Full text data of LGALS3BP
LGALS3BP
(M2BP)
[Confidence: low (only semi-automatic identification from reviews)]
Galectin-3-binding protein (Basement membrane autoantigen p105; Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; MAC2BP; Mac-2 BP; Tumor-associated antigen 90K; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Galectin-3-binding protein (Basement membrane autoantigen p105; Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; MAC2BP; Mac-2 BP; Tumor-associated antigen 90K; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q08380
ID LG3BP_HUMAN Reviewed; 585 AA.
AC Q08380; Q7M4S0; Q9UCH8; Q9UCH9; Q9UCI0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Galectin-3-binding protein;
DE AltName: Full=Basement membrane autoantigen p105;
DE AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE AltName: Full=Mac-2-binding protein;
DE Short=MAC2BP;
DE Short=Mac-2 BP;
DE AltName: Full=Tumor-associated antigen 90K;
DE Flags: Precursor;
GN Name=LGALS3BP; Synonyms=M2BP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-34; 188-191;
RP 193-200; 202-207; 230-242; 244-259; 261-267; 324-328 AND 437-440,
RP INTERACTION WITH LGALS3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8390986;
RA Koths K., Taylor E., Halenbeck R., Casipit C., Wang A.;
RT "Cloning and characterization of a human Mac-2-binding protein, a new
RT member of the superfamily defined by the macrophage scavenger receptor
RT cysteine-rich domain.";
RL J. Biol. Chem. 268:14245-14249(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8034587;
RA Ullrich A., Sures I., D'Egido M., Jallal B., Powell T.J., Herbst R.,
RA Dreps A., Azam M., Rubinstein M., Natoli C.;
RT "The secreted tumor-associated antigen 90K is a potent immune
RT stimulator.";
RL J. Biol. Chem. 269:18401-18407(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 19-40.
RC TISSUE=Ascites, and Serum;
RX PubMed=8454062; DOI=10.1016/0014-5793(93)80037-U;
RA Iacobelli S., Bucci I., D'Egidio M., Giuliani C., Natoli C.,
RA Tinari N., Rubistein M., Schlessinger J.;
RT "Purification and characterization of a 90 kDa protein released from
RT human tumors and tumor cell lines.";
RL FEBS Lett. 319:59-65(1993).
RN [5]
RP PROTEIN SEQUENCE OF 19-38, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=8757764; DOI=10.1111/1523-1747.ep12329629;
RA Chan L.S., Woodley D.T.;
RT "The 105-kDa basement membrane autoantigen p105 is N-terminally
RT homologous to a tumor-associated antigen.";
RL J. Invest. Dermatol. 107:209-214(1996).
RN [6]
RP PROTEIN SEQUENCE OF 442-446, GLYCOSYLATION, INTERACTION WITH LGALS3,
RP AND SUBUNIT STRUCTURE.
RX PubMed=11867635; DOI=10.1074/jbc.M200386200;
RA Hellstern S., Sasaki T., Fauser C., Lustig A., Timpl R., Engel J.;
RT "Functional studies on recombinant domains of Mac-2-binding protein.";
RL J. Biol. Chem. 277:15690-15696(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH LGALS1 AND LGALS3.
RX PubMed=11146440;
RX DOI=10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q;
RA Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S.,
RA Liu F.-T.;
RT "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates
RT galectin-1-induced cell aggregation.";
RL Int. J. Cancer 91:167-172(2001).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192;
RP ASN-398; ASN-551 AND ASN-580, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 AND
RP ASN-580, AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551, AND MASS
RP SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192;
RP ASN-398 AND ASN-551, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP GLYCOSYLATION AT ASN-69; ASN-398; ASN-551 AND ASN-580.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-133, FUNCTION, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND INTERACTION WITH ITGB1; COL4A1; COL5A1;
RP COL6A1; LGALS3; FN1 AND NID.
RX PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT matrix which self-assembles into ring-like structures and binds beta1
RT integrins, collagens and fibronectin.";
RL EMBO J. 17:1606-1613(1998).
CC -!- FUNCTION: Promotes intergrin-mediated cell adhesion. May stimulate
CC host defense against viruses and tumor cells.
CC -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-
CC like structures with a diameter of 30-40 nm. Binds LGALS1 and
CC LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID.
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space,
CC extracellular matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in body fluids such as
CC semen, milk, serum, tears, saliva and urine. Expressed by
CC keratinocytes and fibroblasts.
CC -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC -!- SIMILARITY: Contains 1 SRCR domain.
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DR EMBL; L13210; AAA36193.1; -; mRNA.
DR EMBL; X79089; CAA55699.1; -; mRNA.
DR EMBL; BC002403; AAH02403.1; -; mRNA.
DR EMBL; BC002998; AAH02998.1; -; mRNA.
DR EMBL; BC015761; AAH15761.1; -; mRNA.
DR PIR; A47161; A47161.
DR PIR; A55899; A55899.
DR RefSeq; NP_005558.1; NM_005567.3.
DR UniGene; Hs.514535; -.
DR PDB; 1BY2; X-ray; 2.00 A; A=19-133.
DR PDBsum; 1BY2; -.
DR ProteinModelPortal; Q08380; -.
DR SMR; Q08380; 18-127.
DR IntAct; Q08380; 27.
DR MINT; MINT-1153112; -.
DR STRING; 9606.ENSP00000262776; -.
DR PhosphoSite; Q08380; -.
DR DMDM; 47115668; -.
DR PaxDb; Q08380; -.
DR PeptideAtlas; Q08380; -.
DR PRIDE; Q08380; -.
DR DNASU; 3959; -.
DR Ensembl; ENST00000262776; ENSP00000262776; ENSG00000108679.
DR GeneID; 3959; -.
DR KEGG; hsa:3959; -.
DR UCSC; uc002jwh.3; human.
DR CTD; 3959; -.
DR GeneCards; GC17M076970; -.
DR HGNC; HGNC:6564; LGALS3BP.
DR HPA; CAB002158; -.
DR HPA; HPA000554; -.
DR MIM; 600626; gene.
DR neXtProt; NX_Q08380; -.
DR PharmGKB; PA30341; -.
DR eggNOG; NOG41083; -.
DR HOGENOM; HOG000113318; -.
DR HOVERGEN; HBG052323; -.
DR InParanoid; Q08380; -.
DR KO; K17300; -.
DR OMA; QHPSFLF; -.
DR OrthoDB; EOG7JDQXP; -.
DR PhylomeDB; Q08380; -.
DR EvolutionaryTrace; Q08380; -.
DR GeneWiki; LGALS3BP; -.
DR GenomeRNAi; 3959; -.
DR NextBio; 15536; -.
DR PMAP-CutDB; Q08380; -.
DR PRO; PR:Q08380; -.
DR ArrayExpress; Q08380; -.
DR Bgee; Q08380; -.
DR CleanEx; HS_LGALS3BP; -.
DR Genevestigator; Q08380; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ-like.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; Srcr_rcpt-rel.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1 18
FT CHAIN 19 585 Galectin-3-binding protein.
FT /FTId=PRO_0000033230.
FT DOMAIN 24 124 SRCR.
FT DOMAIN 153 221 BTB.
FT DOMAIN 260 360 BACK.
FT CARBOHYD 69 69 N-linked (GlcNAc...) (complex).
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT CARBOHYD 192 192 N-linked (GlcNAc...).
FT CARBOHYD 362 362 N-linked (GlcNAc...).
FT CARBOHYD 398 398 N-linked (GlcNAc...) (complex).
FT CARBOHYD 551 551 N-linked (GlcNAc...) (complex).
FT CARBOHYD 580 580 N-linked (GlcNAc...) (complex).
FT DISULFID 49 113
FT DISULFID 62 123
FT DISULFID 93 103
FT CONFLICT 19 19 V -> S (in Ref. 5; AA sequence).
FT CONFLICT 25 25 R -> C (in Ref. 4; AA sequence).
