CO9A2_BOVIN
ID CO9A2_BOVIN Reviewed; 688 AA.
AC C0HLN2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 25-MAY-2022, entry version 7.
DE RecName: Full=Collagen alpha-2(IX) chain {ECO:0000250|UniProtKB:Q14055};
DE AltName: Full=Collagen type IX alpha 2 chain {ECO:0000305};
DE Flags: Precursor;
GN Name=COL9A2 {ECO:0000250|UniProtKB:Q14055};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 171-182, AND CROSS-LINKS.
RX PubMed=3609327; DOI=10.1016/0014-5793(87)80842-6;
RA Eyre D.R., Apon S., Wu J.J., Ericsson L.H., Walsh K.A.;
RT "Collagen type IX: evidence for covalent linkages to type II collagen in
RT cartilage.";
RL FEBS Lett. 220:337-341(1987).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 171-195, SUBUNIT, CROSS-LINKS, AND HYDROXYLATION AT
RP LYS-182.
RX PubMed=1429648; DOI=10.1016/s0021-9258(18)50048-x;
RA Wu J.J., Woods P.E., Eyre D.R.;
RT "Identification of cross-linking sites in bovine cartilage type IX collagen
RT reveals an antiparallel type II-type IX molecular relationship and type IX
RT to type IX bonding.";
RL J. Biol. Chem. 267:23007-23014(1992).
RN [4] {ECO:0000305}
RP SUBUNIT.
RX PubMed=2511833; DOI=10.1042/bj2620753;
RA Ayad S., Marriott A., Morgan K., Grant M.E.;
RT "Bovine cartilage types VI and IX collagens. Characterization of their
RT forms in vivo.";
RL Biochem. J. 262:753-761(1989).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=1599476; DOI=10.1016/s0006-291x(05)80998-2;
RA Bishop P., McLeod D., Ayad S.;
RT "Extraction and characterisation of the intact form of bovine vitreous type
RT IX collagen.";
RL Biochem. Biophys. Res. Commun. 185:392-397(1992).
RN [6] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8315278; DOI=10.1177/41.6.8315278;
RA Ruggiero F., Petit B., Ronziere M.C., Farjanel J., Hartmann D.J.,
RA Herbage D.;
RT "Composition and organization of the collagen network produced by fetal
RT bovine chondrocytes cultured at high density.";
RL J. Histochem. Cytochem. 41:867-875(1993).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=8172611; DOI=10.1042/bj2990497;
RA Bishop P.N., Crossman M.V., McLeod D., Ayad S.;
RT "Extraction and characterization of the tissue forms of collagen types II
RT and IX from bovine vitreous.";
RL Biochem. J. 299:497-505(1994).
CC -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the
CC eye. {ECO:0000269|PubMed:1599476, ECO:0000269|PubMed:8172611,
CC ECO:0000269|PubMed:8315278}.
CC -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha
CC 3(IX) chain (Probable). The chains are linked to each other by
CC interchain disulfide bonds (Probable). Trimers are also cross-linked
CC via hydroxylysines (Probable). {ECO:0000305|PubMed:1429648,
CC ECO:0000305|PubMed:2511833}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:8315278}.
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. {ECO:0000305}.
CC -!- PTM: Covalently linked to the telopeptides of type II collagen by
CC hydroxylysine-derived cross-links. {ECO:0000269|PubMed:1429648,
CC ECO:0000269|PubMed:3609327}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; CM008170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; C0HLN2; -.
DR ComplexPortal; CPX-4105; Collagen type IX trimer.
DR STRING; 9913.ENSBTAP00000027483; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 9.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..688
FT /note="Collagen alpha-2(IX) chain"
FT /id="PRO_0000449249"
FT REGION 26..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..162
FT /note="Triple-helical region 4 (COL4)"
FT /evidence="ECO:0000305"
FT REGION 163..179
FT /note="Nonhelical region 4 (NC4)"
FT /evidence="ECO:0000305"
FT REGION 180..518
FT /note="Triple-helical region 3 (COL3)"
FT /evidence="ECO:0000305"
FT REGION 519..548
FT /note="Nonhelical region 3 (NC3)"
FT /evidence="ECO:0000305"
FT REGION 549..631
FT /note="Triple-helical region 2 (COL2)"
FT /evidence="ECO:0000305"
FT REGION 549..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..633
FT /note="Nonhelical region 2 (NC2)"
FT /evidence="ECO:0000305"
FT REGION 634..663
FT /note="Triple-helical region 1 (COL1)"
FT /evidence="ECO:0000305"
FT REGION 664..688
FT /note="Nonhelical region 1 (NC1)"
FT /evidence="ECO:0000305"
FT COMPBIAS 29..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..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:0000305|PubMed:1429648"
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"
SQ SEQUENCE 688 AA; 64963 MW; 8315F21E36D37428 CRC64;
MAPAADPRSL LVLLQVLGLA LAQIRGLPGE PGPPGPPGPP GVPGSDGIDG DKGPPGKAGP
PGPKGEPGKA GTDGPDGKPG IDGLTGAKGE PGPAGIPGVK GQPGLPGPPG LPGPGFAGPP
GPPGPVGLPG EIGLTGPKGD PGPEGPSGPP GPPGKPGRPG TIQGLEGSAD FLCPTNCPAG
VKGPPGLQGV KGHPGRRGLL GDSGRQGKPG PKGDVGASGE QGIPGPPGPQ GVRGYPGMAG
PKGETGPQGY KGMVGSVGAA GSPGEEGPRG PPGRAGEKGD VGSQGVRGPQ GITGPKGATG
PPGIDGKDGT PGTPGVKGSA GQAGRPGNPG HQGLAGVPGM PGTKGGPGDK GEPGRQGFPG
VSGPPGKEGE PGPRGEIGPQ GIMGQKGDHG ERGPVGQPGP QGRQGPKGEQ GPPGIPGPQG
LPGIKGDKGS PGKTGPRGGV GDPGVAGLPG EKGEKGESGE PGPKGQQGVR GEPGYPGPSG
DAGAPGVQGY PGPPGPRGLV GDRGLPGQPG RQGVAGRDAS DQHIEDVVLK MLQEQLAEMA
VSAKREALGA TGMMGPPGPP GPPGYPGKQG PHGHPGPRGV PGIVGAVGQI GNTGPKGKRG
EKGDQGEVGR GHPGMPGPPG IPGLPGRPGQ AINGKDGDRG APGAPGEAGR PGLPGPIGLP
GFCEPAACLG ASAYASGRLT EPGSIKGP
