PGS2_COTJA
ID PGS2_COTJA Reviewed; 356 AA.
AC Q9DE68;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE Flags: Precursor;
GN Name=DCN;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea, and Sclera;
RX PubMed=11102759; DOI=10.1016/s0945-053x(00)00117-7;
RA Corpuz L.M., Dunlevy J.R., Hassell J.R., Conrad A.H., Conrad G.W.;
RT "Molecular cloning and relative tissue expression of decorin and lumican in
RT embryonic quail cornea.";
RL Matrix Biol. 19:699-704(2000).
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; AF125250; AAG48154.1; -; mRNA.
DR RefSeq; NP_001310117.1; NM_001323188.1.
DR AlphaFoldDB; Q9DE68; -.
DR SMR; Q9DE68; -.
DR Ensembl; ENSCJPT00005008312; ENSCJPP00005005070; ENSCJPG00005004901.
DR GeneID; 107311498; -.
DR KEGG; cjo:107311498; -.
DR CTD; 1634; -.
DR GeneTree; ENSGT00940000158382; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000694412; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT PROPEP 16..29
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT /id="PRO_0000032725"
FT CHAIN 30..356
FT /note="Decorin"
FT /id="PRO_0000032726"
FT REPEAT 70..90
FT /note="LRR 1"
FT REPEAT 91..114
FT /note="LRR 2"
FT REPEAT 115..138
FT /note="LRR 3"
FT REPEAT 139..159
FT /note="LRR 4"
FT REPEAT 160..183
FT /note="LRR 5"
FT REPEAT 184..209
FT /note="LRR 6"
FT REPEAT 210..230
FT /note="LRR 7"
FT REPEAT 231..254
FT /note="LRR 8"
FT REPEAT 255..278
FT /note="LRR 9"
FT REPEAT 279..301
FT /note="LRR 10"
FT REPEAT 302..331
FT /note="LRR 11"
FT REPEAT 332..356
FT /note="LRR 12"
FT CARBOHYD 45
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..57
FT /evidence="ECO:0000250"
FT DISULFID 55..64
FT /evidence="ECO:0000250"
FT DISULFID 310..343
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39572 MW; BE9583C6AED7DB26 CRC64;
MRLVLFILLL PVCLATPFHQ KGLFDFMLED EGSADLASTD DPVISGFGPV CPFRCQCHLR
VVQCSDLGLE RVPKDLPPDT TLLDLQNNKI TEIRDGDFKN LKNLHALILV NNKISKISPQ
AFAPLKKLER LYLSKNNLKE LPENMPKSLQ EIRAHENEIS KLRKAVFNGL NQVIVLELGT
NPLKSSGIEN GAFQGMKRLS YIRIADTNIT SIPKGLPPSL TELHLDGNKI SKIDAEGLSG
LTNLAKLGLS FNSISSVENG SLNNVPHLRE LHLNNNELVR VPSGLGEHKY IQVVYLHNNK
IASIGINDFC PLGYNTKKAT YSGVSLFSNP VQYWEIQPSA FRCIHERSAV QIGNYK
