LEG3_HUMAN
ID LEG3_HUMAN Reviewed; 250 AA.
AC P17931; B2RC38; Q16005; Q6IBA7; Q96J47;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 5.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Galectin-3;
DE Short=Gal-3;
DE AltName: Full=35 kDa lectin;
DE AltName: Full=Carbohydrate-binding protein 35;
DE Short=CBP 35;
DE AltName: Full=Galactose-specific lectin 3;
DE AltName: Full=Galactoside-binding protein;
DE Short=GALBP;
DE AltName: Full=IgE-binding protein;
DE AltName: Full=L-31;
DE AltName: Full=Laminin-binding protein;
DE AltName: Full=Lectin L-29;
DE AltName: Full=Mac-2 antigen;
GN Name=LGALS3 {ECO:0000312|HGNC:HGNC:6563}; Synonyms=MAC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-64 AND PRO-98.
RX PubMed=2261464; DOI=10.1021/bi00487a015;
RA Robertson M.W., Albrandt K., Keller D., Liu F.-T.;
RT "Human IgE-binding protein: a soluble lectin exhibiting a highly conserved
RT interspecies sequence and differential recognition of IgE glycoforms.";
RL Biochemistry 29:8093-8100(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-98.
RC TISSUE=Carcinoma;
RX PubMed=2402511; DOI=10.1073/pnas.87.18.7324;
RA Cherayil B., Chaitovitz S., Wong C., Pillai S.;
RT "Molecular cloning of a human macrophage lectin specific for galactose.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7324-7328(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-64 AND PRO-98.
RX PubMed=2022338; DOI=10.1016/0378-1119(91)90139-3;
RA Oda Y., Leffler H., Sakakura Y., Kasai K., Barondes S.H.;
RT "Human breast carcinoma cDNA encoding a galactoside-binding lectin
RT homologous to mouse Mac-2 antigen.";
RL Gene 99:279-283(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2009535;
RA Raz A., Carmi P., Raz T., Hogan V., Mohamed A., Wolman S.R.;
RT "Molecular cloning and chromosomal mapping of a human galactoside-binding
RT protein.";
RL Cancer Res. 51:2173-2178(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=7682704; DOI=10.1073/pnas.90.8.3466;
RA Lotz M.M., Andrews C.W. Jr., Korzelius C.A., Lee E.C., Steele G.D. Jr.,
RA Clarke A., Mercurio A.M.;
RT "Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss
RT of its nuclear localization are associated with the neoplastic progression
RT of colon carcinoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3466-3470(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9439577; DOI=10.1006/abbi.1997.0447;
RA Kadrofske M.M., Openo K.P., Wang J.L.;
RT "The human LGALS3 (galectin-3) gene: determination of the gene structure
RT and functional characterization of the promoter.";
RL Arch. Biochem. Biophys. 349:7-20(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gastric adenocarcinoma;
RA Kato S.;
RT "Human galectin-3 full-length cDNA.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-64 AND PRO-98.
RC TISSUE=Skin;
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 [13]
RP PHOSPHORYLATION AT SER-6 AND SER-12.
RX PubMed=8253806; DOI=10.1016/s0021-9258(19)74371-3;
RA Huflejt M.E., Turck C.W., Lindstedt R., Barondes S.H., Leffler H.;
RT "L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and
RT serine 12 in vivo and by casein kinase I.";
RL J. Biol. Chem. 268:26712-26718(1993).
RN [14]
RP INTERACTION WITH LGALS3BP.
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).
RN [15]
RP INTERACTION WITH ITGB1; ITGA3 AND CSPG4, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [16]
RP FUNCTION IN INFLAMMATION.
RX PubMed=19594635; DOI=10.1111/j.1600-065x.2009.00794.x;
RA Henderson N.C., Sethi T.;
RT "The regulation of inflammation by galectin-3.";
RL Immunol. Rev. 230:160-171(2009).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=19497882; DOI=10.1073/pnas.0903568106;
RA Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y.,
RA Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J., Kim J.S.,
RA Haidarian S., Uddin M., Bohn H., Benirschke K., Santolaya-Forgas J.,
RA Grossman L.I., Erez O., Hassan S.S., Zavodszky P., Papp Z., Wildman D.E.;
RT "A primate subfamily of galectins expressed at the maternal-fetal interface
RT that promote immune cell death.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009).
