ID   PGS1_HORSE              Reviewed;         372 AA.
AC   O46403; Q9N1U5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Biglycan;
DE   AltName: Full=Bone/cartilage proteoglycan I;
DE   AltName: Full=PG-S1;
DE   Flags: Precursor;
GN   Name=BGN;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Richardson D.W., Dodge G.R.;
RT   "Dose dependent effects of corticosteroids on the expression of matrix
RT   related genes in equine articular chondrocytes.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-192.
RX   PubMed=10613847; DOI=10.1101/gr.9.12.1239;
RA   Caetano A.R., Shiue Y.L., Lyons L.A., O'Brien S.J., Laughlin T.F.,
RA   Bowling A.T., Murray J.D.;
RT   "A comparative gene map of the horse (Equus caballus).";
RL   Genome Res. 9:1239-1249(1999).
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: The two attached glycosaminoglycan chains can be either
CC       chondroitin sulfate or dermatan sulfate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
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DR   EMBL; AF035934; AAB88305.1; -; mRNA.
DR   EMBL; AF135020; AAF64248.1; -; Genomic_DNA.
DR   RefSeq; NP_001075308.1; NM_001081839.1.
DR   AlphaFoldDB; O46403; -.
DR   SMR; O46403; -.
DR   STRING; 9796.ENSECAP00000041347; -.
DR   PaxDb; O46403; -.
DR   PeptideAtlas; O46403; -.
DR   PRIDE; O46403; -.
DR   Ensembl; ENSECAT00000036490; ENSECAP00000036049; ENSECAG00000018717.
DR   GeneID; 100033879; -.
DR   KEGG; ecb:100033879; -.
DR   CTD; 633; -.
DR   VGNC; VGNC:15820; BGN.
DR   GeneTree; ENSGT00940000155311; -.
DR   HOGENOM; CLU_000288_186_0_1; -.
DR   InParanoid; O46403; -.
DR   OMA; IHENRIR; -.
DR   OrthoDB; 826997at2759; -.
DR   TreeFam; TF334562; -.
DR   Proteomes; UP000002281; Chromosome X.
DR   Bgee; ENSECAG00000018717; Expressed in articular cartilage of joint and 20 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:P47853"
FT   PROPEP          20..40
FT                   /evidence="ECO:0000250|UniProtKB:P21810"
FT                   /id="PRO_0000032689"
FT   CHAIN           41..372
FT                   /note="Biglycan"
FT                   /id="PRO_0000032690"
FT   REPEAT          86..106
FT                   /note="LRR 1"
FT   REPEAT          107..130
FT                   /note="LRR 2"
FT   REPEAT          131..154
FT                   /note="LRR 3"
FT   REPEAT          155..175
FT                   /note="LRR 4"
FT   REPEAT          176..199
FT                   /note="LRR 5"
FT   REPEAT          200..224
FT                   /note="LRR 6"
FT   REPEAT          225..245
FT                   /note="LRR 7"
FT   REPEAT          246..269
FT                   /note="LRR 8"
FT   REPEAT          270..293
FT                   /note="LRR 9"
FT   REPEAT          294..316
FT                   /note="LRR 10"
FT   REPEAT          317..346
FT                   /note="LRR 11"
FT   REPEAT          347..372
FT                   /note="LRR 12"
FT   CARBOHYD        45
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  41924 MW;  D0BBF8576C5F082E CRC64;
     MPTMWPLWLL ASLLALSQAL PFEQKGFWDF TLDDGLPMLN DEEASGADTT SGIPDLDSLT
     PTFSAMCPFG CHCHLRVVQC SDLGLKAVPK EISPDTTLLD LQNNEISELR KDDFKGLQHL
     YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK
     GVFSGLRNMN CIEMGGNPLE NSGFQPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL
     DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLSRVPAGL
     PDLKLLQVVY LHTNNITKVG VNDFCPVGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT
     DRLAIQFGNY KK