PGS1_MOUSE
ID PGS1_MOUSE Reviewed; 369 AA.
AC P28653; Q61355;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Biglycan;
DE AltName: Full=Bone/cartilage proteoglycan I;
DE AltName: Full=PG-S1;
DE Flags: Precursor;
GN Name=Bgn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Fibroblast;
RA Naitoh Y., Suzuki S.;
RL Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=8043960; DOI=10.1007/bf00356564;
RA Rau W., Just W., Vetter U., Vogel W.;
RT "A dinucleotide repeat in the mouse biglycan gene (EST) on the X
RT chromosome.";
RL Mamm. Genome 5:395-396(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-152.
RC STRAIN=C57BL/6J;
RX PubMed=11311118; DOI=10.1042/bj3550577;
RA Saeaemaenen A.-M.K., Salminen H.J., Rantakokko A.J., Heinegaard D.,
RA Vuorio E.I.;
RT "Murine fibromodulin: cDNA and genomic structure, and age-related
RT expression and distribution in the knee joint.";
RL Biochem. J. 355:577-585(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in collagen fiber assembly. {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; X53928; CAA37875.1; -; mRNA.
DR EMBL; L20276; AAA64360.1; -; mRNA.
DR EMBL; BC005452; AAH05452.1; -; mRNA.
DR EMBL; BC019502; AAH19502.1; -; mRNA.
DR EMBL; Y11758; CAA72422.1; -; mRNA.
DR CCDS; CCDS30204.1; -.
DR PIR; S20811; S20811.
DR RefSeq; NP_031568.2; NM_007542.5.
DR AlphaFoldDB; P28653; -.
DR SMR; P28653; -.
DR BioGRID; 198345; 2.
DR IntAct; P28653; 5.
DR MINT; P28653; -.
DR STRING; 10090.ENSMUSP00000033741; -.
DR GlyGen; P28653; 4 sites.
DR PhosphoSitePlus; P28653; -.
DR jPOST; P28653; -.
DR PaxDb; P28653; -.
DR PeptideAtlas; P28653; -.
DR PRIDE; P28653; -.
DR ProteomicsDB; 288132; -.
DR Antibodypedia; 558; 414 antibodies from 37 providers.
DR DNASU; 12111; -.
DR Ensembl; ENSMUST00000033741; ENSMUSP00000033741; ENSMUSG00000031375.
DR Ensembl; ENSMUST00000169489; ENSMUSP00000126768; ENSMUSG00000031375.
DR GeneID; 12111; -.
DR KEGG; mmu:12111; -.
DR UCSC; uc012hkf.1; mouse.
DR CTD; 633; -.
DR MGI; MGI:88158; Bgn.
DR VEuPathDB; HostDB:ENSMUSG00000031375; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000155311; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; P28653; -.
DR OMA; IHENRIR; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P28653; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 12111; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Bgn; mouse.
DR PRO; PR:P28653; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P28653; protein.
DR Bgee; ENSMUSG00000031375; Expressed in vault of skull and 236 other tissues.
DR ExpressionAtlas; P28653; baseline and differential.
DR Genevisible; P28653; MM.
DR GO; GO:0009986; C:cell surface; ISS:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0061975; P:articular cartilage development; IGI:MGI.
DR GO; GO:0060348; P:bone development; IGI:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
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:0000250|UniProtKB:P47853"
FT PROPEP 17..37
FT /evidence="ECO:0000250|UniProtKB:P21810"
FT /id="PRO_0000032693"
FT CHAIN 38..369
FT /note="Biglycan"
FT /id="PRO_0000032694"
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"
FT CONFLICT 68
FT /note="C -> W (in Ref. 2; AAA64360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41639 MW; 4B57FCC9A1026BE6 CRC64;
MCPLWLLTLL LALSQALPFE QKGFWDFTLD DGLLMMNDEE ASGSDTTSGV PDLDSVTPTF
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
