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Q08380 (LG3BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galectin-3-binding protein
Alternative name(s):
Basement membrane autoantigen p105
Lectin galactoside-binding soluble 3-binding protein
Mac-2-binding protein
Short name=MAC2BP
Short name=Mac-2 BP
Tumor-associated antigen 90K
Gene names
Name:LGALS3BP
Synonyms:M2BP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells. Ref.2 Ref.7 Ref.15

Subunit structure

Homodimers and homomultimers. The multimers form ring-like structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID. Ref.6

Subcellular location

Secreted. Secretedextracellular spaceextracellular matrix Ref.1 Ref.15.

Tissue specificity

Ubiquitous. Detected in body fluids such as semen, milk, serum, tears, saliva and urine. Expressed by keratinocytes and fibroblasts. Ref.1 Ref.2 Ref.5

Sequence similarities

Contains 1 BACK (BTB/Kelch associated) domain.

Contains 1 BTB (POZ) domain.

Contains 1 SRCR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1 Ref.4 Ref.5
Chain19 – 585567Galectin-3-binding protein
PRO_0000033230

Regions

Domain24 – 124101SRCR
Domain153 – 22169BTB
Domain260 – 360101BACK

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) (complex) Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Glycosylation1251N-linked (GlcNAc...) Ref.9 Ref.12
Glycosylation1921N-linked (GlcNAc...) Ref.9 Ref.12
Glycosylation3621N-linked (GlcNAc...)
Glycosylation3981N-linked (GlcNAc...) (complex) Ref.9 Ref.10 Ref.12 Ref.13
Glycosylation5511N-linked (GlcNAc...) (complex) Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Glycosylation5801N-linked (GlcNAc...) (complex) Ref.9 Ref.10 Ref.13
Disulfide bond49 ↔ 113
Disulfide bond62 ↔ 123
Disulfide bond93 ↔ 103

Experimental info

Sequence conflict191V → S AA sequence Ref.5
Sequence conflict251R → C AA sequence Ref.4
Sequence conflict251R → P AA sequence Ref.4
Sequence conflict261L → M AA sequence Ref.5
Sequence conflict30 – 312GA → ED AA sequence Ref.5
Sequence conflict361R → H AA sequence Ref.5
Sequence conflict361R → L AA sequence Ref.4

Secondary structure

..................... 585
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08380 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C488C2E99D77435B

FASTA58565,331
        10         20         30         40         50         60 
MTPPRLFWVW LLVAGTQGVN DGDMRLADGG ATNQGRVEIF YRGQWGTVCD NLWDLTDASV 

        70         80         90        100        110        120 
VCRALGFENA TQALGRAAFG QGSGPIMLDE VQCTGTEASL ADCKSLGWLK SNCRHERDAG 

       130        140        150        160        170        180 
VVCTNETRST HTLDLSRELS EALGQIFDSQ RGCDLSISVN VQGEDALGFC GHTVILTANL 

       190        200        210        220        230        240 
EAQALWKEPG SNVTMSVDAE CVPMVRDLLR YFYSRRIDIT LSSVKCFHKL ASAYGARQLQ 

       250        260        270        280        290        300 
GYCASLFAIL LPQDPSFQMP LDLYAYAVAT GDALLEKLCL QFLAWNFEAL TQAEAWPSVP 

       310        320        330        340        350        360 
TDLLQLLLPR SDLAVPSELA LLKAVDTWSW GERASHEEVE GLVEKIRFPM MLPEELFELQ 

       370        380        390        400        410        420 
FNLSLYWSHE ALFQKKTLQA LEFHTVPFQL LARYKGLNLT EDTYKPRIYT SPTWSAFVTD 

       430        440        450        460        470        480 
SSWSARKSQL VYQSRRGPLV KYSSDYFQAP SDYRYYPYQS FQTPQHPSFL FQDKRVSWSL 

       490        500        510        520        530        540 
VYLPTIQSCW NYGFSCSSDE LPVLGLTKSG GSDRTIAYEN KALMLCEGLF VADVTDFEGW 

