ID   PGS1_SHEEP              Reviewed;         369 AA.
AC   O46390;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-NOV-2023, entry version 104.
DE   RecName: Full=Biglycan;
DE   AltName: Full=Bone/cartilage proteoglycan I;
DE   AltName: Full=PG-S1;
DE   Flags: Precursor;
GN   Name=BGN;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Choroid plexus;
RA   Bruett L., Clements J.E.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- 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; AF034842; AAB87988.1; -; mRNA.
DR   RefSeq; NP_001009201.1; NM_001009201.1.
DR   AlphaFoldDB; O46390; -.
DR   SMR; O46390; -.
DR   STRING; 9940.ENSOARP00000008210; -.
DR   GlyCosmos; O46390; 4 sites, No reported glycans.
DR   PaxDb; 9940-ENSOARP00000008210; -.
DR   GeneID; 443011; -.
DR   KEGG; oas:443011; -.
DR   CTD; 633; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   OrthoDB; 3953748at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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; SM00364; LRR_BAC; 3.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 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..16
FT                   /evidence="ECO:0000250|UniProtKB:P47853"
FT   PROPEP          17..37
FT                   /evidence="ECO:0000250|UniProtKB:P21810"
FT                   /id="PRO_0000032699"
FT   CHAIN           38..369
FT                   /note="Biglycan"
FT                   /id="PRO_0000032700"
FT   REPEAT          83..103
FT                   /note="LRR 1"
FT   REPEAT          104..127
FT                   /note="LRR 2"
FT   REPEAT          128..151
FT                   /note="LRR 3"
FT   REPEAT          152..172
FT                   /note="LRR 4"
FT   REPEAT          173..196
FT                   /note="LRR 5"
FT   REPEAT          197..221
FT                   /note="LRR 6"
FT   REPEAT          222..242
FT                   /note="LRR 7"
FT   REPEAT          243..266
FT                   /note="LRR 8"
FT   REPEAT          267..290
FT                   /note="LRR 9"
FT   REPEAT          291..313
FT                   /note="LRR 10"
FT   REPEAT          314..343
FT                   /note="LRR 11"
FT   REPEAT          344..369
FT                   /note="LRR 12"
FT   CARBOHYD        42
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P21810"
FT   CARBOHYD        48
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P21810"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        64..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..355
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  41523 MW;  048C82C233909EE6 CRC64;
     MCPLWLLAAL LALSQALPFE QKAFWDFTLD DGLPMLNDEE ASGAETTSGI PDLDSLPPTY
     SAMCPFGCHC HLRVVQCSDL GLKAVPKEIS PDTTLLDLQN NDISELRKDD FKGLQHLYAL
     VLVNNKISKI HEKAFSPLRK LQKLYISKNH LVEIPPNLPS SLVELRIHDN RIRKVPKGVF
     SGLRNMNCIE MGGNPLENSG FEPGAFDGLK LNYLRISEAK LTGIPKDLPE TLNELHLDHN
     KIQAIELEDL LRYSKLYRLG LGHNQIRMIE NGSLSFLPTL RELHLDNNKL SRVPAGLPDL
     KLLQVVYLHT NNITKVGVND FCPVGFGVKR AYYNGISLFN NPVPYWEVQP ATFRCVTDRL
     AIQFGNYKK
//