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Protein

Biglycan

Gene

BGN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in collagen fiber assembly.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-BTA-2022870. Chondroitin sulfate biosynthesis.
R-BTA-2022923. Dermatan sulfate biosynthesis.
R-BTA-2024101. CS/DS degradation.
R-BTA-3000178. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Biglycan
Alternative name(s):
Bone/cartilage proteoglycan I
Leucine-rich PG I
PG-S1
Gene namesi
Name:BGN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Propeptidei17 – 37212 PublicationsPRO_0000032685Add
BLAST
Chaini38 – 369332BiglycanPRO_0000032686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421O-linked (Xyl...) (glycosaminoglycan)
Glycosylationi48 – 481O-linked (Xyl...) (glycosaminoglycan)
Disulfide bondi64 ↔ 701 Publication
Disulfide bondi68 ↔ 771 Publication
Glycosylationi181 – 1811O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi199 – 1991O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)
Glycosylationi312 – 3121N-linked (GlcNAc...)1 Publication
Disulfide bondi322 ↔ 3551 Publication

Post-translational modificationi

The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate.

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP21809.
PRIDEiP21809.

Expressioni

Tissue specificityi

Found in several connective tissues, especially in articular cartilages.

Interactioni

Subunit structurei

Homodimer. Forms a ternary complex with MFAP2 and ELN.1 Publication

Protein-protein interaction databases

IntActiP21809. 4 interactions.
STRINGi9913.ENSBTAP00000044462.

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi69 – 713Combined sources
Beta strandi74 – 763Combined sources
Beta strandi95 – 973Combined sources
Turni108 – 1136Combined sources
Beta strandi119 – 1213Combined sources
Helixi132 – 1343Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi164 – 1663Combined sources
Helixi178 – 1803Combined sources
Beta strandi188 – 1903Combined sources
Helixi198 – 2003Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi226 – 2283Combined sources
Helixi273 – 2764Combined sources
Beta strandi282 – 2843Combined sources
Helixi297 – 2993Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi340 – 3434Combined sources
Helixi345 – 3473Combined sources
Helixi350 – 3534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FT3X-ray3.40A/B/C/D/E/F38-369[»]
ProteinModelPortaliP21809.
SMRiP21809. Positions 62-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati83 – 10321LRR 1Add
BLAST
Repeati104 – 12724LRR 2Add
BLAST
Repeati128 – 15124LRR 3Add
BLAST
Repeati152 – 17221LRR 4Add
BLAST
Repeati173 – 19624LRR 5Add
BLAST
Repeati197 – 22125LRR 6Add
BLAST
Repeati222 – 24221LRR 7Add
BLAST
Repeati243 – 26624LRR 8Add
BLAST
Repeati267 – 29024LRR 9Add
BLAST
Repeati291 – 31323LRR 10Add
BLAST
Repeati314 – 34330LRR 11Add
BLAST
Repeati344 – 36926LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi64 – 7714Cys-richAdd
BLAST

