LEG1_HUMAN
ID LEG1_HUMAN Reviewed; 135 AA.
AC P09382; B2R5E8; Q9UDK5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Galectin-1;
DE Short=Gal-1;
DE AltName: Full=14 kDa laminin-binding protein;
DE Short=HLBP14;
DE AltName: Full=14 kDa lectin;
DE AltName: Full=Beta-galactoside-binding lectin L-14-I;
DE AltName: Full=Galaptin;
DE AltName: Full=HBL;
DE AltName: Full=HPL;
DE AltName: Full=Lactose-binding lectin 1;
DE AltName: Full=Lectin galactoside-binding soluble 1;
DE AltName: Full=Putative MAPK-activating protein PM12;
DE AltName: Full=S-Lac lectin 1;
GN Name=LGALS1 {ECO:0000312|HGNC:HGNC:6561};
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].
RC TISSUE=Lung;
RX PubMed=2719964; DOI=10.1016/0167-4781(89)90173-5;
RA Hirabayashi J., Ayaki K., Soma G., Kasai K.;
RT "Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa
RT beta-galactoside-binding lectin.";
RL Biochim. Biophys. Acta 1008:85-91(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta, and Promyelocytic leukemia;
RX PubMed=2910856; DOI=10.1016/s0021-9258(19)85087-1;
RA Couraud P.-O., Casentini-Borocz D., Bringman T.S., Griffith J.,
RA McGrogan M., Nedwin G.E.;
RT "Molecular cloning, characterization, and expression of a human 14-kDa
RT lectin.";
RL J. Biol. Chem. 264:1310-1316(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hepatoma;
RX PubMed=2719646; DOI=10.1042/bj2590291;
RA Abbott W.M., Feizi T.;
RT "Evidence that the 14 kDa soluble beta-galactoside-binding lectin in man is
RT encoded by a single gene.";
RL Biochem. J. 259:291-294(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=18824694; DOI=10.1073/pnas.0807606105;
RA Than N.G., Romero R., Erez O., Weckle A., Tarca A.L., Hotra J., Abbas A.,
RA Han Y.M., Kim S.S., Kusanovic J.P., Gotsch F., Hou Z., Santolaya-Forgas J.,
RA Benirschke K., Papp Z., Grossman L.I., Goodman M., Wildman D.E.;
RT "Emergence of hormonal and redox regulation of galectin-1 in placental
RT mammals: implication in maternal-fetal immune tolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15819-15824(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=1988031; DOI=10.1021/bi00215a013;
RA Gitt M.A., Barondes S.H.;
RT "Genomic sequence and organization of two members of a human lectin gene
RT family.";
RL Biochemistry 30:82-89(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
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 Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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].
RC TISSUE=Placenta, and 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 PROTEIN SEQUENCE OF 2-135.
RC TISSUE=Placenta;
RX PubMed=3065332; DOI=10.1093/oxfordjournals.jbchem.a122401;
RA Hirabayashi J., Kasai K.;
RT "Complete amino acid sequence of a beta-galactoside-binding lectin from
RT human placenta.";
RL J. Biochem. 104:1-4(1988).
RN [14]
RP PROTEIN SEQUENCE OF 2-135.
RC TISSUE=Brain;
RA Bladier D., le Caer J.-P., Joubert R., Caron M., Rossier J.;
RT "Beta-galactosidase soluble lectin from human brain: complete amino acid
RT sequence.";
RL Neurochem. Int. 18:275-281(1991).
RN [15]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [16]
RP PROTEIN SEQUENCE OF 38-49; 101-108 AND 113-128, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP PROTEIN SEQUENCE OF 70-87 AND 122-133.
RC TISSUE=Placenta;
RX PubMed=3611046; DOI=10.1093/oxfordjournals.jbchem.a121968;
RA Hirabayashi J., Kawasaki H., Suzuki K., Kasai K.;
RT "Further characterization and structural studies on human placenta
RT lectin.";
RL J. Biochem. 101:987-995(1987).
RN [18]
RP PROTEIN SEQUENCE OF 20-29; 50-74 AND 132-135, AND INTERACTION WITH LAMININ.
RC TISSUE=Melanoma;
RX PubMed=1386213; DOI=10.1016/0003-9861(92)90650-l;
RA Castronovo V., Luyten F., van den Brule F., Sobel M.E.;
RT "Identification of a 14-kDa laminin binding protein (HLBP14) in human
RT melanoma cells that is identical to the 14-kDa galactoside binding
RT lectin.";
RL Arch. Biochem. Biophys. 297:132-138(1992).