RN [18]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19616076; DOI=10.1016/j.bbagen.2009.07.005;
RA Haudek K.C., Spronk K.J., Voss P.G., Patterson R.J., Wang J.L.,
RA Arnoys E.J.;
RT "Dynamics of galectin-3 in the nucleus and cytoplasm.";
RL Biochim. Biophys. Acta 1800:181-189(2010).
RN [19]
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., Buerckstuemmer T.,
RA 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH CD6 AND ALCAM.
RX PubMed=24945728; DOI=10.1016/j.febslet.2014.05.064;
RA Escoda-Ferran C., Carrasco E., Caballero-Banos M., Miro-Julia C.,
RA Martinez-Florensa M., Consuegra-Fernandez M., Martinez V.G., Liu F.T.,
RA Lozano F.;
RT "Modulation of CD6 function through interaction with galectin-1 and -3.";
RL FEBS Lett. 588:2805-2813(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP FUNCTION, AND INTERACTION WITH TRIM16.
RX PubMed=27693506; DOI=10.1016/j.devcel.2016.08.003;
RA Chauhan S., Kumar S., Jain A., Ponpuak M., Mudd M.H., Kimura T., Choi S.W.,
RA Peters R., Mandell M., Bruun J.A., Johansen T., Deretic V.;
RT "TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct
RT Autophagy in Endomembrane Damage Homeostasis.";
RL Dev. Cell 39:13-27(2016).
RN [24]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 114-250.
RX PubMed=9582341; DOI=10.1074/jbc.273.21.13047;
RA Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S.H.,
RA Rini J.M.;
RT "X-ray crystal structure of the human galectin-3 carbohydrate recognition
RT domain at 2.1-A resolution.";
RL J. Biol. Chem. 273:13047-13052(1998).
CC -!- FUNCTION: Galactose-specific lectin which binds IgE. May mediate with
CC the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial
CC cells migration. Together with DMBT1, required for terminal
CC differentiation of columnar epithelial cells during early embryogenesis
CC (By similarity). In the nucleus: acts as a pre-mRNA splicing factor.
CC Involved in acute inflammatory responses including neutrophil
CC activation and adhesion, chemoattraction of monocytes macrophages,
CC opsonization of apoptotic neutrophils, and activation of mast cells.
CC Together with TRIM16, coordinates the recognition of membrane damage
CC with mobilization of the core autophagy regulators ATG16L1 and BECN1 in
CC response to damaged endomembranes. {ECO:0000250,
CC ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:19594635,
CC ECO:0000269|PubMed:19616076, ECO:0000269|PubMed:27693506}.
CC -!- SUBUNIT: Probably forms homo- or heterodimers. Interacts with DMBT1 (By
CC similarity). Interacts with CD6 and ALCAM (PubMed:24945728). Forms a
CC complex with the ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP,
CC LYPD3, CYHR1 and UACA. Interacts with TRIM16; this interaction mediates
CC autophagy of damage endomembranes. Interacts with cargo receptor
CC TMED10; the interaction mediates the translocation from the cytoplasm
CC into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment)
CC and thereby secretion (PubMed:32272059). {ECO:0000250|UniProtKB:P08699,
CC ECO:0000250|UniProtKB:P16110, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:27693506,
CC ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:9501082}.
CC -!- INTERACTION:
CC P17931; Q13740: ALCAM; NbExp=3; IntAct=EBI-1170392, EBI-1188108;
CC P17931; P30203: CD6; NbExp=2; IntAct=EBI-1170392, EBI-2873748;
CC P17931; P36222: CHI3L1; NbExp=2; IntAct=EBI-1170392, EBI-6917454;
CC P17931; O43186: CRX; NbExp=3; IntAct=EBI-1170392, EBI-748171;
CC P17931; P17813: ENG; NbExp=5; IntAct=EBI-1170392, EBI-2834630;
CC P17931; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1170392, EBI-618309;
CC P17931; Q14627: IL13RA2; NbExp=2; IntAct=EBI-1170392, EBI-4320063;
CC P17931; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1170392, EBI-6509505;
CC P17931; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-1170392, EBI-10988217;
CC P17931; Q29983: MICA; NbExp=2; IntAct=EBI-1170392, EBI-1031130;
CC P17931; P09237: MMP7; NbExp=5; IntAct=EBI-1170392, EBI-6595344;
CC P17931; O14931: NCR3; NbExp=2; IntAct=EBI-1170392, EBI-14989262;
CC P17931; O14931-2: NCR3; NbExp=3; IntAct=EBI-1170392, EBI-15098724;
CC P17931; Q8WUM4: PDCD6IP; NbExp=2; IntAct=EBI-1170392, EBI-310624;
CC P17931; Q13427: PPIG; NbExp=3; IntAct=EBI-1170392, EBI-396072;
CC P17931; Q9NZ81: PRR13; NbExp=4; IntAct=EBI-1170392, EBI-740924;
CC P17931; O75177: SS18L1; NbExp=3; IntAct=EBI-1170392, EBI-744674;
CC P17931; P12763: AHSG; Xeno; NbExp=2; IntAct=EBI-1170392, EBI-9396660;
CC P17931; Q9WU78-1: Pdcd6ip; Xeno; NbExp=2; IntAct=EBI-1170392, EBI-15788421;
CC P17931; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-1170392, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32272059}. Nucleus.
CC Secreted {ECO:0000269|PubMed:32272059}. Note=Secreted by a non-
CC classical secretory pathway and associates with the cell surface. Can
CC be secreted; the secretion is dependent on protein unfolding and
CC facilitated by the cargo receptor TMED10; it results in protein
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) followed by vesicle entry and secretion
CC (PubMed:32272059). {ECO:0000269|PubMed:32272059}.
CC -!- TISSUE SPECIFICITY: A major expression is found in the colonic
CC epithelium. It is also abundant in the activated macrophages. Expressed
CC in fetal membranes. {ECO:0000269|PubMed:19497882}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00118";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LGALS3ID44396ch14q22.html";
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DR EMBL; M57710; AAA35607.1; -; mRNA.
DR EMBL; M35368; AAA88086.1; -; mRNA.
DR EMBL; M36682; AAA36163.1; -; mRNA.
DR EMBL; M64303; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S59012; AAB26229.1; -; mRNA.
DR EMBL; AF031425; AAB86584.1; -; Genomic_DNA.
DR EMBL; AF031422; AAB86584.1; JOINED; Genomic_DNA.
DR EMBL; AF031423; AAB86584.1; JOINED; Genomic_DNA.
DR EMBL; AF031424; AAB86584.1; JOINED; Genomic_DNA.
DR EMBL; AB006780; BAA22164.1; -; mRNA.
DR EMBL; AK314929; BAG37435.1; -; mRNA.
DR EMBL; CR456897; CAG33178.1; -; mRNA.
DR EMBL; AL139316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80658.1; -; Genomic_DNA.
DR EMBL; BC001120; AAH01120.1; -; mRNA.
DR EMBL; BC053667; AAH53667.1; -; mRNA.
DR CCDS; CCDS41956.1; -.
DR PIR; A35820; A35820.
DR RefSeq; NP_002297.2; NM_002306.3.
DR PDB; 1A3K; X-ray; 2.10 A; A=114-250.
DR PDB; 1KJL; X-ray; 1.40 A; A=105-250.
DR PDB; 1KJR; X-ray; 1.55 A; A=105-250.
DR PDB; 2NMN; X-ray; 2.45 A; A=113-250.
DR PDB; 2NMO; X-ray; 1.35 A; A=113-250.
DR PDB; 2NN8; X-ray; 1.35 A; A=113-250.
DR PDB; 2XG3; X-ray; 1.20 A; A=114-250.
DR PDB; 3AYA; X-ray; 2.00 A; A/B=117-250.
DR PDB; 3AYC; X-ray; 1.80 A; A/B=117-250.
DR PDB; 3AYD; X-ray; 1.90 A; A=117-250.
DR PDB; 3AYE; X-ray; 2.00 A; A/B=117-250.
DR PDB; 3T1L; X-ray; 1.60 A; A=108-250.
DR PDB; 3T1M; X-ray; 1.55 A; A=108-250.
DR PDB; 3ZSJ; X-ray; 0.86 A; A=113-250.
DR PDB; 3ZSK; X-ray; 0.90 A; A=114-250.
DR PDB; 3ZSL; X-ray; 1.08 A; A=114-250.
DR PDB; 3ZSM; X-ray; 1.25 A; A=114-250.
DR PDB; 4BLI; X-ray; 1.08 A; A=114-250.
DR PDB; 4BLJ; X-ray; 1.20 A; A=114-250.
DR PDB; 4BM8; X-ray; 0.96 A; A=114-250.
DR PDB; 4JC1; X-ray; 1.50 A; A=108-250.
DR PDB; 4JCK; X-ray; 1.15 A; A=108-250.
DR PDB; 4LBJ; X-ray; 1.80 A; A=114-250.
DR PDB; 4LBK; X-ray; 1.60 A; A=114-250.
DR PDB; 4LBL; X-ray; 1.58 A; A=114-250.
DR PDB; 4LBM; X-ray; 1.55 A; A=112-250.
DR PDB; 4LBN; X-ray; 1.70 A; A=112-250.
DR PDB; 4LBO; X-ray; 1.65 A; A=113-250.
DR PDB; 4R9A; X-ray; 1.20 A; A=111-250.
DR PDB; 4R9B; X-ray; 1.20 A; A=111-250.
DR PDB; 4R9C; X-ray; 1.19 A; A=111-250.
DR PDB; 4R9D; X-ray; 1.24 A; A=111-250.
DR PDB; 4RL7; X-ray; 2.00 A; A=111-250.
DR PDB; 4XBN; X-ray; 2.21 A; A=113-250.
DR PDB; 5E88; X-ray; 1.60 A; A=114-250.
DR PDB; 5E89; X-ray; 1.50 A; A=114-250.
DR PDB; 5E8A; X-ray; 1.50 A; A=114-250.
DR PDB; 5EXO; X-ray; 1.50 A; A=112-250.
DR PDB; 5H9P; X-ray; 2.04 A; A=113-250.
DR PDB; 5H9R; X-ray; 1.58 A; A=113-250.
DR PDB; 5IUQ; X-ray; 1.12 A; A=113-250.
DR PDB; 5NF7; X-ray; 1.59 A; A=106-250.
DR PDB; 5NF9; X-ray; 1.87 A; A=106-250.
DR PDB; 5NFA; X-ray; 1.59 A; A=106-250.
DR PDB; 5NFB; X-ray; 1.59 A; A=106-250.
DR PDB; 5NFC; X-ray; 1.59 A; A=106-250.
DR PDB; 5OAX; X-ray; 1.20 A; A=114-250.
DR PDB; 5ODY; X-ray; 1.15 A; A=113-250.
DR PDB; 6B8K; X-ray; 1.28 A; A=112-250.
DR PDB; 6EOG; X-ray; 1.20 A; A=114-250.
DR PDB; 6EOL; X-ray; 1.50 A; A=114-250.
DR PDB; 6EXY; Other; 1.10 A; A=113-250.
DR PDB; 6EYM; Other; 1.70 A; A=113-250.
DR PDB; 6F2Q; Other; 1.03 A; A=113-250.
DR PDB; 6F6Y; X-ray; 1.41 A; A=114-250.
DR PDB; 6FK2; X-ray; 1.01 A; A=113-250.
DR PDB; 6FOF; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-250.
DR PDB; 6G0V; X-ray; 1.09 A; A=114-250.
DR PDB; 6H64; X-ray; 1.80 A; A/B/C/D/E/F=96-250.
DR PDB; 6I74; X-ray; 0.96 A; A=113-250.
DR PDB; 6I75; X-ray; 1.17 A; A=113-250.
DR PDB; 6I76; X-ray; 1.20 A; A=113-250.
DR PDB; 6I77; X-ray; 1.22 A; A=113-250.
DR PDB; 6I78; X-ray; 1.15 A; A=113-250.
DR PDB; 6KXA; X-ray; 1.23 A; A=113-250.
DR PDB; 6KXB; X-ray; 1.50 A; A=113-250.
DR PDB; 6Q0Q; X-ray; 1.99 A; A=112-250.
DR PDB; 6Q17; X-ray; 1.98 A; A=112-250.
DR PDB; 6QGE; X-ray; 1.16 A; A=113-250.
DR PDB; 6QGF; X-ray; 1.34 A; A=113-250.
DR PDB; 6QLN; X-ray; 1.00 A; A=113-250.
DR PDB; 6QLO; X-ray; 1.18 A; A=113-250.
DR PDB; 6QLP; X-ray; 1.08 A; A=113-250.
DR PDB; 6QLQ; X-ray; 1.08 A; B=113-250.
DR PDB; 6QLR; X-ray; 0.97 A; A=113-250.
DR PDB; 6QLS; X-ray; 1.05 A; A=113-250.
DR PDB; 6QLT; X-ray; 1.15 A; A=113-250.
DR PDB; 6QLU; X-ray; 1.10 A; A=113-250.
DR PDB; 6RHL; X-ray; 1.30 A; A=113-250.
DR PDB; 6RHM; X-ray; 1.60 A; A=113-250.
DR PDB; 6RZF; X-ray; 1.02 A; A=113-250.
DR PDB; 6RZG; X-ray; 1.01 A; A=113-250.
DR PDB; 6RZH; X-ray; 0.95 A; A=113-250.
DR PDB; 6RZI; X-ray; 1.09 A; A=113-250.
DR PDB; 6RZJ; X-ray; 1.10 A; A=113-250.
DR PDB; 6RZK; X-ray; 1.05 A; A=113-250.
DR PDB; 6RZL; X-ray; 1.04 A; A=113-250.
DR PDB; 6RZM; X-ray; 1.34 A; A=113-250.
DR PDB; 6TF6; X-ray; 1.50 A; A=114-250.
DR PDB; 6TF7; X-ray; 1.40 A; A=114-250.
DR PDB; 6Y4C; X-ray; 1.70 A; A=113-250.
DR PDB; 6Y78; X-ray; 1.70 A; A=113-250.
DR PDB; 6ZVF; X-ray; 1.90 A; P=57-65.
DR PDB; 7BE3; X-ray; 1.25 A; A=114-250.
DR PDB; 7CXA; X-ray; 1.97 A; A/B=108-250.
DR PDB; 7DF5; X-ray; 1.08 A; A=108-250.
DR PDBsum; 1A3K; -.
DR PDBsum; 1KJL; -.
DR PDBsum; 1KJR; -.
DR PDBsum; 2NMN; -.
DR PDBsum; 2NMO; -.
DR PDBsum; 2NN8; -.
DR PDBsum; 2XG3; -.
DR PDBsum; 3AYA; -.
DR PDBsum; 3AYC; -.
DR PDBsum; 3AYD; -.
DR PDBsum; 3AYE; -.
DR PDBsum; 3T1L; -.
DR PDBsum; 3T1M; -.
DR PDBsum; 3ZSJ; -.
DR PDBsum; 3ZSK; -.
DR PDBsum; 3ZSL; -.
DR PDBsum; 3ZSM; -.
DR PDBsum; 4BLI; -.
DR PDBsum; 4BLJ; -.
DR PDBsum; 4BM8; -.
DR PDBsum; 4JC1; -.
DR PDBsum; 4JCK; -.
DR PDBsum; 4LBJ; -.
DR PDBsum; 4LBK; -.
DR PDBsum; 4LBL; -.
DR PDBsum; 4LBM; -.
DR PDBsum; 4LBN; -.
DR PDBsum; 4LBO; -.
DR PDBsum; 4R9A; -.
DR PDBsum; 4R9B; -.
DR PDBsum; 4R9C; -.
DR PDBsum; 4R9D; -.
DR PDBsum; 4RL7; -.
DR PDBsum; 4XBN; -.
DR PDBsum; 5E88; -.
DR PDBsum; 5E89; -.
DR PDBsum; 5E8A; -.
DR PDBsum; 5EXO; -.
DR PDBsum; 5H9P; -.
DR PDBsum; 5H9R; -.
DR PDBsum; 5IUQ; -.
DR PDBsum; 5NF7; -.
DR PDBsum; 5NF9; -.
DR PDBsum; 5NFA; -.
DR PDBsum; 5NFB; -.
DR PDBsum; 5NFC; -.
DR PDBsum; 5OAX; -.
DR PDBsum; 5ODY; -.
DR PDBsum; 6B8K; -.
DR PDBsum; 6EOG; -.
DR PDBsum; 6EOL; -.
DR PDBsum; 6EXY; -.
DR PDBsum; 6EYM; -.
DR PDBsum; 6F2Q; -.
DR PDBsum; 6F6Y; -.
DR PDBsum; 6FK2; -.
DR PDBsum; 6FOF; -.
DR PDBsum; 6G0V; -.
DR PDBsum; 6H64; -.
DR PDBsum; 6I74; -.
DR PDBsum; 6I75; -.
DR PDBsum; 6I76; -.
DR PDBsum; 6I77; -.
DR PDBsum; 6I78; -.
DR PDBsum; 6KXA; -.
DR PDBsum; 6KXB; -.
DR PDBsum; 6Q0Q; -.
DR PDBsum; 6Q17; -.
DR PDBsum; 6QGE; -.
DR PDBsum; 6QGF; -.
DR PDBsum; 6QLN; -.
DR PDBsum; 6QLO; -.
DR PDBsum; 6QLP; -.
DR PDBsum; 6QLQ; -.
DR PDBsum; 6QLR; -.
DR PDBsum; 6QLS; -.
DR PDBsum; 6QLT; -.
DR PDBsum; 6QLU; -.
DR PDBsum; 6RHL; -.
DR PDBsum; 6RHM; -.
DR PDBsum; 6RZF; -.
DR PDBsum; 6RZG; -.
DR PDBsum; 6RZH; -.
DR PDBsum; 6RZI; -.
DR PDBsum; 6RZJ; -.
DR PDBsum; 6RZK; -.
DR PDBsum; 6RZL; -.
DR PDBsum; 6RZM; -.
DR PDBsum; 6TF6; -.
DR PDBsum; 6TF7; -.
DR PDBsum; 6Y4C; -.
DR PDBsum; 6Y78; -.
DR PDBsum; 6ZVF; -.
DR PDBsum; 7BE3; -.
DR PDBsum; 7CXA; -.
DR PDBsum; 7DF5; -.
DR AlphaFoldDB; P17931; -.
DR BMRB; P17931; -.
DR SMR; P17931; -.
DR BioGRID; 110149; 315.
DR CORUM; P17931; -.
DR DIP; DIP-45623N; -.
DR IntAct; P17931; 162.
DR MINT; P17931; -.
DR STRING; 9606.ENSP00000254301; -.
DR BindingDB; P17931; -.
DR ChEMBL; CHEMBL4531; -.
DR DrugBank; DB01827; 2,3,5,6-Tetrafluoro-4-Methoxy-Benzamide.
DR DrugBank; DB04465; Lactose.
DR DrugCentral; P17931; -.
DR MoonDB; P17931; Curated.
DR UniLectin; P17931; -.
DR GlyGen; P17931; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P17931; -.
DR PhosphoSitePlus; P17931; -.
DR BioMuta; LGALS3; -.
DR DMDM; 215274262; -.
DR DOSAC-COBS-2DPAGE; P17931; -.
DR REPRODUCTION-2DPAGE; IPI00465431; -.
DR UCD-2DPAGE; P17931; -.
DR EPD; P17931; -.
DR jPOST; P17931; -.
DR MassIVE; P17931; -.
DR MaxQB; P17931; -.
DR PaxDb; P17931; -.
DR PeptideAtlas; P17931; -.
DR PRIDE; P17931; -.
DR ProteomicsDB; 53526; -.
DR ABCD; P17931; 1 sequenced antibody.
DR Antibodypedia; 161; 1774 antibodies from 49 providers.
DR DNASU; 3958; -.
DR Ensembl; ENST00000254301.14; ENSP00000254301.9; ENSG00000131981.16.
DR GeneID; 3958; -.
DR KEGG; hsa:3958; -.
DR MANE-Select; ENST00000254301.14; ENSP00000254301.9; NM_002306.4; NP_002297.2.
DR UCSC; uc001xbr.4; human.
DR CTD; 3958; -.
DR DisGeNET; 3958; -.
DR GeneCards; LGALS3; -.
DR HGNC; HGNC:6563; LGALS3.
DR HPA; ENSG00000131981; Tissue enhanced (intestine).
DR MIM; 153619; gene.
DR neXtProt; NX_P17931; -.
DR OpenTargets; ENSG00000131981; -.
DR PharmGKB; PA30340; -.
DR VEuPathDB; HostDB:ENSG00000131981; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000157224; -.
DR HOGENOM; CLU_072823_0_0_1; -.
DR InParanoid; P17931; -.
DR OMA; CIGGDIA; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; P17931; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; P17931; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8941333; RUNX2 regulates genes involved in differentiation of myeloid cells.
DR SignaLink; P17931; -.
DR SIGNOR; P17931; -.
DR BioGRID-ORCS; 3958; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; LGALS3; human.
DR EvolutionaryTrace; P17931; -.
DR GeneWiki; LGALS3; -.
DR GenomeRNAi; 3958; -.
DR Pharos; P17931; Tchem.
DR PRO; PR:P17931; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P17931; protein.
DR Bgee; ENSG00000131981; Expressed in colonic mucosa and 207 other tissues.
DR ExpressionAtlas; P17931; baseline and differential.
DR Genevisible; P17931; HS.
DR GO; GO:0009986; C:cell surface; ISS:ARUK-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
DR GO; GO:0019863; F:IgE binding; IDA:BHF-UCL.
DR GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IC:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:BHF-UCL.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
DR GO; GO:0071674; P:mononuclear cell migration; IDA:BHF-UCL.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:2000521; P:negative regulation of immunological synapse formation; ISS:BHF-UCL.
DR GO; GO:1903614; P:negative regulation of protein tyrosine phosphatase activity; IC:ARUK-UCL.
DR GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISS:BHF-UCL.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:BHF-UCL.
DR GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:BHF-UCL.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; IDA:BHF-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:ARUK-UCL.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:BHF-UCL.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd00070; GLECT; 1.
DR DisProt; DP01332; -.
DR IDEAL; IID00029; -.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR015534; Galectin_3.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF26; PTHR11346:SF26; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Differentiation; Disulfide bond;
KW IgE-binding protein; Immunity; Innate immunity; Lectin; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT CHAIN 2..250
FT /note="Galectin-3"
FT /id="PRO_0000076930"
FT REPEAT 36..44
FT /note="1"
FT REPEAT 45..53
FT /note="2"
FT REPEAT 54..62
FT /note="3"
FT REPEAT 63..69
FT /note="4; approximate"
FT REPEAT 70..78
FT /note="5"
FT REPEAT 79..88
FT /note="6; approximate"
FT REPEAT 89..100
FT /note="7; approximate"
FT REPEAT 101..109
FT /note="8; approximate"
FT DOMAIN 118..248
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..109
FT /note="8 X 9 AA tandem repeats of Y-P-G-X(3)-P-G-A"
FT MOTIF 226..241
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..187
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8253806"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8253806"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 173
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 64
FT /note="P -> H (in dbSNP:rs4644)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2022338, ECO:0000269|PubMed:2261464"
FT /id="VAR_012988"
FT VARIANT 98
FT /note="T -> P (in dbSNP:rs4652)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2022338, ECO:0000269|PubMed:2261464,
FT ECO:0000269|PubMed:2402511"
FT /id="VAR_012989"
FT VARIANT 183
FT /note="R -> K (in dbSNP:rs10148371)"
FT /id="VAR_049768"
FT CONFLICT 33..52
FT /note="AGGYPGASYPGAYPGQAPPG -> QGLPRGFLSWGLPRAGTPR (in Ref.
FT 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="S -> R (in Ref. 4; M64303)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6FOF"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6FOF"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6ZVF"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3ZSJ"
FT STRAND 233..249
FT /evidence="ECO:0007829|PDB:3ZSJ"
SQ SEQUENCE 250 AA; 26152 MW; C49DDF6D67AE0C88 CRC64;
MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP
GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL
PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN
WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI
DLTSASYTMI
