ID CO9A2_MOUSE Reviewed; 688 AA.
AC Q07643;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Collagen alpha-2(IX) chain;
DE Flags: Precursor;
GN Name=Col9a2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8106484; DOI=10.1016/s0021-9258(17)37655-x;
RA Perala M., Elima K., Metsaranta M., Rosati R., de Crombrugghe B.,
RA Vuorio E.;
RT "The exon structure of the mouse alpha 2(IX) collagen gene shows unexpected
RT divergence from the chick gene.";
RL J. Biol. Chem. 269:5064-5071(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 521-668.
RC STRAIN=C57BL/6J;
RX PubMed=1543751; DOI=10.1016/0167-4781(92)90465-c;
RA Elima K., Metsaeranta M., Kallio J., Peraelae M., Eerola I., Garofalo S.,
RA de Crombrugghe B., Vuorio E.;
RT "Specific hybridization probes for mouse alpha 2(IX) and alpha 1(X)
RT collagen mRNAs.";
RL Biochim. Biophys. Acta 1130:78-80(1992).
CC -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the
CC eye.
CC -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha
CC 3(IX) chain (By similarity). The chains are linked to each other by
CC interchain disulfide bonds (By similarity). Trimers are also cross-
CC linked via hydroxylysines (By similarity).
CC {ECO:0000250|UniProtKB:C0HLN2}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Covalently linked to the telopeptides of type II collagen by
CC lysine-derived cross-links.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; Z22923; CAA80503.1; -; Genomic_DNA.
DR EMBL; X63014; CAA44742.1; -; mRNA.
DR CCDS; CCDS18599.1; -.
DR PIR; A53330; A53330.
DR AlphaFoldDB; Q07643; -.
DR SMR; Q07643; -.
DR ComplexPortal; CPX-2970; Collagen type IX trimer.
DR STRING; 10090.ENSMUSP00000030372; -.
DR GlyCosmos; Q07643; 2 sites, No reported glycans.
DR GlyGen; Q07643; 2 sites.
DR PhosphoSitePlus; Q07643; -.
DR MaxQB; Q07643; -.
DR PaxDb; 10090-ENSMUSP00000030372; -.
DR ProteomicsDB; 283550; -.
DR AGR; MGI:88466; -.
DR MGI; MGI:88466; Col9a2.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q07643; -.
DR PhylomeDB; Q07643; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR ChiTaRS; Col9a2; mouse.
DR PRO; PR:Q07643; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q07643; Protein.
DR GO; GO:0005594; C:collagen type IX trimer; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN ALPHA-1(X) CHAIN; 1.
DR Pfam; PF01391; Collagen; 7.
PE 2: Evidence at transcript level;
KW Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..688
FT /note="Collagen alpha-2(IX) chain"
FT /id="PRO_0000005838"
FT REGION 25..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..162
FT /note="Triple-helical region 4 (COL4)"
FT REGION 163..179
FT /note="Nonhelical region 4 (NC4)"
FT REGION 180..518
FT /note="Triple-helical region 3 (COL3)"
FT REGION 183..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..548
FT /note="Nonhelical region 3 (NC3)"
FT REGION 549..631
FT /note="Triple-helical region 2 (COL2)"
FT REGION 553..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..633
FT /note="Nonhelical region 2 (NC2)"
FT REGION 634..663
FT /note="Triple-helical region 1 (COL1)"
FT REGION 664..688
FT /note="Nonhelical region 1 (NC1)"
FT COMPBIAS 27..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P12108"
FT MOD_RES 182
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P12108"
FT CARBOHYD 168
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250|UniProtKB:P12108"
FT CARBOHYD 182
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P12108"
FT DISULFID 173
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 177
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT VARIANT 525
FT /note="V -> M (in strain: C57BL/6)"
FT VARIANT 610
FT /note="H -> R (in strain: C57BL/6)"
FT VARIANT 666
FT /note="A -> G (in strain: C57BL/6)"
SQ SEQUENCE 688 AA; 65321 MW; 7C7A73D2CD2A039F CRC64;
MTAVPAPRSL FVLLQVLWLA LAQIRGPPGE PGPPGPPGPP GVPGSDGIDG DKGPPGKVGP
PGSKGEPGKP GPDGPDGKPG IDGLMGAKGE PGPVGTPGVK GQPGLPGPPG LPGPGFAGPP
GPPGPVGLPG EIGTPGPKGD PGPEGPSGPP GPPGKPGRPG TIQGLEGSAD FLCPTNCPAG
VKGPQGLQGV KGHPGKRGIL GDPGRQGKPG PKGDVGASGE QGIPGPPGPQ GIRGYPGMAG
PKGEMGPRGY KGMVGSIGAA GPPGEEGPRG PPGEAGEKGD VGSQGARGPQ GITGPKGITG
PPGIDGKDGT PGIPGMKGSA GQVGRPGSPG HQGLAGVPGQ PGTKGGPGDK GEPGQQGLPG
VSGPPGKEGE PGPRGEIGPQ GIMGQKGDQG ERGPVGQPGP QGRQGPKGEQ GPPGIPGPQG
LPGIKGDKGS PGKTGPRGGV GDPGVAGLPG EKGEKGQSGE PGLKGQQGVR GETGYPGPSG
DIGAPGVQGY PGLPGPRGLV GDRGVPGQPG RQGVVGRAAS DQHIVDVVLK MIQEQLAEVA
VSAKREALGA AGMVGLPGPP GPPGYPGKQG PNGHPGPRGI PGIVGAVGQI GNTGPKGKRG
EKGDRGEMGH GHPGMPGPPG IPGLPGRPGQ AINGKDGDRG SPGAPGEAGR PGRPGPVGLP
GFCEPAACLG ASAYTSARLT EPGSIKGP
//
