P21810 (PGS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biglycan

Alternative name(s):
Bone/cartilage proteoglycan I
PG-S1

Gene names

Name:	BGN
Synonyms:	SLRR1A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in collagen fiber assembly By similarity.
Subunit structure	Homodimer. Forms a ternary complex with MFAP2 and ELN By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Found in several connective tissues, especially in articular cartilages.
Post-translational modification	The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate By similarity.
Sequence similarities	Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily. Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	proteinaceous extracellular matrix Non-traceable author statement Ref.2. Source: UniProtKB transport vesicle Inferred from direct assay. Source: LIFEdb
Molecular function	extracellular matrix structural constituent Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 37	18			PRO_0000032691
	Chain	38 – 368	331	Biglycan		PRO_0000032692
Regions
	Repeat	82 – 102	21	LRR 1
	Repeat	103 – 126	24	LRR 2
	Repeat	127 – 150	24	LRR 3
	Repeat	151 – 171	21	LRR 4
	Repeat	172 – 195	24	LRR 5
	Repeat	196 – 220	25	LRR 6
	Repeat	221 – 241	21	LRR 7
	Repeat	242 – 265	24	LRR 8
	Repeat	266 – 289	24	LRR 9
	Repeat	290 – 312	23	LRR 10
	Repeat	313 – 342	30	LRR 11
	Repeat	343 – 368	26	LRR 12
	Compositional bias	63 – 76	14	Cys-rich
Amino acid modifications
	Glycosylation	42	1	O-linked (Xyl...) (glycosaminoglycan) Ref.8
	Glycosylation	47	1	O-linked (Xyl...) (glycosaminoglycan) Ref.8
	Glycosylation	180	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	198	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	270	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	311	1	N-linked (GlcNAc...) Ref.11
	Disulfide bond	63 ↔ 69		By similarity
	Disulfide bond	67 ↔ 76		By similarity
	Disulfide bond	321 ↔ 354		By similarity
Natural variations
	Natural variant	266	1	R → T in a breast cancer sample; somatic mutation. Ref.12		VAR_036605
	Natural variant	288	1	K → N in a breast cancer sample; somatic mutation. Ref.12		VAR_036606
Experimental info
	Sequence conflict	139 – 140	2	KL → NV in AAA52287. Ref.1
	Sequence conflict	163 – 164	2	EL → DV Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21810 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: BF16F304C5CD3B3E	FASTA	368	41,654
	10 20 30 40 50 60 MWPLWRLVSL LALSQALPFE QRGFWDFTLD DGPFMMNDEE ASGADTSGVL DPDSVTPTYS 70 80 90 100 110 120 AMCPFGCHCH LRVVQCSDLG LKSVPKEISP DTTLLDLQNN DISELRKDDF KGLQHLYALV 130 140 150 160 170 180 LVNNKISKIH EKAFSPLRKL QKLYISKNHL VEIPPNLPSS LVELRIHDNR IRKVPKGVFS 190 200 210 220 230 240 GLRNMNCIEM GGNPLENSGF EPGAFDGLKL NYLRISEAKL TGIPKDLPET LNELHLDHNK 250 260 270 280 290 300 IQAIELEDLL RYSKLYRLGL GHNQIRMIEN GSLSFLPTLR ELHLDNNKLA RVPSGLPDLK 310 320 330 340 350 360 LLQVVYLHSN NITKVGVNDF CPMGFGVKRA YYNGISLFNN PVPYWEVQPA TFRCVTDRLA IQFGNYKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species." Fisher L.W., Termine J.D., Young M.F. J. Biol. Chem. 264:4571-4576(1989) [PubMed: 2647739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Bone.
[2]	"Human biglycan gene. Putative promoter, intron-exon junctions, and chromosomal localization." Fisher L.W., Heegaard A.M., Vetter U., Vogel W., Just W., Termine J.D., Young M.F. J. Biol. Chem. 266:14371-14377(1991) [PubMed: 1860845] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Comparative genome sequence analysis of the Bpa/Str region in mouse and man." Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. , Kimberley C., Goerdes M., Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., Brown S.D.M. Genome Res. 10:758-775(2000) [PubMed: 10854409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[8]	"Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II." Roughley P.J., White R.J. Biochem. J. 262:823-827(1989) [PubMed: 2590169] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-57.
[9]	"Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone." Fisher L.W., Hawkins G.R., Tuross N., Termine J.D. J. Biol. Chem. 262:9702-9708(1987) [PubMed: 3597437] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-66.
[10]	"Dinucleotide repeat polymorphism at the human biglycan (BGN) locus." Just W., Rau W., Muller R., Geerkens C., Vogel W. Hum. Mol. Genet. 3:2268-2268(1994) [PubMed: 7881444] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-368. Tissue: Skin.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-311, MASS SPECTROMETRY. Tissue: Liver.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-266 AND ASN-288.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04599 mRNA. Translation: AAA36009.1. M65153, M65152 Genomic DNA. Translation: AAA52287.1. Sequence problems. U82695 Genomic DNA. No translation available. BT007323 mRNA. Translation: AAP35987.1. CH471172 Genomic DNA. Translation: EAW72863.1. CH471172 Genomic DNA. Translation: EAW72864.1. BC002416 mRNA. Translation: AAH02416.1. BC004244 mRNA. Translation: AAH04244.1. U11686 mRNA. Translation: AAC50117.1.
IPI	IPI00010790.
PIR	BGHUN. A40757.
RefSeq	NP_001702.1. NM_001711.4.
UniGene	Hs.821.
3D structure databases
ProteinModelPortal	P21810.
SMR	P21810. Positions 61-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21810. 7 interactions.
STRING	P21810.
Polymorphism databases
DMDM	266762.
Proteomic databases
PRIDE	P21810.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331595; ENSP00000327336; ENSG00000182492.
GeneID	633.
KEGG	hsa:633.
UCSC	uc004fhr.1. human.
Organism-specific databases
CTD	633.
GeneCards	GC0XP152762.
H-InvDB	HIX0017130.
HGNC	HGNC:1044. BGN.
HPA	CAB003678. HPA003157.
MIM	301870. gene.
neXtProt	NX_P21810.
PharmGKB	PA25346.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18351.
HOGENOM	HBG714459.
HOVERGEN	HBG016052.
InParanoid	P21810.
OMA	RLAIQFG.
OrthoDB	EOG4868CN.
PhylomeDB	P21810.
Gene expression databases
ArrayExpress	P21810.
Bgee	P21810.
CleanEx	HS_BGN.
Genevestigator	P21810.
GermOnline	ENSG00000182492. Homo sapiens.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR000372. LRR-contain_N. IPR016352. SLRP_I_decor/aspor/byglycan. [Graphical view]
KO	K08118.
Pfam	PF00560. LRR_1. 1 hit. PF01462. LRRNT. 1 hit. [Graphical view]
PIRSF	PIRSF002490. SLRP_I. 1 hit.
SMART	SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 8 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	2558.
PMAP-CutDB	P21810.
SOURCE	Search...

Entry information

Entry name

PGS1_HUMAN

Accession

Primary (citable) accession number: P21810
Secondary accession number(s): D3DWU3, P13247

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	April 1, 1993
Last modified:	January 25, 2012
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.