PGS1_PIG
ID PGS1_PIG Reviewed; 272 AA.
AC Q9GKQ6; Q9TTB5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Biglycan;
DE AltName: Full=Bone/cartilage proteoglycan I;
DE AltName: Full=PG-S1;
DE Flags: Precursor; Fragments;
GN Name=BGN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-137.
RC TISSUE=Aorta;
RA Zhao B.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-272.
RC TISSUE=Skin;
RA Wang J.F., Boykiw R.H., Reno C.R., Olson M.E., Hart D.A.;
RT "Cloning and sequencing of porcine matrix molecules.";
RL Submitted (JUN-1999) 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}.
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DR EMBL; AF159382; AAF19153.1; -; mRNA.
DR AlphaFoldDB; Q9GKQ6; -.
DR SMR; Q9GKQ6; -.
DR PeptideAtlas; Q9GKQ6; -.
DR PRIDE; Q9GKQ6; -.
DR InParanoid; Q9GKQ6; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
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 PANTHER; PTHR45712:SF11; PTHR45712:SF11; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 5.
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_0000032695"
FT CHAIN 38..272
FT /note="Biglycan"
FT /id="PRO_0000032696"
FT DOMAIN 55..91
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..>137
FT /note="LRR 2"
FT REPEAT 138..161
FT /note="LRR 3"
FT REPEAT 162..183
FT /note="LRR 4"
FT REPEAT 186..209
FT /note="LRR 5"
FT REPEAT 210..232
FT /note="LRR 6"
FT REPEAT 233..254
FT /note="LRR 7"
FT REPEAT 255..>272
FT /note="LRR 8"
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 DISULFID 64..70
FT /evidence="ECO:0000250"
FT DISULFID 68..77
FT /evidence="ECO:0000250"
FT NON_CONS 137..138
FT /evidence="ECO:0000305"
FT NON_TER 272
SQ SEQUENCE 272 AA; 30457 MW; 6EBBAD0EF86378BB CRC64;
MWPLWLLASL LALSQALPFE QKAFWDFTLD DGLPMLNDEE ASGADSTSGI PDLDALPPTF
SAMCPFGCHC HLRVVQCSDL GLKAVPKEIS PDTTLLDLQN NDISELRKDD FKGLQHLYAL
VLVNNKISRS TRRPSAPDGL KLNYLRISEA KLTGIPKDLP ETLNELHLDH NKIQAIELED
LLRYSKLYRL GLGHNQIRMI ENGSLSFLPT LRELHLDNNK LSRVPAGLPD LKLLQVVYLH
TNNITKVGVN DFCPVGFGVK RAYYNGISLF NN