ID PGS1_HUMAN Reviewed; 368 AA. AC P21810; D3DWU3; P13247; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 02-OCT-2024, entry version 223. DE RecName: Full=Biglycan; DE AltName: Full=Bone/cartilage proteoglycan I; DE AltName: Full=PG-S1; DE Flags: Precursor; GN Name=BGN; Synonyms=SLRR1A; 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]. RC TISSUE=Bone; RX PubMed=2647739; DOI=10.1016/s0021-9258(18)83781-4; RA Fisher L.W., Termine J.D., Young M.F.; RT "Deduced protein sequence of bone small proteoglycan I (biglycan) shows RT homology with proteoglycan II (decorin) and several nonconnective tissue RT proteins in a variety of species."; RL J. Biol. Chem. 264:4571-4576(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1860845; DOI=10.1016/s0021-9258(18)98694-1; RA Fisher L.W., Heegaard A.M., Vetter U., Vogel W., Just W., Termine J.D., RA Young M.F.; RT "Human biglycan gene. Putative promoter, intron-exon junctions, and RT chromosomal localization."; RL J. Biol. Chem. 266:14371-14377(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10854409; DOI=10.1101/gr.10.6.758; RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K., RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.; RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and RT man."; RL Genome Res. 10:758-775(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 38-57. 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 38-66. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 361-368. RC TISSUE=Skin; RX PubMed=7881444; DOI=10.1093/hmg/3.12.2268; RA Just W., Rau W., Muller R., Geerkens C., Vogel W.; RT "Dinucleotide repeat polymorphism at the human biglycan (BGN) locus."; RL Hum. Mol. Genet. 3:2268-2268(1994). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-311. 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 TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-42 AND SER-47. 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 [14] RP VARIANTS [LARGE SCALE ANALYSIS] THR-266 AND ASN-288. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP INVOLVEMENT IN SEMDX, VARIANTS SEMDX GLU-147 AND VAL-259, AND RP CHARACTERIZATION OF VARIANTS SEMDX GLU-147. RX PubMed=27236923; DOI=10.1016/j.ajhg.2016.04.004; RA Cho S.Y., Bae J.S., Kim N.K., Forzano F., Girisha K.M., Baldo C., RA Faravelli F., Cho T.J., Kim D., Lee K.Y., Ikegawa S., Shim J.S., Ko A.R., RA Miyake N., Nishimura G., Superti-Furga A., Spranger J., Kim O.H., RA Park W.Y., Jin D.K.; RT "BGN mutations in X-linked spondyloepimetaphyseal dysplasia."; RL Am. J. Hum. Genet. 98:1243-1248(2016). RN [16] RP VARIANTS MRLS SER-80 AND PRO-303, AND INVOLVEMENT IN MRLS. RX PubMed=27632686; DOI=10.1038/gim.2016.126; RA Meester J.A., Vandeweyer G., Pintelon I., Lammens M., Van Hoorick L., RA De Belder S., Waitzman K., Young L., Markham L.W., Vogt J., Richer J., RA Beauchesne L.M., Unger S., Superti-Furga A., Prsa M., Dhillon R., RA Reyniers E., Dietz H.C., Wuyts W., Mortier G., Verstraeten A., Van Laer L., RA Loeys B.L.; RT "Loss-of-function mutations in the X-linked biglycan gene cause a severe RT syndromic form of thoracic aortic aneurysms and dissections."; RL Genet. Med. 19:386-395(2017). CC -!- FUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Forms a ternary complex with MFAP2 and ELN (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC P21810; Q9H410: DSN1; NbExp=3; IntAct=EBI-762076, EBI-1001144; CC P21810; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-762076, EBI-1055254; CC P21810; Q9BRK4: LZTS2; NbExp=4; IntAct=EBI-762076, EBI-741037; CC P21810; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-762076, EBI-21503705; CC P21810; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-762076, EBI-11141397; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Detected in placenta (at protein level) CC (PubMed:32337544). Found in several connective tissues, especially in CC articular cartilages. {ECO:0000269|PubMed:32337544}. CC -!