FT CONFLICT 25 25 R -> P (in Ref. 4; AA sequence).
FT CONFLICT 26 26 L -> M (in Ref. 5; AA sequence).
FT CONFLICT 30 31 GA -> ED (in Ref. 5; AA sequence).
FT CONFLICT 36 36 R -> H (in Ref. 5; AA sequence).
FT CONFLICT 36 36 R -> L (in Ref. 4; AA sequence).
FT STRAND 24 28
FT STRAND 34 41
FT STRAND 44 49
FT HELIX 55 64
FT STRAND 70 74
FT TURN 76 79
FT STRAND 86 88
FT HELIX 100 102
FT HELIX 115 117
FT STRAND 120 123
SQ SEQUENCE 585 AA; 65331 MW; C488C2E99D77435B CRC64;
MTPPRLFWVW LLVAGTQGVN DGDMRLADGG ATNQGRVEIF YRGQWGTVCD NLWDLTDASV
VCRALGFENA TQALGRAAFG QGSGPIMLDE VQCTGTEASL ADCKSLGWLK SNCRHERDAG
VVCTNETRST HTLDLSRELS EALGQIFDSQ RGCDLSISVN VQGEDALGFC GHTVILTANL
EAQALWKEPG SNVTMSVDAE CVPMVRDLLR YFYSRRIDIT LSSVKCFHKL ASAYGARQLQ
GYCASLFAIL LPQDPSFQMP LDLYAYAVAT GDALLEKLCL QFLAWNFEAL TQAEAWPSVP
TDLLQLLLPR SDLAVPSELA LLKAVDTWSW GERASHEEVE GLVEKIRFPM MLPEELFELQ
FNLSLYWSHE ALFQKKTLQA LEFHTVPFQL LARYKGLNLT EDTYKPRIYT SPTWSAFVTD
SSWSARKSQL VYQSRRGPLV KYSSDYFQAP SDYRYYPYQS FQTPQHPSFL FQDKRVSWSL
VYLPTIQSCW NYGFSCSSDE LPVLGLTKSG GSDRTIAYEN KALMLCEGLF VADVTDFEGW
KAAIPSALDT NSSKSTSSFP CPAGHFNGFR TVIRPFYLTN SSGVD
//
ID LG3BP_HUMAN Reviewed; 585 AA.
AC Q08380; Q7M4S0; Q9UCH8; Q9UCH9; Q9UCI0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Galectin-3-binding protein;
DE AltName: Full=Basement membrane autoantigen p105;
DE AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE AltName: Full=Mac-2-binding protein;
DE Short=MAC2BP;
DE Short=Mac-2 BP;
DE AltName: Full=Tumor-associated antigen 90K;
DE Flags: Precursor;
GN Name=LGALS3BP; Synonyms=M2BP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-34; 188-191;
RP 193-200; 202-207; 230-242; 244-259; 261-267; 324-328 AND 437-440,
RP INTERACTION WITH LGALS3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8390986;
RA Koths K., Taylor E., Halenbeck R., Casipit C., Wang A.;
RT "Cloning and characterization of a human Mac-2-binding protein, a new
RT member of the superfamily defined by the macrophage scavenger receptor
RT cysteine-rich domain.";
RL J. Biol. Chem. 268:14245-14249(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8034587;
RA Ullrich A., Sures I., D'Egido M., Jallal B., Powell T.J., Herbst R.,
RA Dreps A., Azam M., Rubinstein M., Natoli C.;
RT "The secreted tumor-associated antigen 90K is a potent immune
RT stimulator.";
RL J. Biol. Chem. 269:18401-18407(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 19-40.
RC TISSUE=Ascites, and Serum;
RX PubMed=8454062; DOI=10.1016/0014-5793(93)80037-U;
RA Iacobelli S., Bucci I., D'Egidio M., Giuliani C., Natoli C.,
RA Tinari N., Rubistein M., Schlessinger J.;
RT "Purification and characterization of a 90 kDa protein released from
RT human tumors and tumor cell lines.";
RL FEBS Lett. 319:59-65(1993).
