LG3BP_MOUSE
ID LG3BP_MOUSE Reviewed; 577 AA.
AC Q07797; O35649; Q3U631; Q3U8K4; Q3UDL5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Galectin-3-binding protein;
DE AltName: Full=Cyp-C-associated protein;
DE Short=CyCAP;
DE AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE AltName: Full=Protein MAMA;
DE Flags: Precursor;
GN Name=Lgals3bp; Synonyms=Cycap, Mama;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP PPIC, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX PubMed=8341703; DOI=10.1073/pnas.90.14.6815;
RA Friedman J.S., Trahey M., Weissman I.L.;
RT "Cloning and characterization of cyclophilin C-associated protein: a
RT candidate natural cellular ligand for cyclophilin C.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6815-6819(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Bone marrow macrophage;
RX PubMed=8119883; DOI=10.1016/s0021-9258(17)37490-2;
RA Chicheportiche Y., Vassalli P.;
RT "Cloning and expression of a mouse macrophage cDNA coding for a membrane
RT glycoprotein of the scavenger receptor cysteine-rich domain family.";
RL J. Biol. Chem. 269:5512-5517(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Aorta, Bone marrow, Thymus, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host
CC defense against viruses and tumor cells (By similarity).
CC {ECO:0000250|UniProtKB:Q08380}.
CC -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-like
CC structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds
CC ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By similarity). Interacts
CC with PPIC (in vitro). The unglycosylated form interacts with PDE4DIP
CC isoform 2/MMG8/SMYLE; this interaction may connect a pericentrosomal
CC complex to the gamma-tubulin ring complex (gamma-TuRC) to promote
CC microtubule assembly and acetylation (By similarity).
CC {ECO:0000250|UniProtKB:Q08380, ECO:0000269|PubMed:8341703}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:8119883}.
CC -!- TISSUE SPECIFICITY: Detected in embryo, liver, spleen, kidney, lung,
CC heart, intestine, thymus and lymph node. {ECO:0000269|PubMed:8119883,
CC ECO:0000269|PubMed:8341703}.
CC -!- INDUCTION: Up-regulated by TNF and IFNG. {ECO:0000269|PubMed:8119883}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8341703}.
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DR EMBL; L16894; AAA37499.1; -; mRNA.
DR EMBL; X67809; CAA48010.1; -; mRNA.
DR EMBL; AK079915; BAC37782.1; -; mRNA.
DR EMBL; AK137836; BAE23505.1; -; mRNA.
DR EMBL; AK150021; BAE29246.1; -; mRNA.
DR EMBL; AK152182; BAE31013.1; -; mRNA.
DR EMBL; AK153313; BAE31894.1; -; mRNA.
DR EMBL; AK153396; BAE31958.1; -; mRNA.
DR EMBL; AK155031; BAE33003.1; -; mRNA.
DR EMBL; AL591404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34661.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34662.1; -; Genomic_DNA.
DR EMBL; BC090658; AAH90658.1; -; mRNA.
DR CCDS; CCDS25701.1; -.
DR PIR; A53202; A53202.
DR RefSeq; NP_035280.1; NM_011150.2.
DR AlphaFoldDB; Q07797; -.
DR SMR; Q07797; -.
DR BioGRID; 202330; 63.
DR IntAct; Q07797; 51.
DR STRING; 10090.ENSMUSP00000035579; -.
DR GlyConnect; 2319; 2 N-Linked glycans (1 site).
DR GlyGen; Q07797; 6 sites, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q07797; -.
DR CPTAC; non-CPTAC-3924; -.
DR EPD; Q07797; -.
DR jPOST; Q07797; -.
DR MaxQB; Q07797; -.
DR PaxDb; Q07797; -.
DR PeptideAtlas; Q07797; -.
DR PRIDE; Q07797; -.
DR ProteomicsDB; 252467; -.
DR Antibodypedia; 604; 429 antibodies from 35 providers.
DR DNASU; 19039; -.
DR Ensembl; ENSMUST00000043722; ENSMUSP00000035579; ENSMUSG00000033880.
DR GeneID; 19039; -.
DR KEGG; mmu:19039; -.
DR UCSC; uc007moz.1; mouse.
DR CTD; 3959; -.
DR MGI; MGI:99554; Lgals3bp.
DR VEuPathDB; HostDB:ENSMUSG00000033880; -.
DR eggNOG; ENOG502QU48; Eukaryota.
DR GeneTree; ENSGT00940000162516; -.
DR HOGENOM; CLU_032646_0_0_1; -.
DR InParanoid; Q07797; -.
DR OMA; FPMMLPQ; -.
DR OrthoDB; 1174057at2759; -.
DR PhylomeDB; Q07797; -.
DR TreeFam; TF331368; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 19039; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Lgals3bp; mouse.
DR PRO; PR:Q07797; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q07797; protein.
DR Bgee; ENSMUSG00000033880; Expressed in small intestine Peyer's patch and 185 other tissues.
DR ExpressionAtlas; Q07797; baseline and differential.
DR Genevisible; Q07797; MM.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; ISS:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF54695; SSF54695; 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 Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..577
FT /note="Galectin-3-binding protein"
FT /id="PRO_0000357035"
FT DOMAIN 24..124
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 153..221
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 260..360
FT /note="BACK"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 62..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 93..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 25
FT /note="R -> G (in Ref. 1; AAA37499)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="H -> P (in Ref. 1; AAA37499)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> C (in Ref. 3; BAE29246)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Q -> K (in Ref. 3; BAE31894)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="D -> E (in Ref. 3; BAE31013)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="KQ -> NE (in Ref. 1; AAA37499)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..577
FT /note="STDMV -> LH (in Ref. 1; AAA37499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64491 MW; 9D4181A7BEC2BD7C CRC64;
MALLWLLSVF LLVPGTQGTE DGDMRLVNGA SANEGRVEIF YRGRWGTVCD NLWNLLDAHV
VCRALGYENA TQALGRAAFG PGKGPIMLDE VECTGTESSL ASCRSLGWMV SRCGHEKDAG
VVCSNDTTGL HILDLSGELS DALGQIFDSQ QGCDLFIQVT GQGYEDLSLC AHTLILRTNP
EAQALWQVVG SSVIMRVDAE CMPVVRDFLR YFYSRRIEVS MSSVKCLHKL ASAYGATELQ
DYCGRLFATL LPQDPTFHTP LDLYAYARAT GDSMLEDLCV QFLAWNFEPL TQSESWSAVP
TTLIQALLPK SELAVSSELD LLKAVDQWST ETIASHEDIE RLVEQVRFPM MLPQELFELQ
FNLSLYQDHQ ALFQRKTMQA LEFHTVPVEV LAKYKGLNLT EDTYKPRLYT SSTWSSLVMA
STWRAQRYEY NRYNQLYTYG YGSVARYNSY QSFQTPQHPS FLFKDKQISW SATYLPTMQS
CWNYGFSCTS NELPVLGLTT SSYSNPTIGY ENRVLILCGG YSVVDVTSFE GSKAPIPTAL
DTNSSKTPSL FPCASGAFSS FRVVIRPFYL TNSTDMV
