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Database: UniProt
Entry: Q29393
LinkDB: Q29393
Original site: Q29393 
ID   PGS2_CANLF              Reviewed;         360 AA.
AC   Q29393;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Decorin;
DE   AltName: Full=Bone proteoglycan II;
DE   AltName: Full=PG-S2;
DE   Flags: Precursor;
GN   Name=DCN; Synonyms=DCN1C;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Glant T.T.;
RT   "Complete coding sequence and genomic structure of canine decorin.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-259.
RX   PubMed=8894053; DOI=10.1007/bf02399951;
RA   Venta P.J., Brouillette J.A., Yuzbasiyan-Gurkan V., Brewer G.J.;
RT   "Gene-specific universal mammalian sequence-tagged sites: application to
RT   the canine genome.";
RL   Biochem. Genet. 34:321-341(1996).
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}. Secreted {ECO:0000250|UniProtKB:P07585}.
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; U83141; AAB51245.1; -; mRNA.
DR   EMBL; L77684; AAA98062.1; -; Genomic_DNA.
DR   RefSeq; NP_001003228.1; NM_001003228.1.
DR   RefSeq; XP_005628882.1; XM_005628825.2.
DR   RefSeq; XP_005628883.1; XM_005628826.2.
DR   RefSeq; XP_005628885.1; XM_005628828.1.
DR   AlphaFoldDB; Q29393; -.
DR   SMR; Q29393; -.
DR   STRING; 9615.ENSCAFP00000009230; -.
DR   GlyCosmos; Q29393; 4 sites, No reported glycans.
DR   SwissPalm; Q29393; -.
DR   PaxDb; 9612-ENSCAFP00000009230; -.
DR   Ensembl; ENSCAFT00000009945.4; ENSCAFP00000009230.3; ENSCAFG00000006142.5.
DR   Ensembl; ENSCAFT00030029909.1; ENSCAFP00030026069.1; ENSCAFG00030016164.1.
DR   Ensembl; ENSCAFT00805012204; ENSCAFP00805009496; ENSCAFG00805006679.
DR   Ensembl; ENSCAFT00845035000.1; ENSCAFP00845027407.1; ENSCAFG00845019761.1.
DR   GeneID; 403904; -.
DR   KEGG; cfa:403904; -.
DR   CTD; 1634; -.
DR   VEuPathDB; HostDB:ENSCAFG00845019761; -.
DR   VGNC; VGNC:54200; DCN.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158382; -.
DR   HOGENOM; CLU_000288_186_0_1; -.
DR   InParanoid; Q29393; -.
DR   OMA; PFHQKGL; -.
DR   OrthoDB; 3953748at2759; -.
DR   TreeFam; TF334562; -.
DR   Reactome; R-CFA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-CFA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-CFA-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-CFA-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-CFA-2024101; CS/DS degradation.
DR   Reactome; R-CFA-3000178; ECM proteoglycans.
DR   Proteomes; UP000002254; Chromosome 15.
DR   Proteomes; UP000694429; Chromosome 15.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Chromosome 15.
DR   Bgee; ENSCAFG00000006142; Expressed in cartilage tissue and 47 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF14; DECORIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   PIRSF; PIRSF002490; SLRP_I; 1.
DR   SMART; SM00364; LRR_BAC; 4.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 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..16
FT                   /evidence="ECO:0000250|UniProtKB:Q01129"
FT   PROPEP          17..30
FT                   /evidence="ECO:0000250|UniProtKB:Q01129"
FT                   /id="PRO_0000032705"
FT   CHAIN           31..360
FT                   /note="Decorin"
FT                   /id="PRO_0000032706"
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|UniProtKB:P07585"
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;  39980 MW;  99BEE11A9C812906 CRC64;
     MKATIIFLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPED RAPDMPDLEL LGPVCPFRCQ
     CHLRVVQCSD LGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHT LILVNNKISK
     ISPGAFTPLL KLERLYLSKN HLKELPEKMP KTLQELRAHE NEITKVRKAV FNGLNQMIVV
     ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLE GNKITKVDAS
     SLKGLNNLAK LGLSFNSISA VDNGTLANTP HLRELHLDNN KLIRVPGGLA EHKYIQVVYL
     HNNNISAVGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK
//
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