RN [5]
RP PROTEIN SEQUENCE OF 19-38, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=8757764; DOI=10.1111/1523-1747.ep12329629;
RA Chan L.S., Woodley D.T.;
RT "The 105-kDa basement membrane autoantigen p105 is N-terminally
RT homologous to a tumor-associated antigen.";
RL J. Invest. Dermatol. 107:209-214(1996).
RN [6]
RP PROTEIN SEQUENCE OF 442-446, GLYCOSYLATION, INTERACTION WITH LGALS3,
RP AND SUBUNIT STRUCTURE.
RX PubMed=11867635; DOI=10.1074/jbc.M200386200;
RA Hellstern S., Sasaki T., Fauser C., Lustig A., Timpl R., Engel J.;
RT "Functional studies on recombinant domains of Mac-2-binding protein.";
RL J. Biol. Chem. 277:15690-15696(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH LGALS1 AND LGALS3.
RX PubMed=11146440;
RX DOI=10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q;
RA Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S.,
RA Liu F.-T.;
RT "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates
RT galectin-1-induced cell aggregation.";
RL Int. J. Cancer 91:167-172(2001).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192;
RP ASN-398; ASN-551 AND ASN-580, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 AND
RP ASN-580, AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551, AND MASS
RP SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192;
RP ASN-398 AND ASN-551, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP GLYCOSYLATION AT ASN-69; ASN-398; ASN-551 AND ASN-580.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-133, FUNCTION, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND INTERACTION WITH ITGB1; COL4A1; COL5A1;
RP COL6A1; LGALS3; FN1 AND NID.
RX PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT matrix which self-assembles into ring-like structures and binds beta1
RT integrins, collagens and fibronectin.";
RL EMBO J. 17:1606-1613(1998).
CC -!- FUNCTION: Promotes intergrin-mediated cell adhesion. May stimulate
CC host defense against viruses and tumor cells.
CC -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-
CC like structures with a diameter of 30-40 nm. Binds LGALS1 and
CC LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID.
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space,
CC extracellular matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in body fluids such as
CC semen, milk, serum, tears, saliva and urine. Expressed by
CC keratinocytes and fibroblasts.
CC -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC -!- SIMILARITY: Contains 1 SRCR domain.
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DR EMBL; L13210; AAA36193.1; -; mRNA.
DR EMBL; X79089; CAA55699.1; -; mRNA.
DR EMBL; BC002403; AAH02403.1; -; mRNA.
DR EMBL; BC002998; AAH02998.1; -; mRNA.
DR EMBL; BC015761; AAH15761.1; -; mRNA.
DR PIR; A47161; A47161.
DR PIR; A55899; A55899.
DR RefSeq; NP_005558.1; NM_005567.3.
DR UniGene; Hs.514535; -.
DR PDB; 1BY2; X-ray; 2.00 A; A=19-133.
DR PDBsum; 1BY2; -.
DR ProteinModelPortal; Q08380; -.
DR SMR; Q08380; 18-127.
DR IntAct; Q08380; 27.
DR MINT; MINT-1153112; -.
DR STRING; 9606.ENSP00000262776; -.
DR PhosphoSite; Q08380; -.
DR DMDM; 47115668; -.
DR PaxDb; Q08380; -.
DR PeptideAtlas; Q08380; -.
DR PRIDE; Q08380; -.
DR DNASU; 3959; -.
DR Ensembl; ENST00000262776; ENSP00000262776; ENSG00000108679.
DR GeneID; 3959; -.
DR KEGG; hsa:3959; -.
DR UCSC; uc002jwh.3; human.
DR CTD; 3959; -.
DR GeneCards; GC17M076970; -.
DR HGNC; HGNC:6564; LGALS3BP.
DR HPA; CAB002158; -.
DR HPA; HPA000554; -.
DR MIM; 600626; gene.
DR neXtProt; NX_Q08380; -.
DR PharmGKB; PA30341; -.
DR eggNOG; NOG41083; -.
DR HOGENOM; HOG000113318; -.
DR HOVERGEN; HBG052323; -.
DR InParanoid; Q08380; -.
DR KO; K17300; -.
DR OMA; QHPSFLF; -.
DR OrthoDB; EOG7JDQXP; -.
DR PhylomeDB; Q08380; -.
DR EvolutionaryTrace; Q08380; -.
DR GeneWiki; LGALS3BP; -.
DR GenomeRNAi; 3959; -.
DR NextBio; 15536; -.
DR PMAP-CutDB; Q08380; -.
DR PRO; PR:Q08380; -.
DR ArrayExpress; Q08380; -.
DR Bgee; Q08380; -.
DR CleanEx; HS_LGALS3BP; -.
DR Genevestigator; Q08380; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ-like.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; Srcr_rcpt-rel.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1 18
FT CHAIN 19 585 Galectin-3-binding protein.
FT /FTId=PRO_0000033230.
FT DOMAIN 24 124 SRCR.
FT DOMAIN 153 221 BTB.
FT DOMAIN 260 360 BACK.
FT CARBOHYD 69 69 N-linked (GlcNAc...) (complex).
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT CARBOHYD 192 192 N-linked (GlcNAc...).
FT CARBOHYD 362 362 N-linked (GlcNAc...).
FT CARBOHYD 398 398 N-linked (GlcNAc...) (complex).
FT CARBOHYD 551 551 N-linked (GlcNAc...) (complex).
FT CARBOHYD 580 580 N-linked (GlcNAc...) (complex).
FT DISULFID 49 113
FT DISULFID 62 123
FT DISULFID 93 103
FT CONFLICT 19 19 V -> S (in Ref. 5; AA sequence).
FT CONFLICT 25 25 R -> C (in Ref. 4; AA sequence).
FT CONFLICT 25 25 R -> P (in Ref. 4; AA sequence).
FT CONFLICT 26 26 L -> M (in Ref. 5; AA sequence).
FT CONFLICT 30 31 GA -> ED (in Ref. 5; AA sequence).
FT CONFLICT 36 36 R -> H (in Ref. 5; AA sequence).
FT CONFLICT 36 36 R -> L (in Ref. 4; AA sequence).
FT STRAND 24 28
FT STRAND 34 41
FT STRAND 44 49
FT HELIX 55 64
FT STRAND 70 74
FT TURN 76 79
FT STRAND 86 88
FT HELIX 100 102
FT HELIX 115 117
FT STRAND 120 123
SQ SEQUENCE 585 AA; 65331 MW; C488C2E99D77435B CRC64;
MTPPRLFWVW LLVAGTQGVN DGDMRLADGG ATNQGRVEIF YRGQWGTVCD NLWDLTDASV
VCRALGFENA TQALGRAAFG QGSGPIMLDE VQCTGTEASL ADCKSLGWLK SNCRHERDAG
VVCTNETRST HTLDLSRELS EALGQIFDSQ RGCDLSISVN VQGEDALGFC GHTVILTANL
EAQALWKEPG SNVTMSVDAE CVPMVRDLLR YFYSRRIDIT LSSVKCFHKL ASAYGARQLQ
GYCASLFAIL LPQDPSFQMP LDLYAYAVAT GDALLEKLCL QFLAWNFEAL TQAEAWPSVP
TDLLQLLLPR SDLAVPSELA LLKAVDTWSW GERASHEEVE GLVEKIRFPM MLPEELFELQ
FNLSLYWSHE ALFQKKTLQA LEFHTVPFQL LARYKGLNLT EDTYKPRIYT SPTWSAFVTD
SSWSARKSQL VYQSRRGPLV KYSSDYFQAP SDYRYYPYQS FQTPQHPSFL FQDKRVSWSL
VYLPTIQSCW NYGFSCSSDE LPVLGLTKSG GSDRTIAYEN KALMLCEGLF VADVTDFEGW
KAAIPSALDT NSSKSTSSFP CPAGHFNGFR TVIRPFYLTN SSGVD
//
MIM
600626
*RECORD*
*FIELD* NO
600626
*FIELD* TI
*600626 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 3 BINDING PROTEIN; LGALS3BP
;;MAC2-BINDING PROTEIN; MAC2BP;;
read moreSERUM PROTEIN 90K; 90K;;
L3 ANTIGEN
*FIELD* TX
CLONING
Using the monoclonal antibody SP-2, Iacobelli et al. (1986), Iacobelli
et al. (1988), and Iacobelli et al. (1993) identified a 90-kD protein,
designated serum protein 90K, that was found at elevated concentrations
in the serum of patients with various types of breast, lung, colorectal,
ovary, and endometrial cancer. Koths et al. (1993) cloned a cDNA
encoding 90K, which they called MAC2BP, from a human monocytic cell line
cDNA library using degenerate PCR primers based on the protein sequence.
