CO9A1_CHICK
ID CO9A1_CHICK Reviewed; 920 AA.
AC P12106; Q90779;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Collagen alpha-1(IX) chain;
DE Flags: Precursor;
GN Name=COL9A1;
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] OF 1-416.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-299, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3339014; DOI=10.1016/s0021-9258(18)69209-9;
RA Vasios G., Nishimura I., Konomi H., van der Rest M., Ninomiya Y.,
RA Olsen B.R.;
RT "Cartilage type IX collagen-proteoglycan contains a large amino-terminal
RT globular domain encoded by multiple exons.";
RL J. Biol. Chem. 263:2324-2329(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 183-920.
RX PubMed=6328487; DOI=10.1073/pnas.81.10.3014;
RA Ninomiya Y., Olsen B.R.;
RT "Synthesis and characterization of cDNA encoding a cartilage-specific short
RT collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3014-3018(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 834-920.
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).
RN [5]
RP PROTEIN SEQUENCE OF 262-272 AND 778-797.
RX PubMed=2981204; DOI=10.1016/s0021-9258(18)89719-8;
RA van der Rest M., Mayne R., Ninomiya Y., Seidah N.G., Chretien M.,
RA Olsen B.R.;
RT "The structure of type IX collagen.";
RL J. Biol. Chem. 260:220-225(1985).
RN [6]
RP PROTEIN SEQUENCE OF 778-797.
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).
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 EMBL; M28659; AAA48708.1; -; mRNA.
DR EMBL; J03539; AAA48702.1; -; mRNA.
DR EMBL; K01702; AAA48675.1; -; mRNA.
DR EMBL; M11325; AAA48642.1; -; Genomic_DNA.
DR EMBL; M11324; AAA48642.1; JOINED; Genomic_DNA.
DR PIR; B34493; B34493.
DR AlphaFoldDB; P12106; -.
DR SMR; P12106; -.
DR ComplexPortal; CPX-4104; Collagen type IX trimer.
DR STRING; 9031.ENSGALP00000036264; -.
DR PaxDb; P12106; -.
DR VEuPathDB; HostDB:geneid_771873; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P12106; -.
DR PhylomeDB; P12106; -.
DR Proteomes; UP000000539; 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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 7.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Collagen; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..920
FT /note="Collagen alpha-1(IX) chain"
FT /id="PRO_0000005767"
FT DOMAIN 50..244
FT /note="Laminin G-like"
FT DOMAIN 267..323
FT /note="Collagen-like 1"
FT DOMAIN 324..355
FT /note="Collagen-like 2"
FT DOMAIN 356..401
FT /note="Collagen-like 3"
FT DOMAIN 414..470
FT /note="Collagen-like 4"
FT DOMAIN 554..612
FT /note="Collagen-like 5"
FT DOMAIN 613..642
FT /note="Collagen-like 6"
FT DOMAIN 653..711
FT /note="Collagen-like 7"
FT DOMAIN 712..753
FT /note="Collagen-like 8"
FT DOMAIN 788..842
FT /note="Collagen-like 9"
FT REGION 24..266
FT /note="Nonhelical region (N-Terminal) (NC4)"
FT REGION 264..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..899
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..242
FT /evidence="ECO:0000255"
FT DISULFID 198..252
FT /evidence="ECO:0000255"
FT CONFLICT 25
FT /note="Y -> I (in Ref. 2; AAA48702)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="E -> Q (in Ref. 2; AAA48702)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 920 AA; 91474 MW; 8C1B36ED8B7755EE CRC64;
MKSNWKITAF LYMCSFLGSF ISATYQQQSR LPVILGARQR TDLCPTIRIG EDDLPGFDLI
SQFQIEKAAS QGIVQRVVGS TALQVAYKLG PNVDFRIPTS AIYSNGLPDE YSFLTTFRMT
GATLQKYWTI WQIQDSSGKE QVGVNLNGPM KSVEFSYKGV DGSLQTASFL HLPFLFDSQW
HKLMISVETT SVTLFIDCIK VETLNIKPKG KISVDGFSVL GRLKNNPQIS VPFEVQWMPI
HCDPLRPQRE GCGELPARIS QTVIERGLPG PPGPPGPPGP PGVPGIDGID GERGPNGPPG
PPGPDGDAGK AGSPGLPGEP GADGLTGPDG SPGATGPKGQ KGEPGPPGAR GLPGKGLLGP
PGPAGAAGLP GEVGRAGPPG DPGKRGPPGP PGPPGPRGTI GLQDGDPLCP NACPPGRPGH
AGLMGMKGQK GSKGESGELG KQGYKGEEGG QGPIGEVGAQ GPLGIPGIRG ITGITGPKGN
KGARGLDGGP GPQGLPGAPG GQGQRGPVGE EGPKGERGPQ GTRGINGLPG PKGESGLPGV
DGREGIPGMP GAKGEPGKPG TPGDTGPPGL PGLPGSPGMK GIPGPKGNRG PPGVPGLMGN
SGKPGEQGPE GEAGPTGPRG PPGSRGEPGP AGPPGLPGKW GPQGDIGLPG LPGPPGLPGG
KGDRGSAGEP GPKGEQGAPG SEGDAGEKGD LGDMGLPGAK GSVGNPGDPG SRGPEGSRGL
PGMEGPRGAP GPRGLQGEQG APGLPGSQGP AGKEPTDQHI KQVCMRVMQE QLSQLAASLR
RPEFGAPGLP GRPGPPGAPG PPGENGFPGQ LGPRGLPGLK GPPGEIGRKG PKGEAGERGE
RGFPGRGVKG LPGPRGLPGE PGKPSYGREG RDGVRGPPGV AGQPGIPGPP GPPGPPGYCE
PSSCRMQAGQ RAAGKNMKGP
