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 11-NOV-2015, entry version 179. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT protein 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 RT 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 RT of 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 RT 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 31-50. RX PubMed=2590169; 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; RA Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.; RT "Purification and partial characterization of small proteoglycans I RT and II, bone sialoproteins I and II, and osteonectin from the mineral RT compartment of developing human bone."; RL J. Biol. Chem. 262:9702-9708(1987). RN [10] RP INVOLVEMENT IN CONGENITAL STROMAL CORNEAL DYSTROPHY. 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 RT the 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 RT multiple 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 CC TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts CC with DPT (By similarity). {ECO:0000250}. 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 CC chondroitin sulfate or dermatan sulfate depending upon the tissue CC of origin. CC -!- DISEASE: Corneal dystrophy, congenital stromal (CSCD) CC [MIM:610048]: A corneal dystrophy characterized by congenital CC corneal opacification consisting of a large number of flakes and CC spots throughout all layers of the stroma. It results in CC progressive, painless visual loss. Corneal erosions and CC photophobia are absent. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) CC family. SLRP class I subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 12 LRR (leucine-rich) repeats. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/dcn/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001920.3. [P07585-1] DR RefSeq; NP_598010.1; NM_133503.2. [P07585-1] DR RefSeq; NP_598011.1; NM_133504.2. [P07585-2] DR RefSeq; NP_598012.1; NM_133505.2. [P07585-3] DR RefSeq; NP_598013.1; NM_133506.2. [P07585-4] DR RefSeq; NP_598014.1; NM_133507.2. [P07585-5] DR RefSeq; XP_005268750.1; XM_005268693.1. [P07585-1] DR RefSeq; XP_006719333.1; XM_006719270.1. [P07585-1] DR UniGene; Hs.156316; -. DR ProteinModelPortal; P07585; -. DR SMR; P07585; 51-355. DR BioGrid; 108002; 19. DR IntAct; P07585; 8. DR STRING; 9606.ENSP00000052754; -. DR PhosphoSite; P07585; -. DR BioMuta; DCN; -. DR DMDM; 129951; -. DR PaxDb; P07585; -. DR PRIDE; P07585; -. DR DNASU; 1634; -. DR Ensembl; ENST00000052754; ENSP00000052754; ENSG00000011465. [P07585-1] DR Ensembl; ENST00000393155; ENSP00000376862; ENSG00000011465. [P07585-1] DR Ensembl; ENST00000420120; ENSP00000413723; ENSG00000011465. [P07585-2] DR Ensembl; ENST00000425043; ENSP00000401021; ENSG00000011465. [P07585-3] DR Ensembl; ENST00000441303; ENSP00000399815; ENSG00000011465. [P07585-4] DR Ensembl; ENST00000456569; ENSP00000398514; ENSG00000011465. [P07585-5] DR Ensembl; ENST00000547568; ENSP00000447674; ENSG00000011465. [P07585-3] DR Ensembl; ENST00000552962; ENSP00000447654; ENSG00000011465. [P07585-1] DR GeneID; 1634; -. DR KEGG; hsa:1634; -. DR UCSC; uc001tbo.3; human. [P07585-2] DR UCSC; uc001tbp.3; human. [P07585-3] DR UCSC; uc001tbq.3; human. [P07585-4] DR UCSC; uc001tbr.3; human. [P07585-5] DR UCSC; uc001tbt.3; human. [P07585-1] DR CTD; 1634; -. DR GeneCards; DCN; -. DR GeneReviews; DCN; -. DR HGNC; HGNC:2705; DCN. DR HPA; CAB017118; -. DR HPA; HPA003315; -. DR MIM; 125255; gene. DR MIM; 610048; phenotype. DR neXtProt; NX_P07585; -. DR Orphanet; 101068; Congenital stromal corneal dystrophy. DR PharmGKB; PA27177; -. DR eggNOG; KOG0619; Eukaryota. DR eggNOG; COG4886; LUCA. DR GeneTree; ENSGT00760000118969; -. DR HOGENOM; HOG000261690; -. DR HOVERGEN; HBG016052; -. DR InParanoid; P07585; -. DR KO; K04660; -. DR OMA; PLGPVCP; -. DR OrthoDB; EOG76739V; -. DR PhylomeDB; P07585; -. DR TreeFam; TF334562; -. 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 ChiTaRS; DCN; human. DR GeneWiki; Decorin; -. DR GenomeRNAi; 1634; -. DR NextBio; 6702; -. DR PMAP-CutDB; P07585; -. DR PRO; PR:P07585; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P07585; -. DR CleanEx; HS_DCN; -. DR ExpressionAtlas; P07585; baseline and differential. DR Genevisible; P07585; HS. DR GO; GO:0005589; C:collagen type VI trimer; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl. DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome. DR GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome. DR GO; GO:0030204; P:chondroitin sulfate metabolic process; TAS:Reactome. DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl. DR GO; GO:0001890; P:placenta development; IEA:Ensembl. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:CACAO. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR InterPro; IPR028549; Decorin. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR000372; LRRNT. DR InterPro; IPR016352; SLRP_I_decor/aspor/byglycan. DR PANTHER; PTHR24369:SF5; PTHR24369:SF5; 1. DR Pfam; PF13855; LRR_8; 3. DR Pfam; PF01462; LRRNT; 1. DR PIRSF; PIRSF002490; SLRP_I; 1. DR SMART; SM00369; LRR_TYP; 1. DR SMART; SM00013; LRRNT; 1. DR PROSITE; PS51450; LRR; 8. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Corneal dystrophy; KW Direct protein sequencing; Disulfide bond; Extracellular matrix; KW Glycoprotein; Leucine-rich repeat; Polymorphism; Proteoglycan; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 16 {ECO:0000255}. FT PROPEP 17 30 {ECO:0000269|PubMed:2590169, FT ECO:0000269|PubMed:3597437}. FT /FTId=PRO_0000032709. FT CHAIN 31 359 Decorin. FT /FTId=PRO_0000032710. FT REPEAT 73 93 LRR 1. FT REPEAT 94 117 LRR 2. FT REPEAT 118 141 LRR 3. FT REPEAT 142 162 LRR 4. FT REPEAT 163 186 LRR 5. FT REPEAT 187 212 LRR 6. FT REPEAT 213 233 LRR 7. FT REPEAT 234 257 LRR 8. FT REPEAT 258 281 LRR 9. FT REPEAT 282 304 LRR 10. FT REPEAT 305 334 LRR 11. FT REPEAT 335 359 LRR 12. FT COMPBIAS 54 67 Cys-rich. FT CARBOHYD 34 34 O-linked (Xyl...) (glycosaminoglycan). FT {ECO:0000269|PubMed:3484330}. FT CARBOHYD 211 211 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 262 262 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 303 303 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 54 60 {ECO:0000250}. FT DISULFID 58 67 {ECO:0000250}. FT DISULFID 313 346 {ECO:0000250}. FT VAR_SEQ 71 179 Missing (in isoform B). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_006172. FT VAR_SEQ 72 75 LDKV -> CLPS (in isoform E). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_006175. FT VAR_SEQ 73 219 Missing (in isoform C). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_006173. FT VAR_SEQ 76 359 Missing (in isoform E). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_006176. FT VAR_SEQ 109 295 Missing (in isoform D). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_006174. FT VARIANT 268 268 T -> M (in dbSNP:rs3138268). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_014351. FT VARIANT 273 273 E -> Q (in dbSNP:rs1803344). FT /FTId=VAR_011975. FT CONFLICT 37 37 G -> A (in Ref. 9; AA sequence). FT {ECO:0000305}. FT CONFLICT 45 45 D -> P (in Ref. 9; AA sequence). FT {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 //