PGS2_RAT
ID PGS2_RAT Reviewed; 354 AA.
AC Q01129;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=Dermatan sulfate proteoglycan-II;
DE Short=DSPG;
DE AltName: Full=PG-S2;
DE AltName: Full=PG40;
DE Flags: Precursor;
GN Name=Dcn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=1390895; DOI=10.1016/0167-4781(92)90019-v;
RA Abramson S.R., Woessner J.F.;
RT "cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin).";
RL Biochim. Biophys. Acta 1132:225-227(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-354.
RX PubMed=1493796;
RA Asundi V.K., Dreher K.L.;
RT "Molecular characterization of vascular smooth muscle decorin: deduced core
RT protein structure and regulation of gene expression.";
RL Eur. J. Cell Biol. 59:314-321(1992).
RN [4]
RP PROTEIN SEQUENCE OF 31-48 AND 171-191.
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=2764879; DOI=10.1042/bj2600413;
RA Kokenyesi R., Woessner J.F.;
RT "Purification and characterization of a small dermatan sulphate
RT proteoglycan implicated in the dilatation of the rat uterine cervix.";
RL Biochem. J. 260:413-419(1989).
RN [5]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-16, CLEAVAGE OF PROPEPTIDE AFTER
RP GLU-30, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: May affect the rate of fibrils formation (By similarity). May
CC be implicated in the dilatation of the rat cervix. {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 -!- DEVELOPMENTAL STAGE: The amount of DSPG per cervix increases 4-fold
CC during pregnancy, then falls precipitously within 1 day post partum.
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; Z12298; CAA78170.1; -; mRNA.
DR EMBL; BC083750; AAH83750.1; -; mRNA.
DR EMBL; X59859; CAA42519.1; -; mRNA.
DR PIR; S29145; S29145.
DR RefSeq; NP_077043.1; NM_024129.1.
DR RefSeq; XP_006241347.1; XM_006241285.1.
DR AlphaFoldDB; Q01129; -.
DR SMR; Q01129; -.
DR BioGRID; 247822; 4.
DR IntAct; Q01129; 1.
DR STRING; 10116.ENSRNOP00000006070; -.
DR GlyGen; Q01129; 5 sites.
DR iPTMnet; Q01129; -.
DR PhosphoSitePlus; Q01129; -.
DR PaxDb; Q01129; -.
DR PRIDE; Q01129; -.
DR Ensembl; ENSRNOT00000006070; ENSRNOP00000006070; ENSRNOG00000004554.
DR GeneID; 29139; -.
DR KEGG; rno:29139; -.
DR UCSC; RGD:61895; rat.
DR CTD; 1634; -.
DR RGD; 61895; Dcn.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158382; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; Q01129; -.
DR OMA; MSQVIVM; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q01129; -.
DR TreeFam; TF334562; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:Q01129; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004554; Expressed in stomach and 20 other tissues.
DR Genevisible; Q01129; RN.
DR GO; GO:0005589; C:collagen type VI trimer; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IDA:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; ISO:RGD.
DR GO; GO:0001890; P:placenta development; IEP:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 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:0000269|PubMed:26479776"
FT PROPEP 17..30
FT /evidence="ECO:0000269|PubMed:26479776,
FT ECO:0000269|PubMed:2764879"
FT /id="PRO_0000032719"
FT CHAIN 31..354
FT /note="Decorin"
FT /id="PRO_0000032720"
FT REPEAT 68..88
FT /note="LRR 1"
FT REPEAT 89..112
FT /note="LRR 2"
FT REPEAT 113..136
FT /note="LRR 3"
FT REPEAT 137..157
FT /note="LRR 4"
FT REPEAT 158..181
FT /note="LRR 5"
FT REPEAT 182..207
FT /note="LRR 6"
FT REPEAT 208..228
FT /note="LRR 7"
FT REPEAT 229..252
FT /note="LRR 8"
FT REPEAT 253..276
FT /note="LRR 9"
FT REPEAT 277..299
FT /note="LRR 10"
FT REPEAT 300..329
FT /note="LRR 11"
FT REPEAT 330..354
FT /note="LRR 12"
FT CARBOHYD 34
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..55
FT /evidence="ECO:0000250"
FT DISULFID 53..62
FT /evidence="ECO:0000250"
FT DISULFID 308..341
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39805 MW; 152D92F42D9F5A5B CRC64;
MKATLVLFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP YRCQCHLRVV
QCSDLGLDKV PWEFPPDTTL LDLQNNKITE IKEGAFKNLK DLHTLILVNN KISKISPEAF
KPLVKLERLY LSKNHLKELP EKLPKTLQEL RLHDNEITKL KKSVFNGLNR MIVIELGGNP
LKNSGIENGA LQGMKGLGYI RISDTNITAI PQGLPTSISE LHLDGNKIAK VDAASLKGMS
NLSKLGLSFN SITVVENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYVQ VVYLHNNNIS
EVGQHDFCLP SYQTRKTSYT AVSLYSNPVR YWQIHPHTFR CVFGRSTIQL GNYK