MAC2BP is a 585-amino acid protein containing an N-terminal region that
is 45% identical to the extracellular, cysteine-rich domain of
macrophage scavenger receptor (MSR1; 153622), indicating that MAC2BP is
a member of the MSR1 superfamily. Koths et al. (1993) showed by
immunoblotting that breast milk, serum, semen, saliva, urine, and tears
likely contain MAC2B.
Ullrich et al. (1994) found by Northern blot analysis that all examined
normal tissues, with the exception of peripheral blood lymphocytes,
contain high levels of a 2.2-kb 90K transcript, with the highest levels
present in the gastrointestinal tissues. They also showed that primary
tumor samples and tumor cell lines express the 90K transcript at widely
varying levels.
GENE FUNCTION
Koths et al. (1993) found that MAC2BP specifically bound the human
macrophage-associated lectin LGALS3 (153619) via a carbohydrate-specific
interaction.
Ullrich et al. (1994) noted that 90K is present at elevated levels in
the serum of subpopulations of patients with AIDS. They demonstrated
that 90K could stimulate host defense systems, such as natural killer
cell and lymphokine-activated killer cell activities, and could induce
secretion of interleukin-2 (IL2; 147680). Ullrich et al. (1994)
suggested that oncogenic transformation, viral infection, or invasion by
pathogens enhances the production of 90K, which then stimulates the host
immune system via induction of IL2 and possibly other cytokines.
Using affinity chromatography and mass spectrometric analysis, Nonaka et
al. (2011) identified MAC2BP as a ligand for the lectin receptor DCSIGN
(CD209; 604672). DCSIGN recognized MAC2BP derived from some colorectal
carcinomas, but not from others. Recognition depended on the presence of
alpha-1,3,4-fucose moieties of Le glycans expressed on DCSIGN-binding
MAC2BP.
MAPPING
Calabrese et al. (1995) mapped the human 90K gene to chromosome 17q25 by
FISH. Brakebusch et al. (1997) used FISH to localize the mouse 90K gene
to chromosome 11, region E.
*FIELD* RF
1. Brakebusch, C.; Jallal, B.; Fusco, O.; Iacobelli, S.; Ullrich,
A.: Expression of the 90K immunostimulator gene is controlled by
a promoter with unique features. J. Biol. Chem. 272: 3674-3682,
1997.
2. Calabrese, G.; Sures, I.; Pompetti, F.; Natoli, G.; Palka, G.;
Iacobelli, S.: The gene (LGALS3BP) encoding the serum protein 90K,
associated with cancer and infection by the human immunodeficiency
virus, maps at 17q25. Cytogenet. Cell Genet. 69: 223-225, 1995.
3. Iacobelli, S.; Arno, E.; D'Orazio, A.; Coletti, G.: Detection
of antigens recognized by a novel monoclonal antibody in tissue and
serum from patients with breast cancer. Cancer Res. 46: 3005-3010,
1986.