RN [19]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=2383549; DOI=10.1021/bi00474a014;
RA Sharma A., Chemelli R., Allen H.J.;
RT "Human splenic galaptin: physicochemical characterization.";
RL Biochemistry 29:5309-5314(1990).
RN [20]
RP CHARACTERIZATION.
RX PubMed=7501023; DOI=10.1038/378736a0;
RA Perillo N.L., Pace K.E., Seilhamer J.J., Baum L.G.;
RT "Apoptosis of T cells mediated by galectin-1.";
RL Nature 378:736-739(1995).
RN [21]
RP CHARACTERIZATION.
RC TISSUE=Placenta;
RX PubMed=10369126; DOI=10.1016/s0165-2478(99)00012-7;
RA Walzel H., Schulz U., Neels P., Brock J.;
RT "Galectin-1, a natural ligand for the receptor-type protein tyrosine
RT phosphatase CD45.";
RL Immunol. Lett. 67:193-202(1999).
RN [22]
RP CHARACTERIZATION.
RX PubMed=10764829; DOI=10.1093/glycob/10.4.413;
RA Fouillit M., Joubert-Caron R., Poirier F., Bourin P., Monostori E.,
RA Levi-Strauss M., Raphael M., Bladier D., Caron M.;
RT "Regulation of CD45-induced signaling by galectin-1 in Burkitt lymphoma B
RT cells.";
RL Glycobiology 10:413-419(2000).
RN [23]
RP INTERACTION WITH LGALS3BP.
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., Liu F.-T.;
RT "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-
RT 1-induced cell aggregation.";
RL Int. J. Cancer 91:167-172(2001).
RN [24]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14617626; DOI=10.1074/jbc.m311183200;
RA He J., Baum L.G.;
RT "Presentation of galectin-1 by extracellular matrix triggers T cell
RT death.";
RL J. Biol. Chem. 279:4705-4712(2004).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RA Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O.,
RA Stansalas J., Mohamed A.O.;
RT "Abnormal proteins in primary breast cancer tissues from 25 Sudanese
RT patients.";
RL Eur. J. Inflamm. 6:115-121(2008).
RN [26]
RP FUNCTION, AND 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 [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [28]
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 [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP INTERACTION WITH SUSD2.
RX PubMed=23131994; DOI=10.1158/1541-7786.mcr-12-0501-t;
RA Watson A.P., Evans R.L., Egland K.A.;
RT "Multiple functions of sushi domain containing 2 (SUSD2) in breast
RT tumorigenesis.";
RL Mol. Cancer Res. 11:74-85(2013).
RN [33]
RP INTERACTION WITH CD6 AND ALCAM, AND FUNCTION.
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 [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP PHOSPHORYLATION AT SER-30.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [37]
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 [38]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, AND
RP SUBUNIT.
RX PubMed=15476813; DOI=10.1016/j.jmb.2004.08.078;
RA Lopez-Lucendo M.F., Solis D., Andre S., Hirabayashi J., Kasai K.,
RA Kaltner H., Gabius H.-J., Romero A.;
RT "Growth-regulatory human galectin-1: crystallographic characterisation of
RT the structural changes induced by single-site mutations and their impact on
RT the thermodynamics of ligand binding.";
RL J. Mol. Biol. 343:957-970(2004).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-135 IN COMPLEX WITH LACTOSE,
RP INTERACTION WITH CD2; CD3; CD7; CD43 AND CD45, SUBUNIT, AND FUNCTION.
RX PubMed=18796645; DOI=10.1093/glycob/cwn089;
RA Nishi N., Abe A., Iwaki J., Yoshida H., Itoh A., Shoji H., Kamitori S.,
RA Hirabayashi J., Nakamura T.;
RT "Functional and structural bases of a cysteine-less mutant as a long-
RT lasting substitute for galectin-1.";
RL Glycobiology 18:1065-1073(2008).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=19128029; DOI=10.1021/bi801855g;
RA Di Lella S., Ma L., Ricci J.C., Rabinovich G.A., Asher S.A.,
RA Alvarez R.M.S.;
RT "Critical role of the solvent environment in galectin-1 binding to the
RT disaccharide lactose.";
RL Biochemistry 48:786-791(2009).
CC -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC complex carbohydrates. Plays a role in regulating apoptosis, cell
CC proliferation and cell differentiation. Inhibits CD45 protein
CC phosphatase activity and therefore the dephosphorylation of Lyn kinase.
CC Strong inducer of T-cell apoptosis. {ECO:0000269|PubMed:14617626,
CC ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:19497882,
CC ECO:0000269|PubMed:24945728}.
CC -!- SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6,
CC CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-
CC acetyllactosamine). Interacts with SUSD2. 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:0000269|PubMed:11146440,
CC ECO:0000269|PubMed:1386213, ECO:0000269|PubMed:15476813,
CC ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:23131994,
CC ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:32272059}.
