PGS2_HUMAN
ID PGS2_HUMAN Reviewed; 359 AA.
AC P07585; Q9P0Z0; Q9P0Z1; Q9Y5N8; Q9Y5N9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 228.
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; Synonyms=SLRR1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3484330; DOI=10.1073/pnas.83.20.7683;
RA Krusius T., Ruoslahti E.;
RT "Primary structure of an extracellular matrix proteoglycan core protein
RT deduced from cloned cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7683-7687(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=8432527; DOI=10.1006/geno.1993.1023;
RA Vetter U., Vogel W., Just W., Young M.F., Fisher L.W.;
RT "Human decorin gene: intron-exon junctions and chromosomal localization.";
RL Genomics 15:161-168(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
RX PubMed=8432526; DOI=10.1006/geno.1993.1022;
RA Danielson K.G., Fazzio A., Cohen I.R., Cannizzaro L., Iozzo R.V.;
RT "The human decorin gene: intron-exon organization, discovery of two
RT alternatively spliced exons in the 5' untranslated region, and mapping of
RT the gene to chromosome 12q23.";
RL Genomics 15:146-160(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
RA Cs-Szabo G., Glant T.T.;
RT "Alternative splicing of human decorin.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-268.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [8]
RP PROTEIN SEQUENCE OF 31-50.
RX PubMed=2590169; DOI=10.1042/bj2620823;
RA Roughley P.J., White R.J.;
RT "Dermatan sulphate proteoglycans of human articular cartilage. The
RT properties of dermatan sulphate proteoglycans I and II.";
RL Biochem. J. 262:823-827(1989).
RN [9]
RP PROTEIN SEQUENCE OF 31-49.
RX PubMed=3597437; DOI=10.1016/s0021-9258(18)47991-4;
RA Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.;
RT "Purification and partial characterization of small proteoglycans I and II,
RT bone sialoproteins I and II, and osteonectin from the mineral compartment
RT of developing human bone.";
RL J. Biol. Chem. 262:9702-9708(1987).
RN [10]
RP INVOLVEMENT IN CSCD.
RX PubMed=15671264; DOI=10.1167/iovs.04-0804;
RA Bredrup C., Knappskog P.M., Majewski J., Rodahl E., Boman H.;
RT "Congenital stromal dystrophy of the cornea caused by a mutation in the
RT decorin gene.";
RL Invest. Ophthalmol. Vis. Sci. 46:420-426(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-211 AND ASN-262.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May affect the rate of fibrils formation.
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 -!- INTERACTION:
CC P07585; P13497-2: BMP1; NbExp=2; IntAct=EBI-9663608, EBI-12509497;
CC P07585; O75063: FAM20B; NbExp=4; IntAct=EBI-9663608, EBI-11090967;
CC P07585; P02751: FN1; NbExp=9; IntAct=EBI-9663608, EBI-1220319;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A;
CC IsoId=P07585-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P07585-2; Sequence=VSP_006172;
CC Name=C;
CC IsoId=P07585-3; Sequence=VSP_006173;
CC Name=D;
CC IsoId=P07585-4; Sequence=VSP_006174;
CC Name=E;
CC IsoId=P07585-5; Sequence=VSP_006175, VSP_006176;
CC -!- PTM: The attached glycosaminoglycan chain can be either chondroitin
CC sulfate or dermatan sulfate depending upon the tissue of origin.
CC -!- DISEASE: Corneal dystrophy, congenital stromal (CSCD) [MIM:610048]: A
CC corneal dystrophy characterized by congenital corneal opacification
CC consisting of a large number of flakes and spots throughout all layers
CC of the stroma. It results in progressive, painless visual loss. Corneal
CC erosions and photophobia are absent. {ECO:0000269|PubMed:15671264}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/dcn/";
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DR EMBL; M14219; AAB00774.1; -; mRNA.
DR EMBL; L01131; AAA52301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L01125; AAA52301.1; JOINED; Genomic_DNA.