4. Iacobelli, S.; Arno, E.; Sismondi, P.; Natoli, C.; Gentiloni, N.;
Scambia, G.; Giai, M.; Cortese, P.; Panici, P. B.; Mancuso, S.: Measurement
of a breast cancer associated antigen detected by monoclonal antibody
(SP-2) in sera of cancer patients. Breast Cancer Res. Treat. 11:
19-30, 1988.
5. Iacobelli, S.; Bucci, I.; D'Egidio, M.; Giuliani, C.; Natoli, C.;
Tinari, N.; Rubistein, M.; Schlessinger, J.: Purification and characterization
of a 90 kDa protein released from human tumors and tumor cell lines. FEBS
Lett. 319: 59-65, 1993.
6. Koths, K.; Taylor, E.; Halenbeck, R.; Casipit, C.; Wang, A.: 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. J. Biol. Chem. 268: 14245-14249, 1993.
7. Nonaka, M.; Ma, B. Y.; Imaeda, H.; Kawabe, K.; Kawasaki, N.; Hodohara,
K.; Kawasaki, N.; Andoh, A.; Fujiyama, Y.; Kawasaki, T.: Dendritic
cell-specific intercellular adhesion molecule 3-grabbing non-integrin
(DC-SIGN) recognizes a novel ligand, Mac-2-binding protein, characteristically
expressed on human colorectal carcinomas. J. Biol. Chem. 286: 22403-22413,
2011.
8. Ullrich, A.; Sures, I.; D'Egidio, M.; Jallal, B.; Powell, T. J.;
Herbst, R.; Dreps, A.; Azam, M.; Rubinstein, M.; Natoli, C.; Shawver,
L. K.; Schlessinger, J.; Iacobelli, S.: The secreted tumor-associated
antigen 90K is a potent immune stimulator. J. Biol. Chem. 269: 18401-18407,
1994.
*FIELD* CN
Patricia A. Hartz - updated: 10/21/2011
Patti M. Sherman - updated: 1/29/1998
*FIELD* CD
Victor A. McKusick: 6/27/1995
*FIELD* ED
mgross: 10/31/2011
terry: 10/21/2011
dholmes: 1/29/1998
mark: 6/27/1995
*RECORD*
*FIELD* NO
600626
*FIELD* TI
*600626 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 3 BINDING PROTEIN; LGALS3BP
;;MAC2-BINDING PROTEIN; MAC2BP;;
read moreSERUM PROTEIN 90K; 90K;;
L3 ANTIGEN
*FIELD* TX
CLONING
Using the monoclonal antibody SP-2, Iacobelli et al. (1986), Iacobelli
et al. (1988), and Iacobelli et al. (1993) identified a 90-kD protein,
designated serum protein 90K, that was found at elevated concentrations
in the serum of patients with various types of breast, lung, colorectal,
ovary, and endometrial cancer. Koths et al. (1993) cloned a cDNA
encoding 90K, which they called MAC2BP, from a human monocytic cell line
cDNA library using degenerate PCR primers based on the protein sequence.
MAC2BP is a 585-amino acid protein containing an N-terminal region that
is 45% identical to the extracellular, cysteine-rich domain of
macrophage scavenger receptor (MSR1; 153622), indicating that MAC2BP is
a member of the MSR1 superfamily. Koths et al. (1993) showed by
immunoblotting that breast milk, serum, semen, saliva, urine, and tears
likely contain MAC2B.
Ullrich et al. (1994) found by Northern blot analysis that all examined
normal tissues, with the exception of peripheral blood lymphocytes,
contain high levels of a 2.2-kb 90K transcript, with the highest levels
present in the gastrointestinal tissues. They also showed that primary
tumor samples and tumor cell lines express the 90K transcript at widely
varying levels.
GENE FUNCTION
Koths et al. (1993) found that MAC2BP specifically bound the human
macrophage-associated lectin LGALS3 (153619) via a carbohydrate-specific
interaction.
