PGS2_SHEEP
ID PGS2_SHEEP Reviewed; 360 AA.
AC Q9TTE2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE AltName: Full=PG40;
DE Flags: Precursor;
GN Name=DCN;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myometrium;
RX PubMed=10644528; DOI=10.1152/ajpcell.2000.278.1.c199;
RA Wu W.X., Zhang Q., Unno N., Derks J.B., Nathanielsz P.W.;
RT "Characterization of decorin mRNA in pregnant intrauterine tissues of the
RT ewe and regulation by steroids.";
RL Am. J. Physiol. 278:C199-C206(2000).
CC -!- FUNCTION: May affect the rate of fibrils formation. {ECO:0000250}.
CC -!- SUBUNIT: Binds to type I and type II collagen, fibronectin and TGF-
CC beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT
CC (By similarity). {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; AF125041; AAF00585.1; -; mRNA.
DR RefSeq; NP_001009218.1; NM_001009218.1.
DR AlphaFoldDB; Q9TTE2; -.
DR SMR; Q9TTE2; -.
DR STRING; 9940.ENSOARP00000016893; -.
DR GeneID; 443048; -.
DR KEGG; oas:443048; -.
DR CTD; 1634; -.
DR eggNOG; KOG0619; Eukaryota.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000002356; 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; 8.
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..16
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT PROPEP 17..30
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT /id="PRO_0000032721"
FT CHAIN 31..360
FT /note="Decorin"
FT /id="PRO_0000032722"
FT REPEAT 74..94
FT /note="LRR 1"
FT REPEAT 95..118
FT /note="LRR 2"
FT REPEAT 119..142
FT /note="LRR 3"
FT REPEAT 143..163
FT /note="LRR 4"
FT REPEAT 164..187
FT /note="LRR 5"
FT REPEAT 188..213
FT /note="LRR 6"
FT REPEAT 214..234
FT /note="LRR 7"
FT REPEAT 235..258
FT /note="LRR 8"
FT REPEAT 259..282
FT /note="LRR 9"
FT REPEAT 283..305
FT /note="LRR 10"
FT REPEAT 306..335
FT /note="LRR 11"
FT REPEAT 336..360
FT /note="LRR 12"
FT CARBOHYD 34
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..61
FT /evidence="ECO:0000250"
FT DISULFID 59..68
FT /evidence="ECO:0000250"
FT DISULFID 314..347
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 39972 MW; 0095D0DFDAB88624 CRC64;
MKATIIFFLV AQVSWAGPFQ QKGLFDFMLE DEASGIGPEE RFHEVPELEP MGPVCPFRCQ
CHLRVVQCSD LGLEKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK
ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKSV FNGLNQMIVV
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA
SLKGLNNLAK LGLSFNSISA VDNGSLANTP HLRELHLNNN KLVKVPGGLA DHKYIQVVYL
HNNNISAIGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RAAVQLGNYK
