PGS1_CANLF
ID PGS1_CANLF Reviewed; 369 AA.
AC O02678;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Biglycan;
DE AltName: Full=Bone/cartilage proteoglycan I;
DE AltName: Full=PG-S1;
DE Flags: Precursor;
GN Name=BGN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Glant T.T.;
RT "Complete coding sequence of canine biglycan.";
RL Submitted (DEC-1996) 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 -!- 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; U83140; AAB51244.1; -; mRNA.
DR RefSeq; NP_001003229.1; NM_001003229.1.
DR AlphaFoldDB; O02678; -.
DR SMR; O02678; -.
DR STRING; 9612.ENSCAFP00000028297; -.
DR CPTAC; CPTAC-3273; -.
DR CPTAC; CPTAC-3278; -.
DR PaxDb; O02678; -.
DR PRIDE; O02678; -.
DR GeneID; 403905; -.
DR KEGG; cfa:403905; -.
DR CTD; 633; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; O02678; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 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_0000032687"
FT CHAIN 38..369
FT /note="Biglycan"
FT /id="PRO_0000032688"
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; 41566 MW; 8C919E922D6377E6 CRC64;
MWPLWLVASL LALSQALPFE QKGFWDFTLD DGLPMLNDEE ASGAETTSGV PDLDALTPTY
SAMCPFGCHC HLRVVQCSDL GLKAVPKEIS PDTMLLDLQN NDISELRADD FKGLHHLYAL
VLVNNKISKI HEKAFSPLRK LQKLYISKNH LVEIPPNLPS SLVELRIHDN RIRKVPKGVF
SGLRNMNCIE MGGNPLENSG FEPGAFDGLK LNYLRISEAK LTGIPKDLPE TLNELHLDHN
KIQAIELEDL LRYSKLYRLG LGHNQIRMIE NGSLSFLPTL RELHLDNNKL SRVPSGLPDL
KLLQVVYLHT NNITKVGVND FCPVGFGVKR AYYNGISLFN NPVPYWEVQP ATFRCVTDRL
AIQFGNYKK