       550        560        570        580 
KAAIPSALDT NSSKSTSSFP CPAGHFNGFR TVIRPFYLTN SSGVD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain."
Koths K., Taylor E., Halenbeck R., Casipit C., Wang A.
J. Biol. Chem. 268:14245-14249(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-34; 188-191; 193-200; 202-207; 230-242; 244-259; 261-267; 324-328 AND 437-440, INTERACTION WITH LGALS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"The secreted tumor-associated antigen 90K is a potent immune stimulator."
Ullrich A., Sures I., D'Egido M., Jallal B., Powell T.J., Herbst R., Dreps A., Azam M., Rubinstein M., Natoli C.
J. Biol. Chem. 269:18401-18407(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, TISSUE SPECIFICITY.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Lung.
[4]"Purification and characterization of a 90 kDa protein released from human tumors and tumor cell lines."
Iacobelli S., Bucci I., D'Egidio M., Giuliani C., Natoli C., Tinari N., Rubistein M., Schlessinger J.
FEBS Lett. 319:59-65(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-40.
Tissue: Ascites and Serum.
[5]"The 105-kDa basement membrane autoantigen p105 is N-terminally homologous to a tumor-associated antigen."
Chan L.S., Woodley D.T.
J. Invest. Dermatol. 107:209-214(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-38, TISSUE SPECIFICITY.
Tissue: Fibroblast.
[6]"Functional studies on recombinant domains of Mac-2-binding protein."
Hellstern S., Sasaki T., Fauser C., Lustig A., Timpl R., Engel J.
J. Biol. Chem. 277:15690-15696(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 442-446, GLYCOSYLATION, INTERACTION WITH LGALS3, SUBUNIT STRUCTURE.
[7]"Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation."
Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S., Liu F.-T.
Int. J. Cancer 91:167-172(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGALS1 AND LGALS3.
[8]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
Tissue: Bile.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192; ASN-398; ASN-551 AND ASN-580.
Tissue: Plasma.
[10]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 AND ASN-580.
Tissue: Saliva.
[11]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551.
Tissue: Milk.
[12]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192; ASN-398 AND ASN-551.
Tissue: Liver.
[13]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-69; ASN-398; ASN-551 AND ASN-580.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin."
Sasaki T., Brakebusch C., Engel J., Timpl R.
EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-133, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, INTERACTION WITH ITGB1; COL4A1; COL5A1; COL6A1; LGALS3; FN1 AND NID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13210 mRNA. Translation: AAA36193.1.
X79089 mRNA. Translation: CAA55699.1.
BC002403 mRNA. Translation: AAH02403.1.
BC002998 mRNA. Translation: AAH02998.1.
BC015761 mRNA. Translation: AAH15761.1.
CCDSCCDS11759.1.
PIRA47161.
A55899.
RefSeqNP_005558.1. NM_005567.3.
UniGeneHs.514535.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY2X-ray2.00A19-133[»]
ProteinModelPortalQ08380.
SMRQ08380. Positions 18-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110150. 52 interactions.
IntActQ08380. 27 interactions.
MINTMINT-1153112.
STRING9606.ENSP00000262776.

PTM databases

PhosphoSiteQ08380.

Polymorphism databases

DMDM47115668.

Proteomic databases

MaxQBQ08380.
PaxDbQ08380.
PeptideAtlasQ08380.
PRIDEQ08380.

Protocols and materials databases

DNASU3959.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262776; ENSP00000262776; ENSG00000108679.
GeneID3959.
KEGGhsa:3959.
UCSCuc002jwh.3. human.

Organism-specific databases

CTD3959.
GeneCardsGC17M076970.
HGNCHGNC:6564. LGALS3BP.
HPACAB002158.
HPA000554.
MIM600626. gene.
neXtProtNX_Q08380.
PharmGKBPA30341.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41083.
HOGENOMHOG000113318.
HOVERGENHBG052323.
InParanoidQ08380.
KOK17300.
OMAQHPSFLF.
OrthoDBEOG7JDQXP.
PhylomeDBQ08380.
TreeFamTF331368.

Gene expression databases

ArrayExpressQ08380.
BgeeQ08380.
CleanExHS_LGALS3BP.
GenevestigatorQ08380.

Family and domain databases

Gene3D3.10.250.10. 1 hit.
3.30.710.10. 1 hit.
InterProIPR011705. BACK.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamPF07707. BACK. 1 hit.
PF00530. SRCR. 1 hit.
[Graphical view]
PRINTSPR00258. SPERACTRCPTR.
SMARTSM00875. BACK. 1 hit.
SM00202. SR. 1 hit.
[Graphical view]
SUPFAMSSF56487. SSF56487. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ08380.
GeneWikiLGALS3BP.
GenomeRNAi3959.
NextBio15536.
PMAP-CutDBQ08380.
PROQ08380.
SOURCESearch...

Entry information

Entry nameLG3BP_HUMAN
AccessionPrimary (citable) accession number: Q08380
Secondary accession number(s): Q7M4S0 expand/collapse secondary AC list , Q9UCH8, Q9UCH9, Q9UCI0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM