PGS2_CHICK
ID PGS2_CHICK Reviewed; 357 AA.
AC P28675;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE Flags: Precursor;
GN Name=DCN;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=White leghorn; TISSUE=Cornea;
RX PubMed=1605630; DOI=10.1016/0003-9861(92)90562-b;
RA Li W., Vergnes J.-P., Cornuet P.K., Hassell J.R.;
RT "cDNA clone to chick corneal chondroitin/dermatan sulfate proteoglycan
RT reveals identity to decorin.";
RL Arch. Biochem. Biophys. 296:190-197(1992).
CC -!- FUNCTION: May affect the rate of fibrils formation. {ECO:0000250}.
CC -!- SUBUNIT: Binds to type I and type II collagen, to fibronectin and TGF-
CC beta. Forms a ternary complex with MFAP2 and ELN (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: The attached glycosaminoglycan chain can be either chondroitin
CC sulfate or dermatan sulfate depending upon the tissue of origin.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000305}.
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DR EMBL; X63797; CAA45318.1; -; mRNA.
DR PIR; S24317; S24317.
DR RefSeq; NP_001025918.1; NM_001030747.2.
DR AlphaFoldDB; P28675; -.
DR SMR; P28675; -.
DR STRING; 9031.ENSGALP00000018373; -.
DR GeneID; 417892; -.
DR KEGG; gga:417892; -.
DR CTD; 1634; -.
DR VEuPathDB; HostDB:geneid_417892; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; P28675; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P28675; -.
DR PRO; PR:P28675; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; IEA:InterPro.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR028549; Decorin.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR PANTHER; PTHR45712:SF14; PTHR45712:SF14; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR PIRSF; PIRSF002490; SLRP_I; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Proteoglycan; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT PROPEP 17..30
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT /id="PRO_0000032723"
FT CHAIN 31..357
FT /note="Decorin"
FT /id="PRO_0000032724"
FT REPEAT 71..91
FT /note="LRR 1"
FT REPEAT 92..115
FT /note="LRR 2"
FT REPEAT 116..139
FT /note="LRR 3"
FT REPEAT 140..160
FT /note="LRR 4"
FT REPEAT 161..184
FT /note="LRR 5"
FT REPEAT 185..210
FT /note="LRR 6"
FT REPEAT 211..231
FT /note="LRR 7"
FT REPEAT 232..255
FT /note="LRR 8"
FT REPEAT 256..279
FT /note="LRR 9"
FT REPEAT 280..302
FT /note="LRR 10"
FT REPEAT 303..332
FT /note="LRR 11"
FT REPEAT 333..357
FT /note="LRR 12"
FT CARBOHYD 46
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..58
FT /evidence="ECO:0000250"
FT DISULFID 56..65
FT /evidence="ECO:0000250"
FT DISULFID 311..344
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 39687 MW; 31B104C7C3CD711D CRC64;
MRLVLLFVLL LPVCLATRFH QKGLFDFMIE DEGSADMAPT DDPVISGFGP VCPFRCQCHL
RVVQCSDLGL ERVPKDLPPD TTLLDLQNNK ITEIKEGDFK NLKNLHALIL VNNKISKISP
AAFAPLKKLE RLYLSKNNLK ELPENMPKSL QEIRAHENEI SKLRKAVFNG LNQVIVLELG
TNPLKSSGIE NGAFQGMKRL SYIRIADTNI TSIPKGLPPS LTELHLDGNK ISKIDAEGLS
GLTNLAKLGL SFNSISSVEN GSLNNVPHLR ELHLNNNELV RVPSGLGEHK YIQVVYLHNN
KIASIGINDF CPLGYNTKKA TYSGVSLFSN PVQYWEIQPS AFRCIHERSA VQIGNYK
