PGS1_RAT
ID PGS1_RAT Reviewed; 369 AA.
AC P47853;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Biglycan;
DE AltName: Full=Bone/cartilage proteoglycan I;
DE AltName: Full=PG-S1;
DE Flags: Precursor;
GN Name=Bgn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Vascular smooth muscle;
RX PubMed=2081545;
RA Dreher K.L., Asundi V.K., Matzura D., Cowan K.;
RT "Vascular smooth muscle biglycan represents a highly conserved proteoglycan
RT within the arterial wall.";
RL Eur. J. Cell Biol. 53:296-304(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
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}.
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DR EMBL; U17834; AAA58797.1; -; mRNA.
DR EMBL; BC072480; AAH72480.1; -; mRNA.
DR PIR; PT0077; PT0077.
DR PIR; S32793; S32793.
DR RefSeq; NP_058783.1; NM_017087.1.
DR AlphaFoldDB; P47853; -.
DR SMR; P47853; -.
DR BioGRID; 247235; 4.
DR IntAct; P47853; 9.
DR STRING; 10116.ENSRNOP00000023920; -.
DR GlyGen; P47853; 4 sites.
DR iPTMnet; P47853; -.
DR PhosphoSitePlus; P47853; -.
DR PaxDb; P47853; -.
DR PRIDE; P47853; -.
DR Ensembl; ENSRNOT00000119907; ENSRNOP00000078269; ENSRNOG00000055962.
DR GeneID; 25181; -.
DR KEGG; rno:25181; -.
DR CTD; 633; -.
DR RGD; 2207; Bgn.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000155311; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; P47853; -.
DR OMA; IHENRIR; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P47853; -.
DR TreeFam; TF334562; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:P47853; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000055962; Expressed in lung and 18 other tissues.
DR Genevisible; P47853; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR GO; GO:0061975; P:articular cartilage development; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; IEP:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; ISO:RGD.
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 Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:26479776"
FT PROPEP 17..37
FT /evidence="ECO:0000250|UniProtKB:P21810"
FT /id="PRO_0000032697"
FT CHAIN 38..369
FT /note="Biglycan"
FT /id="PRO_0000032698"
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"
FT CARBOHYD 48
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
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; 41706 MW; 319DC15117F2C604 CRC64;
MRPLWLLTLL LALSQALPFE QKGFWDFTLD DGLLMMNDEE ASGSDTTSGV PDLDSLTPTF
SAMCPFGCHC HLRVVQCSDL GLKTVPKEIS PDTTLLDLQN NDISELRKDD FKGLQHLYAL
VLVNNKISKI HEKAFSPLRK LQKLYISKNH LVEIPPNLPS SLVELRIHDN RIRKVPKGVF
SGLRNMNCIE MGGNPLENSG FEPGAFDGLK LNYLRISEAK LTGIPKDLPE TLNELHLDHN
KIQAIELEDL LRYSKLYRLG LGHNQIRMIE NGSLSFLPTL RELHLDNNKL SRVPAGLPDL
KLLQVVYLHS NNITKVGIND FCPMGFGVKR AYYNGISLFN NPVPYWEVQP ATFRCVTDRL
AIQFGNYKK
