CO9A1_MOUSE
ID CO9A1_MOUSE Reviewed; 921 AA.
AC Q05722; Q61269; Q61270; Q61433; Q61940;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Collagen alpha-1(IX) chain;
DE Flags: Precursor;
GN Name=Col9a1;
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 [MRNA] (ISOFORM LONG).
RX PubMed=8305476; DOI=10.1016/0167-4838(94)90033-7;
RA Abe N., Yoshioka H., Inoue H., Ninomiya Y.;
RT "The complete primary structure of the long form of mouse alpha 1(IX)
RT collagen chain and its expression during limb development.";
RL Biochim. Biophys. Acta 1204:61-67(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Embryo;
RX PubMed=8061915; DOI=10.1016/0945-053x(94)90024-8;
RA Rokos I., Muragaki Y., Warman M., Olsen B.R.;
RT "Assembly and sequencing of a cDNA covering the entire mouse alpha 1(IX)
RT collagen chain.";
RL Matrix Biol. 14:1-8(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 759-906.
RX PubMed=2054384; DOI=10.1016/0167-4781(91)90014-d;
RA Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
RT "Specific hybridization probes for mouse type I, II, III and IX collagen
RT mRNAs.";
RL Biochim. Biophys. Acta 1089:241-243(1991).
RN [4]
RP ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Liver, and Spleen;
RX PubMed=1690886; DOI=10.1073/pnas.87.7.2400;
RA Muragaki Y., Nishimura I., Henney A., Ninomiya Y., Olsen B.R.;
RT "The alpha 1 (IX) collagen gene gives rise to two different transcripts in
RT both mouse embryonic and human fetal RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2400-2404(1990).
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=Q05722-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q05722-2; Sequence=VSP_001143, VSP_001144;
CC -!- DOMAIN: Each subunit is composed of three triple-helical domains
CC interspersed with non-collagenous domains. The globular domain at the
CC N-terminus of type IX collagen molecules represents the NC4 domain
CC which may participate in electrostatic interactions with polyanionic
CC glycosaminoglycans in cartilage.
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; D17511; BAA04463.1; -; mRNA.
DR EMBL; L12215; AAA21834.1; -; mRNA.
DR EMBL; X57984; CAA41049.1; -; Genomic_DNA.
DR EMBL; M32136; AAA53523.1; -; Genomic_DNA.
DR EMBL; M32132; AAA53523.1; JOINED; Genomic_DNA.
DR EMBL; M32136; AAA53522.1; -; Genomic_DNA.
DR EMBL; M32134; AAA53522.1; JOINED; Genomic_DNA.
DR CCDS; CCDS35527.1; -. [Q05722-1]
DR PIR; A35980; A35980.
DR PIR; S40495; S40495.
DR PIR; S42617; S42617.
DR RefSeq; NP_031766.3; NM_007740.3.
DR AlphaFoldDB; Q05722; -.
DR SMR; Q05722; -.
DR ComplexPortal; CPX-2970; Collagen type IX trimer.
DR STRING; 10090.ENSMUSP00000051579; -.
DR iPTMnet; Q05722; -.
DR PhosphoSitePlus; Q05722; -.
DR MaxQB; Q05722; -.
DR PaxDb; Q05722; -.
DR PRIDE; Q05722; -.
DR ProteomicsDB; 283475; -. [Q05722-1]
DR ProteomicsDB; 283476; -. [Q05722-2]
DR DNASU; 12839; -.
DR GeneID; 12839; -.
DR KEGG; mmu:12839; -.
DR CTD; 1297; -.
DR MGI; MGI:88465; Col9a1.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q05722; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; Q05722; -.
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 BioGRID-ORCS; 12839; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Col9a1; mouse.