DR EMBL; L01126; AAA52301.1; JOINED; Genomic_DNA.
DR EMBL; L01127; AAA52301.1; JOINED; Genomic_DNA.
DR EMBL; L01129; AAA52301.1; JOINED; Genomic_DNA.
DR EMBL; L01130; AAA52301.1; JOINED; Genomic_DNA.
DR EMBL; AH005442; AAB60901.1; -; Genomic_DNA.
DR EMBL; AF138300; AAD44713.1; -; mRNA.
DR EMBL; AF138301; AAF61437.1; -; mRNA.
DR EMBL; AF138302; AAD44714.1; -; mRNA.
DR EMBL; AF138303; AAF61438.1; -; mRNA.
DR EMBL; AF138304; AAD44715.1; -; mRNA.
DR EMBL; BT019800; AAV38603.1; -; mRNA.
DR EMBL; AF491944; AAL92176.1; -; Genomic_DNA.
DR EMBL; BC005322; AAH05322.1; -; mRNA.
DR CCDS; CCDS44951.1; -. [P07585-5]
DR CCDS; CCDS9039.1; -. [P07585-1]
DR CCDS; CCDS9040.1; -. [P07585-2]
DR CCDS; CCDS9041.1; -. [P07585-3]
DR CCDS; CCDS9042.1; -. [P07585-4]
DR PIR; A45016; NBHUC8.
DR PIR; B28457; B28457.
DR RefSeq; NP_001911.1; NM_001920.4. [P07585-1]
DR RefSeq; NP_598010.1; NM_133503.3. [P07585-1]
DR RefSeq; NP_598011.1; NM_133504.3. [P07585-2]
DR RefSeq; NP_598012.1; NM_133505.3. [P07585-3]
DR RefSeq; NP_598013.1; NM_133506.3. [P07585-4]
DR RefSeq; NP_598014.1; NM_133507.3. [P07585-5]
DR RefSeq; XP_005268750.1; XM_005268693.1.
DR RefSeq; XP_006719333.1; XM_006719270.1.
DR RefSeq; XP_016874406.1; XM_017018917.1.
DR AlphaFoldDB; P07585; -.
DR SMR; P07585; -.
DR BioGRID; 108002; 24.
DR IntAct; P07585; 16.
DR STRING; 9606.ENSP00000052754; -.
DR GlyConnect; 1169; 69 N-Linked glycans (3 sites).
DR GlyGen; P07585; 6 sites, 68 N-linked glycans (3 sites).
DR iPTMnet; P07585; -.
DR PhosphoSitePlus; P07585; -.
DR BioMuta; DCN; -.
DR DMDM; 129951; -.
DR EPD; P07585; -.
DR jPOST; P07585; -.
DR MassIVE; P07585; -.
DR PaxDb; P07585; -.
DR PeptideAtlas; P07585; -.
DR PRIDE; P07585; -.
DR ProteomicsDB; 52014; -. [P07585-1]
DR ProteomicsDB; 52015; -. [P07585-2]
DR ProteomicsDB; 52016; -. [P07585-3]
DR ProteomicsDB; 52017; -. [P07585-4]
DR ProteomicsDB; 52018; -. [P07585-5]
DR Antibodypedia; 754; 630 antibodies from 40 providers.
DR DNASU; 1634; -.
DR Ensembl; ENST00000052754.10; ENSP00000052754.5; ENSG00000011465.18. [P07585-1]
DR Ensembl; ENST00000420120.6; ENSP00000413723.2; ENSG00000011465.18. [P07585-2]
DR Ensembl; ENST00000425043.5; ENSP00000401021.1; ENSG00000011465.18. [P07585-3]
DR Ensembl; ENST00000441303.6; ENSP00000399815.2; ENSG00000011465.18. [P07585-4]
DR Ensembl; ENST00000456569.2; ENSP00000398514.2; ENSG00000011465.18. [P07585-5]
DR Ensembl; ENST00000547568.6; ENSP00000447674.2; ENSG00000011465.18. [P07585-3]
DR Ensembl; ENST00000552962.5; ENSP00000447654.1; ENSG00000011465.18. [P07585-1]
DR GeneID; 1634; -.
