CO9A2_CHICK
ID CO9A2_CHICK Reviewed; 677 AA.
AC P12108; Q90585;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Collagen alpha-2(IX) chain;
DE Flags: Precursor;
GN Name=COL9A2;
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].
RA Ninomiya Y., Castagnola P., Gerecke D., Gordon M.K., Jacenko O.,
RA LuValle P., McCarthy M., Muragaki Y., Nishimura I., Oh S., Rosenblum N.,
RA Sato N., Sugrue S., Taylor R., Vasios G., Yamaguchi N., Olsen B.R.;
RT "The molecular biology of collagens with short triple-helical domains.";
RL (In) Sandell L.J., Boyd C.D. (eds.);
RL Extracellular Matrix Genes, pp.79-114, Academic Press, San Diego (1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-174.
RX PubMed=2584206; DOI=10.1016/s0021-9258(19)47214-1;
RA Nishimura I., Muragaki Y., Olsen B.R.;
RT "Tissue-specific forms of type IX collagen-proteoglycan arise from the use
RT of two widely separated promoters.";
RL J. Biol. Chem. 264:20033-20041(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-195, PROTEIN SEQUENCE OF 147-165 AND
RP 170-188, HYDROXYLATION AT LYS-181, AND GLYCOSYLATION AT LYS-181.
RX PubMed=3473493; DOI=10.1073/pnas.84.12.4044;
RA McCormick D., van der Rest M., Goodship J., Lozano G., Ninomiya Y.,
RA Olsen B.R.;
RT "Structure of the glycosaminoglycan domain in the type IX collagen-
RT proteoglycan.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4044-4048(1987).
RN [4]
RP PROTEIN SEQUENCE OF 156-178, HYDROXYLATION AT PRO-158 AND PRO-178, AND
RP GLYCOSYLATION AT SER-167.
RX PubMed=3335523; DOI=10.1016/s0021-9258(19)35417-1;
RA Huber S., Winterhalter K.H., Vaughan L.;
RT "Isolation and sequence analysis of the glycosaminoglycan attachment site
RT of type IX collagen.";
RL J. Biol. Chem. 263:752-756(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 401-677, AND PROTEIN SEQUENCE OF 433-450 AND
RP 542-562.
RX PubMed=2996593; DOI=10.1021/bi00336a061;
RA Ninomiya Y., van der Rest M., Mayne R., Lozano G., Olsen B.R.;
RT "Construction and characterization of cDNA encoding the alpha 2 chain of
RT chicken type IX collagen.";
RL Biochemistry 24:4223-4229(1985).
RN [6]
RP PROTEIN SEQUENCE OF 170-184, HYDROXYLATION AT LYS-181, AND GLYCOSYLATION AT
RP LYS-181.
RX PubMed=3123475; DOI=10.1016/s0021-9258(19)77922-8;
RA van der Rest M., Mayne R.;
RT "Type IX collagen proteoglycan from cartilage is covalently cross-linked to
RT type II collagen.";
RL J. Biol. Chem. 263:1615-1618(1988).
RN [7]
RP PROTEIN SEQUENCE OF 218-243.
RX PubMed=3868958; DOI=10.1111/j.1749-6632.1985.tb51155.x;
RA Mayne R., van der Rest M., Ninomiya Y., Olsen B.R.;
RT "The structure of type IX collagen.";
RL Ann. N. Y. Acad. Sci. 460:38-46(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-677.
RX PubMed=3858862; DOI=10.1073/pnas.82.12.4050;
RA Lozano G., Ninomiya Y., Thompson H., Olsen B.R.;
RT "A distinct class of vertebrate collagen genes encodes chicken type IX
RT collagen polypeptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4050-4054(1985).
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 {ECO:0000269|PubMed:3123475, ECO:0000269|PubMed:3335523,
CC ECO:0000269|PubMed:3473493}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; M28660; AAA48709.1; -; mRNA.
DR EMBL; M16715; AAA48644.1; -; mRNA.
DR EMBL; AH002439; AAA48643.1; -; Genomic_DNA.
DR PIR; S23296; S23296.
DR AlphaFoldDB; P12108; -.
DR ComplexPortal; CPX-4104; Collagen type IX trimer.
DR STRING; 9031.ENSGALP00000042507; -.
DR VEuPathDB; HostDB:geneid_396524; -.
DR InParanoid; P12108; -.
DR OrthoDB; 1051097at2759; -.
DR PhylomeDB; P12108; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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 InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 7.
PE 1: Evidence at protein level;
KW Collagen; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..677
FT /note="Collagen alpha-2(IX) chain"
FT /id="PRO_0000005839"
FT REGION 25..161
FT /note="Triple-helical region 4 (COL4)"
FT REGION 28..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..178
FT /note="Nonhelical region 4 (NC4)"
FT REGION 179..517
FT /note="Triple-helical region 3 (COL3)"
FT REGION 518..547
FT /note="Nonhelical region 3 (NC3)"
FT REGION 548..630
FT /note="Triple-helical region 2 (COL2)"
FT REGION 550..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..632
FT /note="Nonhelical region 2 (NC2)"
FT REGION 633..662
FT /note="Triple-helical region 1 (COL1)"
FT REGION 663..677
FT /note="Nonhelical region 1 (NC1)"
FT COMPBIAS 28..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3335523"
FT MOD_RES 178
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3335523"
FT MOD_RES 181
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:3123475,
FT ECO:0000269|PubMed:3473493"
FT MOD_RES 190
FT /note="Allysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 167
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:3335523"
FT CARBOHYD 181
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:3123475,
FT ECO:0000269|PubMed:3473493"
FT DISULFID 172
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 176
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT CONFLICT 402..403
FT /note="QS -> RA (in Ref. 5; AAA48643)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="E -> Q (in Ref. 8; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="A -> D (in Ref. 5; AAA48643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 63796 MW; 77BAE474A675BD89 CRC64;
MAHRSPALCL LLLHAACLCL AQLRGPPGEP GPRGPPGPPG VPGADGIDGD KGSPGAPGSP
GAKGEPGAPG PDGPPGKPGL DGLTGAKGSR GPWGGQGLKG QPGLPGPPGL PGPSLPGPPG
LPGQVGLPGE IGVPGPKGDP GPDGPRGPPG PPGKPGPPGH IQGVEGSADF LCPTNCPPGP
KGPQGLQGLK GHRGRPGALG EPGQQGKQGP KGDVGVSGEQ GVPGPPGPQG QRGYPGMAGP
KGETGPAGYK GMVGTIGAAG RPGREGPKGP PGDPGEKGEL GGRGIRGPQG DIGPKGDMGL
PGIDGKDGTP GIPGVKGTAG QPGRPGPPGH RGQAGLPGQP GSKGGPGDKG EVGARGQQGI
TGTPGLDGEP GPPGDAGTAG VPGLKGDRGE RGPVGAPGEA GQSGPKGEQG PPGIPGPQGL
PGVKGDKGSP GKTGPKGSTG DPGVHGLAGV KGEKGESGEP GPKGQQGIQG ELGFPGPSGD
AGSPGVRGYP GPPGPRGLLG ERGVPGMPGQ RGVAGRDAGD QHIIDVVLKM MQEQLAEVAV
SAKRAALGGV GAMGPPGPPG PPGPPGEQGL HGPMGPRGVP GLLGAAGQIG NIGPKGKRGE
KGERGDTGRG HPGMPGPPGI PGLPGIPGHA LAGKDGERGP PGVPGDAGRP GSPGPAGLPG
FCEPAACLGA LPTPRHG