DR PRO; PR:Q05722; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q05722; protein.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005594; C:collagen type IX trimer; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060349; P:bone morphogenesis; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0035988; P:chondrocyte proliferation; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 9.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Disulfide bond; Extracellular matrix;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..921
FT /note="Collagen alpha-1(IX) chain"
FT /id="PRO_0000005766"
FT DOMAIN 50..244
FT /note="Laminin G-like"
FT DOMAIN 269..325
FT /note="Collagen-like 1"
FT DOMAIN 326..356
FT /note="Collagen-like 2"
FT DOMAIN 358..403
FT /note="Collagen-like 3"
FT DOMAIN 416..472
FT /note="Collagen-like 4"
FT DOMAIN 473..512
FT /note="Collagen-like 5"
FT DOMAIN 604..656
FT /note="Collagen-like 6"
FT DOMAIN 657..711
FT /note="Collagen-like 7"
FT DOMAIN 712..755
FT /note="Collagen-like 8"
FT DOMAIN 790..847
FT /note="Collagen-like 9"
FT REGION 24..268
FT /note="Nonhelical region (NC4)"
FT REGION 253..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..405
FT /note="Triple-helical region (COL3)"
FT REGION 406..417
FT /note="Nonhelical region (NC3)"
FT REGION 418..756
FT /note="Triple-helical region (COL2)"
FT REGION 757..786
FT /note="Nonhelical region (NC2)"
FT REGION 783..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..901
FT /note="Triple-helical region (COL1)"
FT REGION 902..921
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 272..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT DISULFID 44..242
FT /evidence="ECO:0000250"
FT DISULFID 198..252
FT /evidence="ECO:0000250"
FT DISULFID 411
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 415
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001143"
FT VAR_SEQ 261
FT /note="T -> MAWAAWGRGVLGLSLMLSGLRLCAAQT (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001144"
FT CONFLICT 110
FT /note="E -> R (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="M -> V (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> G (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> D (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="K -> E (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 569..570
FT /note="LQ -> IA (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="E -> D (in Ref. 2; AAA21834)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="V -> A (in Ref. 2; AAA21834 and 3; CAA41049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 92092 MW; BC79177D36DCFFFC CRC64;
MKNFWKISVF FCVCSCLGPW VSATLKRRAR FPANSISNGG SELCPKIRIG QDDLPGFDLI
SQFQIEKAAS RRTIQRVVGS TALQVAYKLG SNVDFRIPTR HLYPSGLPEE YSFLTTFRMT
GSTLEKHWNI WQIQDSAGRE QVGVKINGQT KSVAFSYKGL DGSLQTAAFL NLPSLFDSRW
HKLMIGVERT SATLFIDCIR IESLPIKPRG QIDADGFAVL GKLVDNPQVS VPFELQWMLI
HCDPLRPRRE TCHELPIRIT TSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP
PGPPGPPGDP GKPGAPGKPG TPGADGLTGP DGSPGSVGPR GQKGEPGVPG SRGFPGRGIP
GPPGPPGTTG LPGELGRVGP IGDPGKRGPP GPPGPPGPSG TIGFHDGDPL CPNSCPPGRS
GYPGLPGMRG HKGAKGEIGE PGRQGHKGEE GDQGELGEVG AQGPPGPQGL RGITGIVGDK
GEKGARGFDG EPGPQGIPGA AGDQGQRGPP GETGPKGDRG IQGSRGIPGS PGPKGDTGLP
GVDGRDGIPG MPGTKGEAGK PGPPGDVGLQ GLPGVPGIPG AKGVAGEKGN TGAPGKPGQL
GSSGKPGQQG PPGEVGPRGP RGLPGSRGPV GPEGSPGIPG KLGSVGSPGL PGLPGPPGLP
GMKGDRGVFG EPGPKGEQGA SGEEGEAGAR GDLGDMGQPG PKGSVGNPGE PGLRGPEGIR
GLPGVEGPRG PPGPRGMQGE QGATGLPGIQ GPPGRAPTDQ HIKQVCMRVV QEHFVEMAAS
LKRPDTGASG LPGRPGPPGP PGPPGENGFP GQMGIRGLPG IKGPPGALGL RGPKGDLGEK
GERGPPGRGP KGLPGAIGLP GDPGPASYGK NGRDGEQGPP GVAGIPGVPG PPGPPGPPGF
CEPASCTLQS GQRAFSKGPD K
