PGS1_HUMAN
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 03-AUG-2022, entry version 211.
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 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 [14]
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 [15]
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: Found in several connective tissues, especially in
CC articular cartilages.
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}.
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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; 16.
DR CORUM; P21810; -.
DR IntAct; P21810; 20.
DR MINT; P21810; -.
DR STRING; 9606.ENSP00000327336; -.
DR GlyConnect; 1042; 92 N-Linked glycans (2 sites).
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 EPD; P21810; -.
DR jPOST; P21810; -.
DR MassIVE; P21810; -.
DR MaxQB; P21810; -.
DR PaxDb; P21810; -.
DR PeptideAtlas; P21810; -.
DR PRIDE; P21810; -.
DR ProteomicsDB; 53928; -.
DR Antibodypedia; 558; 414 antibodies from 37 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 CTD; 633; -.
DR DisGeNET; 633; -.
DR GeneCards; BGN; -.
DR GeneReviews; BGN; -.
DR HGNC; HGNC:1044; BGN.
DR HPA; ENSG00000182492; Low tissue specificity.
DR MalaCards; BGN; -.
DR MIM; 300106; phenotype.
DR MIM; 300989; phenotype.
DR MIM; 301870; gene.
DR neXtProt; NX_P21810; -.
DR OpenTargets; ENSG00000182492; -.
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; IHENRIR; -.
DR OrthoDB; 826997at2759; -.
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; 15 hits in 704 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 187 other tissues.
DR ExpressionAtlas; P21810; baseline and differential.
DR Genevisible; P21810; HS.
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: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 GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR028547; Biglycan.
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:SF11; PTHR45712:SF11; 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 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; Reference proteome; Repeat; Secreted;
KW 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 CARBOHYD 47
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:2590169"
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; unknown pathological 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; unknown pathological 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
