ID   CO9A3_CHICK             Reviewed;         675 AA.
AC   P32017;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Collagen alpha-3(IX) chain;
DE   Flags: Precursor;
GN   Name=COL9A3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1577778; DOI=10.1016/s0021-9258(19)50201-0;
RA   Har-El R., Sharma Y.D., Aguilera A., Ueyama N., Wu J.J., Eyre D.R.,
RA   Juricic L., Chandrasekaran S., Li M., Nah H.D., Upholt W.B., Tanzer M.L.;
RT   "Cloning and developmental expression of the alpha 3 chain of chicken type
RT   IX collagen.";
RL   J. Biol. Chem. 267:10070-10076(1992).
CC   -!- FUNCTION: Collagen type IX is a minor cartilage non-fibrillar collagen.
CC       It is associated with type II collagen fibrils.
CC   -!- SUBUNIT: Trimers composed of three different chains: alpha 1(IX), alpha
CC       2(IX), and alpha 3(IX).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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; M83179; AAB59960.1; -; mRNA.
DR   AlphaFoldDB; P32017; -.
DR   SMR; P32017; -.
DR   ComplexPortal; CPX-4104; Collagen type IX trimer.
DR   STRING; 9031.ENSGALP00000009015; -.
DR   PaxDb; P32017; -.
DR   PRIDE; P32017; -.
DR   VEuPathDB; HostDB:geneid_396242; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; P32017; -.
DR   PhylomeDB; P32017; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005594; C:collagen type IX trimer; IBA:GO_Central.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0008585; P:female gonad development; IBA:GO_Central.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01391; Collagen; 8.
PE   2: Evidence at transcript level;
KW   Collagen; Extracellular matrix; Glycoprotein; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..675
FT                   /note="Collagen alpha-3(IX) chain"
FT                   /id="PRO_0000005849"
FT   REGION          22..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          25..515
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          516..546
FT                   /note="Nonhelical region 3 (NC3)"
FT   REGION          542..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..626
FT                   /note="Triple-helical region 2 (COL2)"
FT   REGION          627..631
FT                   /note="Nonhelical region 2 (NC2)"
FT   REGION          632..658
FT                   /note="Triple-helical region 1 (COL1)"
FT   REGION          659..675
FT                   /note="Nonhelical region 1 (NC1)"
FT   MOTIF           242..244
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           591..593
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        89..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..158
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   675 AA;  63013 MW;  C983FBC924A10098 CRC64;
     MTVFPTLGLL FLCQLLATTS AQRVGPQGPP GPRGPPGPSG KDGIDGEPGP SGLPGPPGPK
     GAPGKPGAAG EAGLPGLPGV DGLTGTDGPP GPNGPPGDRG ALGPAGPPGP AGKGLPGPPG
     PPGPSGLPGG NGFRGPPGPS GLPGFPGPPG PPGPPGLAGI IPEGGGDLQC PALCPPGPPG
     PPGMPGFKGH TGHKGGPGEI GKEGEKGSPG PPGPPGIPGS VGLQGPRGLR GLPGPMGPAG
     DRGDIGFRGP PGIPGPPGRA GDQGNKGPQG FRGPKGDTGR PGPKGNPGAR GLIGEPGIPG
     KDGRDGAPGL DGEKGDAARM GVPGEKGPNG LPGLPGRAGI KGSKGEPGSP GEMGEAGPSG
     EPGIPGDVGI PGDRGLPGPR GATGPVGLPG PIGAPGVRGF QGPKGSSGEP GLPGPTGIRG
     ESGDRGPAGV IGAKGSQGIA GADGLPGDKG ELGPFGPPGQ KGEPGKRGEL GPKGAQGPNG
     TAGAPGIPGH PGPMGHQGEQ GVPGITGKPG PPGKEASEQH IRELCGEMIN DQIAQLAANL
     RKPLSPGMTG RPGPAGPPGP PGATGSVGHP GARGPPGYRG PTGELGDPGP RGDTGEKGDK
     GPAGQGIDGP DGDQGPQGLP GVPGISKNGR DGAQGEPGLP GDPGTPGAVG AQGTPGICDT
     SACMGAVGAS TSKKS