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   24-JUL-2024, entry version 239.
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).
RN   [13]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-34.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [14]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-34.
RX   PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA   Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA   Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA   Larson G., Salanti A., Clausen T.M.;
RT   "An affinity chromatography and glycoproteomics workflow to profile the
RT   chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT   the placenta and in cancer.";
RL   Glycobiology 30:989-1002(2020).
RN   [15]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-34.
RX   PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA   Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA   Pandey A.;
RT   "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL   J. Proteins Proteom. 13:187-203(2022).
RN   [16]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-34.
RX   PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA   Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT   "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT   Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL   Mol. Cell. Proteomics 22:100617-100617(2023).
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. Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
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   -!- TISSUE SPECIFICITY: Detected in placenta (at protein level)
CC       (PubMed:32337544). Detected in cerebrospinal fluid, fibroblasts and
CC       urine (at protein level) (PubMed:25326458, PubMed:36213313,
CC       PubMed:37453717). {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313,
CC       ECO:0000269|PubMed:37453717}.
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; 26.
DR   IntAct; P07585; 17.
DR   STRING; 9606.ENSP00000052754; -.
DR   GlyConnect; 1169; 69 N-Linked glycans (3 sites).
DR   GlyCosmos; P07585; 4 sites, 68 glycans.
DR   GlyGen; P07585; 6 sites, 68 N-linked glycans (3 sites).
DR   iPTMnet; P07585; -.
DR   PhosphoSitePlus; P07585; -.
DR   SwissPalm; P07585; -.
DR   BioMuta; DCN; -.
DR   DMDM; 129951; -.
DR   jPOST; P07585; -.
DR   MassIVE; P07585; -.
DR   PaxDb; 9606-ENSP00000052754; -.
DR   PeptideAtlas; 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; 661 antibodies from 41 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   AGR; HGNC:2705; -.
DR   CTD; 1634; -.
DR   DisGeNET; 1634; -.
DR   GeneCards; DCN; -.
DR   GeneReviews; DCN; -.
DR   HGNC; HGNC:2705; DCN.
DR   HPA; ENSG00000011465; Tissue enhanced (ovary).
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; PFHQKGL; -.
DR   OrthoDB; 3953748at2759; -.
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; 8 hits in 1159 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 209 other cell types or tissues.
DR   ExpressionAtlas; P07585; baseline and differential.
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: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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
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; IPR050333; SLRP.
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; 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:25326458,
FT                   ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313,
FT                   ECO:0000269|PubMed:37453717"
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
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