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP21809.
KOiK08118.
OMAiQRGFWDF.
OrthoDBiEOG76739V.
TreeFamiTF334562.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028547. Biglycan.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF6. PTHR24369:SF6. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPLWPLAAL LALSQALPFE QKAFWDFTLD DGLPMLNDEE ASGAETTSGI
60 70 80 90 100
PDLDSLPPTY SAMCPFGCHC HLRVVQCSDL GLKAVPKEIS PDTTLLDLQN
110 120 130 140 150
NDISELRKDD FKGLQHLYAL VLVNNKISKI HEKAFSPLRK LQKLYISKNH
160 170 180 190 200
LVEIPPNLPS SLVELRIHDN RIRKVPKGVF SGLRNMNCIE MGGNPLENSG
210 220 230 240 250
FEPGAFDGLK LNYLRISEAK LTGIPKDLPE TLNELHLDHN KIQAIELEDL
260 270 280 290 300
LRYSKLYRLG LGHNQIRMIE NGSLSFLPTL RELHLDNNKL SRVPAGLPDL
310 320 330 340 350
KLLQVVYLHT NNITKVGVND FCPVGFGVKR AYYNGISLFN NPVPYWEVQP
360
ATFRCVTDRL AIQFGNYKK
Length:369
Mass (Da):41,590
Last modified:May 2, 2006 - v3
Checksum:iB86C2149723AD0DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521V → C in AAB46746 (PubMed:8673009).Curated
Sequence conflicti188 – 1881C → E AA sequence (PubMed:2656687).Curated
Sequence conflicti354 – 3541R → A in AAB46746 (PubMed:8673009).Curated
Sequence conflicti368 – 3692KK → Y AA sequence (PubMed:2656687).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82652 mRNA. Translation: AAB46746.2.
BT021201 mRNA. Translation: AAX31383.1.
BC118460 mRNA. Translation: AAI18461.1.
PIRiS32559.
RefSeqiNP_847888.2. NM_178318.4.
XP_005227715.1. XM_005227658.3.
UniGeneiBt.5351.

Genome annotation databases

EnsembliENSBTAT00000047242; ENSBTAP00000044462; ENSBTAG00000005250.
GeneIDi280733.
KEGGibta:280733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82652 mRNA. Translation: AAB46746.2.
BT021201 mRNA. Translation: AAX31383.1.
BC118460 mRNA. Translation: AAI18461.1.
PIRiS32559.
RefSeqiNP_847888.2. NM_178318.4.
XP_005227715.1. XM_005227658.3.
UniGeneiBt.5351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FT3X-ray3.40A/B/C/D/E/F38-369[»]
ProteinModelPortaliP21809.
SMRiP21809. Positions 62-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21809. 4 interactions.
STRINGi9913.ENSBTAP00000044462.

Proteomic databases

PaxDbiP21809.
PRIDEiP21809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000047242; ENSBTAP00000044462; ENSBTAG00000005250.
GeneIDi280733.
KEGGibta:280733.

Organism-specific databases

CTDi633.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP21809.
KOiK08118.
OMAiQRGFWDF.
OrthoDBiEOG76739V.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiR-BTA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-BTA-2022870. Chondroitin sulfate biosynthesis.
R-BTA-2022923. Dermatan sulfate biosynthesis.
R-BTA-2024101. CS/DS degradation.
R-BTA-3000178. ECM proteoglycans.

Miscellaneous databases

EvolutionaryTraceiP21809.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028547. Biglycan.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF6. PTHR24369:SF6. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of bovine aorta biglycan core protein deduced from cloned cDNA."
    Xu J.H., Radhakrishnamurthy B., Srinivasan S.R., Berenson G.S.
    Biochem. Mol. Biol. Int. 37:263-272(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Aorta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal lung.
  4. "The primary structure of the core protein of the small, leucine-rich proteoglycan (PG I) from bovine articular cartilage."
    Neame P.J., Choi H.U., Rosenberg L.C.
    J. Biol. Chem. 264:8653-8661(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-369.
    Tissue: Cartilage.
  5. "Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography."
    Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C., Neame P.J.
    J. Biol. Chem. 264:2876-2884(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-63.
    Tissue: Cartilage.
  6. "Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1."
    Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.
    J. Biol. Chem. 277:3950-3957(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MFAP2 AND ELN.
  7. "Crystal structure of the biglycan dimer and evidence that dimerization is essential for folding and stability of class I small leucine-rich repeat proteoglycans."
    Scott P.G., Dodd C.M., Bergmann E.M., Sheehan J.K., Bishop P.N.
    J. Biol. Chem. 281:13324-13332(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 38-369, DISULFIDE BONDS, SUBUNIT, GLYCOSYLATION AT ASN-312.

Entry informationi

Entry nameiPGS1_BOVIN
AccessioniPrimary (citable) accession number: P21809
Secondary accession number(s): P79259, Q17QB0, Q5BIM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 2, 2006
Last modified: June 8, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.