PGS2_RABIT
ID PGS2_RABIT Reviewed; 360 AA.
AC Q28888; Q28608;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE Flags: Precursor;
GN Name=DCN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea;
RX PubMed=7822148;
RA Zhan Q., Burrows R., Cintron C.;
RT "Cloning and in situ hybridization of rabbit decorin in corneal tissues.";
RL Invest. Ophthalmol. Vis. Sci. 36:206-215(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-358.
RC TISSUE=Cartilage;
RA Hering T.M., Kollar J.;
RT "The primary structure of rabbit chondrocyte decorin deduced from
RT nucleotide sequence.";
RL Submitted (NOV-1993) 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 {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; S76584; AAB33083.1; -; mRNA.
DR EMBL; U03394; AAC04315.1; -; mRNA.
DR PIR; I47020; I47020.
DR RefSeq; NP_001075799.1; NM_001082330.1.
DR RefSeq; XP_008254943.1; XM_008256721.1.
DR RefSeq; XP_008254944.1; XM_008256722.2.
DR AlphaFoldDB; Q28888; -.
DR SMR; Q28888; -.
DR STRING; 9986.ENSOCUP00000006027; -.
DR Ensembl; ENSOCUT00000006967; ENSOCUP00000006027; ENSOCUG00000006969.
DR GeneID; 100009171; -.
DR KEGG; ocu:100009171; -.
DR CTD; 1634; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158382; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; Q28888; -.
DR OMA; MSQVIVM; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000006969; Expressed in uterus and 17 other tissues.
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; 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_0000032717"
FT CHAIN 31..360
FT /note="Decorin"
FT /id="PRO_0000032718"
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; 39896 MW; 0B50C6756FE02369 CRC64;
MTATLILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPDE RAPELPDLDM LGPVCPFRCQ
CHLRVVQCSD LGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK
ISPGAFTPLV KLERLYLSKN HLKELPEKMP KSLQELRAHE NEITKVRKSV FSGMNQMIVI
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKIDAS
SLKGLNNLAK LGLSFNDISA VDNGSLANAP HLRELHLDNN KLIRVPGGLA DHKYIQVVYL
HNNNISVVGA NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYM RSAIQLGNYK
