PGS2_PIG
ID PGS2_PIG Reviewed; 360 AA.
AC Q9XSD9; Q9XSH4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE Flags: Precursor;
GN Name=DCN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Yorkshire;
RA Stephenson S., Schnoke M., Vesely I.;
RT "Cloning of the porcine decorin gene.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=Yorkshire; TISSUE=Aorta;
RA Stephenson S., Schnoke M., Vesely I.;
RT "Alternatively spliced version of the porcine decorin gene.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9XSD9-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9XSD9-2; Sequence=VSP_006177;
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; AF125537; AAD23578.1; -; mRNA.
DR EMBL; AF140270; AAD33862.1; -; mRNA.
DR RefSeq; NP_999085.1; NM_213920.1. [Q9XSD9-1]
DR AlphaFoldDB; Q9XSD9; -.
DR SMR; Q9XSD9; -.
DR STRING; 9823.ENSSSCP00000000977; -.
DR PaxDb; Q9XSD9; -.
DR PeptideAtlas; Q9XSD9; -.
DR PRIDE; Q9XSD9; -.
DR GeneID; 396957; -.
DR KEGG; ssc:396957; -.
DR CTD; 1634; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q9XSD9; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Leucine-rich repeat; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT PROPEP 17..30
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT /id="PRO_0000032715"
FT CHAIN 31..360
FT /note="Decorin"
FT /id="PRO_0000032716"
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"
FT VAR_SEQ 281..318
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_006177"
SQ SEQUENCE 360 AA; 39899 MW; 8573DE8DDEBA7509 CRC64;
MKATIVFLLL AQVSWAGPFQ QKGLFDFMLE DEASGIGPED RFPEVPELEP LGPMCPFRCQ
CHLRVVQCSD LGLDKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK
ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKAV FNGLNQMIVV
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKISKVDAA
SLKGLNNLAK LGLGFNSIST VDNGSLANTP HLRELHLNNN KLNKVPGGLA EHKYIQVVYL
HNNNISAVGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK
