PGS1_XENLA
ID PGS1_XENLA Reviewed; 368 AA.
AC Q9IB75;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Biglycan;
DE Flags: Precursor;
GN Name=bgn;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Goto T., Kubota H.Y.;
RT "cDNA of biglycan of Xenopus laevis.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {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; AB037269; BAA90246.1; -; mRNA.
DR RefSeq; NP_001084178.1; NM_001090709.1.
DR AlphaFoldDB; Q9IB75; -.
DR SMR; Q9IB75; -.
DR GeneID; 399351; -.
DR CTD; 399351; -.
DR Xenbase; XB-GENE-17331698; bgn.L.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 399351; Expressed in camera-type eye and 17 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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.
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_0000032701"
FT CHAIN 38..368
FT /note="Biglycan"
FT /id="PRO_0000032702"
FT REPEAT 82..102
FT /note="LRR 1"
FT REPEAT 103..126
FT /note="LRR 2"
FT REPEAT 127..150
FT /note="LRR 3"
FT REPEAT 151..171
FT /note="LRR 4"
FT REPEAT 172..195
FT /note="LRR 5"
FT REPEAT 196..220
FT /note="LRR 6"
FT REPEAT 221..241
FT /note="LRR 7"
FT REPEAT 242..265
FT /note="LRR 8"
FT REPEAT 266..289
FT /note="LRR 9"
FT REPEAT 290..312
FT /note="LRR 10"
FT REPEAT 313..342
FT /note="LRR 11"
FT REPEAT 343..368
FT /note="LRR 12"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..69
FT /evidence="ECO:0000250"
FT DISULFID 67..76
FT /evidence="ECO:0000250"
FT DISULFID 321..354
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 41197 MW; 53ADF7E7E3BDC528 CRC64;
MKVLLLLCSC ILVIHALPFE QRGFWDFSMD DGMAMMKDEE ASGVGPIPTE SIPDVGLPPM
DLCPFGCQCH LRVVQCSDLG LTSIPKNLPK DTTLLDLQNN KITEIKKDDF KGLTNLYALV
IVNNKISKIN EKAFEPLQKM QKLYISKNNL EEIPKNLPKS LVELRIHENK IKKVPKGVFS
GLKNMNCIEM GGNPLENGGI EAGAFDGLKL NYLRVSEAKL SGIPKGLPST LNELHLDNNK
IQAIEKEDLS QYASLYRLGL GHNNIRMIEN GSLSFMPVLR ELHLDNNKLS KVPPGLPDMK
LLQVVYLHSN NITQVGVNDF CPIGFGVKRA YYNGISLFNN PVPYWEVQPA TFRCVTDRLA
IQFGNYRK