ID   CO9A1_RAT               Reviewed;         325 AA.
AC   P20850;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Collagen alpha-1(IX) chain;
DE   Flags: Fragment;
GN   Name=Col9a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2465149; DOI=10.1111/j.1432-1033.1989.tb14522.x;
RA   Kimura T., Mattei M.-G., Stevens J.W., Goldring M.B., Ninomiya Y.,
RA   Olsen B.R.;
RT   "Molecular cloning of rat and human type IX collagen cDNA and localization
RT   of the alpha 1(IX) gene on the human chromosome 6.";
RL   Eur. J. Biochem. 179:71-78(1989).
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   -!- 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   PIR; S02170; S02170.
DR   AlphaFoldDB; P20850; -.
DR   ComplexPortal; CPX-4103; Collagen type IX trimer.
DR   STRING; 10116.ENSRNOP00000018116; -.
DR   PaxDb; P20850; -.
DR   UCSC; RGD:1309425; rat.
DR   RGD; 1309425; Col9a1.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; P20850; -.
DR   PhylomeDB; P20850; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005594; C:collagen type IX trimer; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0051216; P:cartilage development; ISO:RGD.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEP:RGD.
DR   GO; GO:0035988; P:chondrocyte proliferation; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0003417; P:growth plate cartilage development; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR   GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01391; Collagen; 5.
PE   3: Inferred from homology;
KW   Collagen; Extracellular matrix; Hydroxylation; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Zinc.
FT   CHAIN           <1..325
FT                   /note="Collagen alpha-1(IX) chain"
FT                   /id="PRO_0000059400"
FT   REGION          1..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   325 AA;  31256 MW;  9A7600CC2A727466 CRC64;
     PGQLGNSGKP GQQGPPGEVG PRGPRGLPGS RGPVGPEGSP GIPGKLGPLG SPGLPGLPGP
     PGLPGMKGDR GVFGEPGPKG EQGASGEEGE AGVRGDLGDM GQPGPKGSVG NPGEPGLRGP
     EGIRGLPGVE GPRGPPGPRG VQGEQGATGL PGIQGPPGRA PTDQHIKQVC MRVVQEHFAE
     MAASLKRPDT GASGLPGRPG PPGPPGPPGE NGFPGQMGIR GLPGIKGPPG ALGLRGPKGD
     LGEKGERGPP GRGPKGLPGA IGLPGDPGPA SYGKNGRDGE QGPPGVAGIP GVPGPPGPPG
     PPGFCEPASC TLQAGQRAFS KGPDK