Ullrich et al. (1994) noted that 90K is present at elevated levels in
the serum of subpopulations of patients with AIDS. They demonstrated
that 90K could stimulate host defense systems, such as natural killer
cell and lymphokine-activated killer cell activities, and could induce
secretion of interleukin-2 (IL2; 147680). Ullrich et al. (1994)
suggested that oncogenic transformation, viral infection, or invasion by
pathogens enhances the production of 90K, which then stimulates the host
immune system via induction of IL2 and possibly other cytokines.
Using affinity chromatography and mass spectrometric analysis, Nonaka et
al. (2011) identified MAC2BP as a ligand for the lectin receptor DCSIGN
(CD209; 604672). DCSIGN recognized MAC2BP derived from some colorectal
carcinomas, but not from others. Recognition depended on the presence of
alpha-1,3,4-fucose moieties of Le glycans expressed on DCSIGN-binding
MAC2BP.
MAPPING
Calabrese et al. (1995) mapped the human 90K gene to chromosome 17q25 by
FISH. Brakebusch et al. (1997) used FISH to localize the mouse 90K gene
to chromosome 11, region E.
*FIELD* RF
1. Brakebusch, C.; Jallal, B.; Fusco, O.; Iacobelli, S.; Ullrich,
A.: Expression of the 90K immunostimulator gene is controlled by
a promoter with unique features. J. Biol. Chem. 272: 3674-3682,
1997.
2. Calabrese, G.; Sures, I.; Pompetti, F.; Natoli, G.; Palka, G.;
Iacobelli, S.: The gene (LGALS3BP) encoding the serum protein 90K,
associated with cancer and infection by the human immunodeficiency
virus, maps at 17q25. Cytogenet. Cell Genet. 69: 223-225, 1995.
3. Iacobelli, S.; Arno, E.; D'Orazio, A.; Coletti, G.: Detection
of antigens recognized by a novel monoclonal antibody in tissue and
serum from patients with breast cancer. Cancer Res. 46: 3005-3010,
1986.
4. Iacobelli, S.; Arno, E.; Sismondi, P.; Natoli, C.; Gentiloni, N.;
Scambia, G.; Giai, M.; Cortese, P.; Panici, P. B.; Mancuso, S.: Measurement
of a breast cancer associated antigen detected by monoclonal antibody
(SP-2) in sera of cancer patients. Breast Cancer Res. Treat. 11:
19-30, 1988.
5. Iacobelli, S.; Bucci, I.; D'Egidio, M.; Giuliani, C.; Natoli, C.;
Tinari, N.; Rubistein, M.; Schlessinger, J.: Purification and characterization
of a 90 kDa protein released from human tumors and tumor cell lines. FEBS
Lett. 319: 59-65, 1993.
6. Koths, K.; Taylor, E.; Halenbeck, R.; Casipit, C.; Wang, A.: 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. J. Biol. Chem. 268: 14245-14249, 1993.
7. Nonaka, M.; Ma, B. Y.; Imaeda, H.; Kawabe, K.; Kawasaki, N.; Hodohara,
K.; Kawasaki, N.; Andoh, A.; Fujiyama, Y.; Kawasaki, T.: Dendritic
cell-specific intercellular adhesion molecule 3-grabbing non-integrin
(DC-SIGN) recognizes a novel ligand, Mac-2-binding protein, characteristically
expressed on human colorectal carcinomas. J. Biol. Chem. 286: 22403-22413,
2011.
8. Ullrich, A.; Sures, I.; D'Egidio, M.; Jallal, B.; Powell, T. J.;
Herbst, R.; Dreps, A.; Azam, M.; Rubinstein, M.; Natoli, C.; Shawver,
L. K.; Schlessinger, J.; Iacobelli, S.: The secreted tumor-associated
antigen 90K is a potent immune stimulator. J. Biol. Chem. 269: 18401-18407,
1994.
*FIELD* CN
Patricia A. Hartz - updated: 10/21/2011
Patti M. Sherman - updated: 1/29/1998
*FIELD* CD
Victor A. McKusick: 6/27/1995
*FIELD* ED
mgross: 10/31/2011
terry: 10/21/2011
dholmes: 1/29/1998
mark: 6/27/1995