40919.1 .
    M10613 Genomic DNA. Translation: AAA40920.1 .
    X79816 mRNA. Translation: CAA56213.1 .
    PIRi A05152.
    I60384.
    RefSeqi NP_037061.1. NM_012929.1.
    UniGenei Rn.10124.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P05539. 1 interaction.

    Proteomic databases

    PaxDbi P05539.
    PRIDEi P05539.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25412.
    KEGGi rno:25412.
    UCSCi RGD:2375. rat.

    Organism-specific databases

    CTDi 1280.
    RGDi 2375. Col2a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    KOi K06236.
    PhylomeDBi P05539.

    Miscellaneous databases

    NextBioi 606543.
    PROi P05539.

    Gene expression databases

    Genevestigatori P05539.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 4 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. "Complete rat type II collagen cDNA sequence."
      Urabe K., Sarkar G., Bolander M.E.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    2. "Isolation and characterization of a cDNA clone for the amino-terminal portion of the pro-alpha 1(II) chain of cartilage collagen."
      Kohno K., Martin G.R., Yamada Y.
      J. Biol. Chem. 259:13668-13673(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122.
    3. "Structure of the promoter of the rat type II procollagen gene."
      Kohno K., Sullivan M., Yamada Y.
      J. Biol. Chem. 260:4441-4447(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 370-422.
      Strain: DA.
      Tissue: Cartilage.
    5. "A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
      Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
      J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-602; PRO-839; PRO-1076; PRO-1118; PRO-1133; PRO-1139 AND PRO-1145, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCO2A1_RAT
    AccessioniPrimary (citable) accession number: P05539
    Secondary accession number(s): Q63123, Q63565, Q78DY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 111 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3