- PTM: The two attached glycosaminoglycan chains can be either CC chondroitin sulfate or dermatan sulfate. {ECO:0000250}. CC -!- DISEASE: Meester-Loeys syndrome (MRLS) [MIM:300989]: An X-linked, CC thoracic aortic aneurysm syndrome characterized by early-onset, severe CC aortic aneurysm and dissection. Other recurrent findings include CC hypertelorism, pectus deformity, joint hypermobility, contractures, and CC mild skeletal dysplasia. {ECO:0000269|PubMed:27632686}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, X-linked (SEMDX) CC [MIM:300106]: An X-linked recessive bone disease characterized by CC severe short-trunk dwarfism, brachydactyly, metaphyseal flaring of CC lower extremities, short and broad long bone diaphyses, moderate CC platyspondyly, normal facies, and normal intelligence. CC {ECO:0000269|PubMed:27236923}. Note=The disease is caused by variants 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 --------------------------------------------------------------------------- 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; J04599; AAA36009.1; -; mRNA. DR EMBL; M65153; AAA52287.1; ALT_SEQ; Genomic_DNA. DR EMBL; M65152; AAA52287.1; JOINED; Genomic_DNA. DR EMBL; U82695; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BT007323; AAP35987.1; -; mRNA. DR EMBL; CH471172; EAW72863.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72864.1; -; Genomic_DNA. DR EMBL; BC002416; AAH02416.1; -; mRNA. DR EMBL; BC004244; AAH04244.1; -; mRNA. DR EMBL; U11686; AAC50117.1; -; mRNA. DR CCDS; CCDS14721.1; -. DR PIR; A40757; BGHUN. DR RefSeq; NP_001702.1; NM_001711.5. DR RefSeq; XP_016885213.1; XM_017029724.1. DR AlphaFoldDB; P21810; -. DR SMR; P21810; -. DR BioGRID; 107102; 19. DR CORUM; P21810; -. DR IntAct; P21810; 20. DR MINT; P21810; -. DR STRING; 9606.ENSP00000327336; -. DR GlyConnect; 1042; 92 N-Linked glycans (2 sites). DR GlyCosmos; P21810; 8 sites, 109 glycans. DR GlyGen; P21810; 8 sites, 108 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P21810; -. DR PhosphoSitePlus; P21810; -. DR BioMuta; BGN; -. DR DMDM; 266762; -. DR jPOST; P21810; -. DR MassIVE; P21810; -. DR PaxDb; 9606-ENSP00000327336; -. DR PeptideAtlas; P21810; -. DR ProteomicsDB; 53928; -. DR Antibodypedia; 558; 453 antibodies from 38 providers. DR DNASU; 633; -. DR Ensembl; ENST00000331595.9; ENSP00000327336.4; ENSG00000182492.16. DR GeneID; 633; -. DR KEGG; hsa:633; -. DR MANE-Select; ENST00000331595.9; ENSP00000327336.4; NM_001711.6; NP_001702.1. DR UCSC; uc004fhr.3; human. DR AGR; HGNC:1044; -. DR CTD; 633; -. DR DisGeNET; 633; -. DR GeneCards; BGN; -. DR GeneReviews; BGN; -. DR HGNC; HGNC:1044; BGN. DR HPA; ENSG00000182492; Tissue enhanced (heart). DR MalaCards; BGN; -. DR MIM; 300106; phenotype. DR MIM; 300989; phenotype. DR MIM; 301870; gene. DR neXtProt; NX_P21810; -. DR OpenTargets; ENSG00000182492; -. DR Orphanet; 622925; X-linked severe syndromic thoracic aortic aneurysm and dissection. DR Orphanet; 93349; X-linked spondyloepimetaphyseal dysplasia. DR PharmGKB; PA25346; -. DR VEuPathDB; HostDB:ENSG00000182492; -. DR eggNOG; KOG0619; Eukaryota. DR GeneTree; ENSGT00940000155311; -. DR HOGENOM; CLU_000288_186_0_1; -. DR InParanoid; P21810; -. DR OMA; GHNNIRM; -. DR OrthoDB; 3953748at2759; -. DR PhylomeDB; P21810; -. DR TreeFam; TF334562; -. DR PathwayCommons; P21810; -. 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; P21810; -. DR SIGNOR; P21810; -. DR BioGRID-ORCS; 633; 18 hits in 782 CRISPR screens. DR ChiTaRS; BGN; human. DR GeneWiki; Biglycan; -. DR GenomeRNAi; 633; -. DR Pharos; P21810; Tbio. DR PRO; PR:P21810; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P21810; protein. DR Bgee; ENSG00000182492; Expressed in descending thoracic aorta and 189 other cell types or tissues. DR ExpressionAtlas; P21810; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb. DR GO; GO:0019955; F:cytokine binding; IEA:Ensembl. DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. 