DR KEGG; hsa:1634; -.
DR MANE-Select; ENST00000052754.10; ENSP00000052754.5; NM_001920.5; NP_001911.1.
DR UCSC; uc001tbo.4; human. [P07585-1]
DR CTD; 1634; -.
DR DisGeNET; 1634; -.
DR GeneCards; DCN; -.
DR GeneReviews; DCN; -.
DR HGNC; HGNC:2705; DCN.
DR HPA; ENSG00000011465; Low tissue specificity.
DR MalaCards; DCN; -.
DR MIM; 125255; gene.
DR MIM; 610048; phenotype.
DR neXtProt; NX_P07585; -.
DR OpenTargets; ENSG00000011465; -.
DR Orphanet; 101068; Congenital stromal corneal dystrophy.
DR PharmGKB; PA27177; -.
DR VEuPathDB; HostDB:ENSG00000011465; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158382; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; P07585; -.
DR OMA; MSQVIVM; -.
DR PhylomeDB; P07585; -.
DR TreeFam; TF334562; -.
DR PathwayCommons; P07585; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR SignaLink; P07585; -.
DR SIGNOR; P07585; -.
DR BioGRID-ORCS; 1634; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; DCN; human.
DR GeneWiki; Decorin; -.
DR GenomeRNAi; 1634; -.
DR Pharos; P07585; Tbio.
DR PRO; PR:P07585; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P07585; protein.
DR Bgee; ENSG00000011465; Expressed in decidua and 207 other tissues.
DR ExpressionAtlas; P07585; baseline and differential.
DR Genevisible; P07585; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
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; ISS:BHF-UCL.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:MGI.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IDA:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:CACAO.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IDA:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IGI:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IGI:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
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; 6.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Corneal dystrophy; Direct protein sequencing;
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:0000269|PubMed:2590169,
FT ECO:0000269|PubMed:3597437"
FT /id="PRO_0000032709"
FT CHAIN 31..359
FT /note="Decorin"
FT /id="PRO_0000032710"
FT REPEAT 73..93
FT /note="LRR 1"
FT REPEAT 94..117
FT /note="LRR 2"
FT REPEAT 118..141
FT /note="LRR 3"
FT REPEAT 142..162
FT /note="LRR 4"
FT REPEAT 163..186
FT /note="LRR 5"
FT REPEAT 187..212
FT /note="LRR 6"
FT REPEAT 213..233
FT /note="LRR 7"
FT REPEAT 234..257
FT /note="LRR 8"
FT REPEAT 258..281
FT /note="LRR 9"
FT REPEAT 282..304
FT /note="LRR 10"
FT REPEAT 305..334
FT /note="LRR 11"
FT REPEAT 335..359
FT /note="LRR 12"
FT CARBOHYD 34
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:3484330"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..60
FT /evidence="ECO:0000250"
FT DISULFID 58..67
FT /evidence="ECO:0000250"
FT DISULFID 313..346
FT /evidence="ECO:0000250"
FT VAR_SEQ 71..179
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006172"
FT VAR_SEQ 72..75
FT /note="LDKV -> CLPS (in isoform E)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006175"
FT VAR_SEQ 73..219
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006173"
FT VAR_SEQ 76..359
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006176"
FT VAR_SEQ 109..295
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006174"
FT VARIANT 268
FT /note="T -> M (in dbSNP:rs3138268)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014351"
FT VARIANT 273
FT /note="E -> Q (in dbSNP:rs1803344)"
FT /id="VAR_011975"
FT CONFLICT 37
FT /note="G -> A (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="D -> P (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39747 MW; FF511E871A1A52DD CRC64;
MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC
HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV
SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE
LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS
LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH
NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYK
