PGS1_BOVIN
ID PGS1_BOVIN Reviewed; 369 AA.
AC P21809; P79259; Q17QB0; Q5BIM3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Biglycan;
DE AltName: Full=Bone/cartilage proteoglycan I;
DE AltName: Full=Leucine-rich PG I;
DE AltName: Full=PG-S1;
DE Flags: Precursor;
GN Name=BGN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=8673009;
RA Xu J.H., Radhakrishnamurthy B., Srinivasan S.R., Berenson G.S.;
RT "Primary structure of bovine aorta biglycan core protein deduced from
RT cloned cDNA.";
RL Biochem. Mol. Biol. Int. 37:263-272(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 38-369.
RC TISSUE=Cartilage;
RX PubMed=2656687; DOI=10.1016/s0021-9258(18)81842-7;
RA Neame P.J., Choi H.U., Rosenberg L.C.;
RT "The primary structure of the core protein of the small, leucine-rich
RT proteoglycan (PG I) from bovine articular cartilage.";
RL J. Biol. Chem. 264:8653-8661(1989).
RN [5]
RP PROTEIN SEQUENCE OF 38-63.
RC TISSUE=Cartilage;
RX PubMed=2914936; DOI=10.1016/s0021-9258(19)81694-0;
RA Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C., Neame P.J.;
RT "Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-
RT PGII, from bovine articular cartilage and skin isolated by octyl-sepharose
RT chromatography.";
RL J. Biol. Chem. 264:2876-2884(1989).
RN [6]
RP INTERACTION WITH MFAP2 AND ELN.
RX PubMed=11723132; DOI=10.1074/jbc.m109540200;
RA Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.;
RT "Molecular interactions of biglycan and decorin with elastic fiber
RT components: biglycan forms a ternary complex with tropoelastin and
RT microfibril-associated glycoprotein 1.";
RL J. Biol. Chem. 277:3950-3957(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 38-369, DISULFIDE BONDS, SUBUNIT,
RP AND GLYCOSYLATION AT ASN-312.
RX PubMed=16547006; DOI=10.1074/jbc.m513470200;
RA Scott P.G., Dodd C.M., Bergmann E.M., Sheehan J.K., Bishop P.N.;
RT "Crystal structure of the biglycan dimer and evidence that dimerization is
RT essential for folding and stability of class I small leucine-rich repeat
RT proteoglycans.";
RL J. Biol. Chem. 281:13324-13332(2006).
CC -!- FUNCTION: May be involved in collagen fiber assembly.
CC -!- SUBUNIT: Homodimer. Forms a ternary complex with MFAP2 and ELN.
CC {ECO:0000269|PubMed:16547006}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000305}.
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DR EMBL; S82652; AAB46746.2; -; mRNA.
DR EMBL; BT021201; AAX31383.1; -; mRNA.
DR EMBL; BC118460; AAI18461.1; -; mRNA.
DR PIR; S32559; S32559.
DR RefSeq; NP_847888.2; NM_178318.4.
DR RefSeq; XP_005227715.1; XM_005227658.3.
DR PDB; 2FT3; X-ray; 3.40 A; A/B/C/D/E/F=38-369.
DR PDBsum; 2FT3; -.
DR AlphaFoldDB; P21809; -.
DR SMR; P21809; -.
DR IntAct; P21809; 4.
DR STRING; 9913.ENSBTAP00000044462; -.
DR iPTMnet; P21809; -.
DR PaxDb; P21809; -.
DR PeptideAtlas; P21809; -.
DR PRIDE; P21809; -.
DR Ensembl; ENSBTAT00000047242; ENSBTAP00000044462; ENSBTAG00000005250.
DR GeneID; 280733; -.
DR KEGG; bta:280733; -.
DR CTD; 633; -.
DR VEuPathDB; HostDB:ENSBTAG00000005250; -.
DR VGNC; VGNC:26481; BGN.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000155311; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; P21809; -.
DR OMA; IHENRIR; -.
DR OrthoDB; 826997at2759; -.
DR TreeFam; TF334562; -.
DR Reactome; R-BTA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-BTA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-BTA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-BTA-2024101; CS/DS degradation.
DR Reactome; R-BTA-3000178; ECM proteoglycans.
DR EvolutionaryTrace; P21809; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000005250; Expressed in trachea and 104 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0030133; C:transport vesicle; ISS:AgBase.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
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:2656687,
FT ECO:0000269|PubMed:2914936"
FT /id="PRO_0000032685"
FT CHAIN 38..369
FT /note="Biglycan"
FT /id="PRO_0000032686"
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 CARBOHYD 48
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT CARBOHYD 181
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16547006"
FT DISULFID 64..70
FT /evidence="ECO:0000269|PubMed:16547006"
FT DISULFID 68..77
FT /evidence="ECO:0000269|PubMed:16547006"
FT DISULFID 322..355
FT /evidence="ECO:0000269|PubMed:16547006"
FT CONFLICT 152
FT /note="V -> C (in Ref. 1; AAB46746)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="C -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="R -> A (in Ref. 1; AAB46746)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="KK -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2FT3"
FT TURN 108..113
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2FT3"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2FT3"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2FT3"
SQ SEQUENCE 369 AA; 41590 MW; B86C2149723AD0DA CRC64;
MWPLWPLAAL 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