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:0061975; P:articular cartilage development; IEA:Ensembl. DR GO; GO:0060348; P:bone development; 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; IPR050333; SLRP. DR InterPro; IPR016352; SLRP_I_decor/aspor/byglycan. DR PANTHER; PTHR45712; AGAP008170-PA; 1. DR PANTHER; PTHR45712:SF11; BIGLYCAN; 1. DR Pfam; PF13855; LRR_8; 3. DR Pfam; PF01462; LRRNT; 1. DR PIRSF; PIRSF002490; SLRP_I; 1. DR SMART; SM00369; LRR_TYP; 8. DR SMART; SM00013; LRRNT; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 8. PE 1: Evidence at protein level; KW Aortic aneurysm; Direct protein sequencing; Disease variant; KW Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; KW Leucine-rich repeat; Proteoglycan; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000250|UniProtKB:P47853" FT PROPEP 17..37 FT /evidence="ECO:0000269|PubMed:2590169, FT ECO:0000269|PubMed:3597437" FT /id="PRO_0000032691" FT CHAIN 38..368 FT /note="Biglycan" FT /id="PRO_0000032692" FT REPEAT 82..102 FT /note="LRR 1" FT REPEAT 103..126 FT /note="LRR 2" FT REPEAT 127..150 FT /note="LRR 3" FT REPEAT 151..171 FT /note="LRR 4" FT REPEAT 172..195 FT /note="LRR 5" FT REPEAT 196..220 FT /note="LRR 6" FT REPEAT 221..241 FT /note="LRR 7" FT REPEAT 242..265 FT /note="LRR 8" FT REPEAT 266..289 FT /note="LRR 9" FT REPEAT 290..312 FT /note="LRR 10" FT REPEAT 313..342 FT /note="LRR 11" FT REPEAT 343..368 FT /note="LRR 12" FT CARBOHYD 42 FT /note="O-linked (Xyl...) (glycosaminoglycan) serine" FT /evidence="ECO:0000269|PubMed:2590169, FT ECO:0000269|PubMed:32337544" FT CARBOHYD 47 FT /note="O-linked (Xyl...) (glycosaminoglycan) serine" FT /evidence="ECO:0000269|PubMed:2590169, FT ECO:0000269|PubMed:32337544" FT CARBOHYD 180 FT /note="O-linked (Xyl...) (glycosaminoglycan) serine" FT /evidence="ECO:0000255" FT CARBOHYD 198 FT /note="O-linked (Xyl...) (glycosaminoglycan) serine" FT /evidence="ECO:0000255" FT CARBOHYD 270 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 63..69 FT /evidence="ECO:0000250" FT DISULFID 67..76 FT /evidence="ECO:0000250" FT DISULFID 321..354 FT /evidence="ECO:0000250" FT VARIANT 80 FT /note="G -> S (in MRLS; uncertain significance; FT dbSNP:rs886037825)" FT /evidence="ECO:0000269|PubMed:27632686" FT /id="VAR_078028" FT VARIANT 147 FT /note="K -> E (in SEMDX; reduced protein stability; FT dbSNP:rs879255604)" FT /evidence="ECO:0000269|PubMed:27236923" FT /id="VAR_076590" FT VARIANT 259 FT /note="G -> V (in SEMDX; dbSNP:rs879255605)" FT /evidence="ECO:0000269|PubMed:27236923" FT /id="VAR_076591" FT VARIANT 266 FT /note="R -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036605" FT VARIANT 288 FT /note="K -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036606" FT VARIANT 303 FT /note="Q -> P (in MRLS; uncertain significance; FT dbSNP:rs886037824)" FT /evidence="ECO:0000269|PubMed:27632686" FT /id="VAR_078029" FT CONFLICT 139..140 FT /note="KL -> NV (in Ref. 1; AAA52287)" FT /evidence="ECO:0000305" FT CONFLICT 163..164 FT /note="EL -> DV (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 368 AA; 41654 MW; BF16F304C5CD3B3E CRC64; MWPLWRLVSL LALSQALPFE QRGFWDFTLD DGPFMMNDEE ASGADTSGVL DPDSVTPTYS AMCPFGCHCH LRVVQCSDLG LKSVPKEISP DTTLLDLQNN DISELRKDDF KGLQHLYALV LVNNKISKIH EKAFSPLRKL QKLYISKNHL VEIPPNLPSS LVELRIHDNR IRKVPKGVFS GLRNMNCIEM GGNPLENSGF EPGAFDGLKL NYLRISEAKL TGIPKDLPET LNELHLDHNK IQAIELEDLL RYSKLYRLGL GHNQIRMIEN GSLSFLPTLR ELHLDNNKLA RVPSGLPDLK LLQVVYLHSN NITKVGVNDF CPMGFGVKRA YYNGISLFNN PVPYWEVQPA TFRCVTDRLA IQFGNYKK //