CC -!- INTERACTION:
CC P09382; Q13740: ALCAM; NbExp=3; IntAct=EBI-1048875, EBI-1188108;
CC P09382; P02649: APOE; NbExp=3; IntAct=EBI-1048875, EBI-1222467;
CC P09382; P27797: CALR; NbExp=3; IntAct=EBI-1048875, EBI-1049597;
CC P09382; P30203: CD6; NbExp=2; IntAct=EBI-1048875, EBI-2873748;
CC P09382; P36957: DLST; NbExp=3; IntAct=EBI-1048875, EBI-351007;
CC P09382; P35968: KDR; NbExp=3; IntAct=EBI-1048875, EBI-1005487;
CC P09382; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-1048875, EBI-1055945;
CC P09382; P16284: PECAM1; NbExp=4; IntAct=EBI-1048875, EBI-716404;
CC P09382; P08575: PTPRC; NbExp=2; IntAct=EBI-1048875, EBI-1341;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:14617626}. Cytoplasm
CC {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:32272059}.
CC Note=Can be secreted; the secretion is dependent on protein unfolding
CC and 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
CC secretion. {ECO:0000269|PubMed:32272059}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta, maternal decidua and fetal
CC membranes. Within placenta, expressed in trophoblasts, stromal cells,
CC villous endothelium, syncytiotrophoblast apical membrane and villous
CC stroma. Within fetal membranes, expressed in amnion, chorioamniotic
CC mesenchyma and chorion (at protein level). Expressed in cardiac,
CC smooth, and skeletal muscle, neurons, thymus, kidney and hematopoietic
CC cells. {ECO:0000269|PubMed:18824694, ECO:0000269|PubMed:19497882}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00116";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X14829; CAA32938.1; -; mRNA.
DR EMBL; J04456; AAA36170.1; -; mRNA.
DR EMBL; X15256; CAA33328.1; -; mRNA.
DR EMBL; EU363770; ACA58297.1; -; mRNA.
DR EMBL; M57678; AAB00777.1; -; Genomic_DNA.
DR EMBL; AB097036; BAC77389.1; -; mRNA.
DR EMBL; CR456511; CAG30397.1; -; mRNA.
DR EMBL; AK312161; BAG35095.1; -; mRNA.
DR EMBL; BT006775; AAP35421.1; -; mRNA.
DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60178.1; -; Genomic_DNA.
DR EMBL; BC001693; AAH01693.1; -; mRNA.
DR EMBL; BC020675; AAH20675.1; -; mRNA.
DR CCDS; CCDS13954.1; -.
DR PIR; A37134; LNHUGB.
DR RefSeq; NP_002296.1; NM_002305.3.
DR PDB; 1GZW; X-ray; 1.70 A; A/B=2-135.
DR PDB; 1W6M; X-ray; 2.30 A; A/B=2-135.
DR PDB; 1W6N; X-ray; 1.65 A; A/B=2-135.
DR PDB; 1W6O; X-ray; 1.90 A; A/B=2-135.
DR PDB; 1W6P; X-ray; 1.80 A; A/B=2-135.
DR PDB; 1W6Q; X-ray; 2.10 A; A/B=2-135.
DR PDB; 2KM2; NMR; -; A/B=2-135.
DR PDB; 2ZKN; X-ray; 1.86 A; A/B=2-135.
DR PDB; 3OY8; X-ray; 2.19 A; A/B=2-135.
DR PDB; 3OYW; X-ray; 2.50 A; A/B=2-135.
DR PDB; 3T2T; X-ray; 1.90 A; A/B=1-135.
DR PDB; 3W58; X-ray; 1.58 A; A/B/C/D=2-135.
DR PDB; 3W59; X-ray; 2.10 A; A/B/C/D=2-135.
DR PDB; 4Q1P; X-ray; 1.46 A; A/B=1-135.
DR PDB; 4Q1R; X-ray; 1.47 A; A/B=1-135.
DR PDB; 4Q26; X-ray; 1.40 A; A/B/G/H=1-135.
DR PDB; 4Q27; X-ray; 1.20 A; A/B=1-135.
DR PDB; 4Q2F; X-ray; 1.40 A; A/B=1-135.
DR PDB; 4XBL; X-ray; 1.93 A; A/B=1-135.
DR PDB; 4Y1U; X-ray; 1.76 A; A/B=3-135.
DR PDB; 4Y1V; X-ray; 2.32 A; A/B=3-135.
DR PDB; 4Y1X; X-ray; 2.45 A; A/B=3-135.
DR PDB; 4Y1Y; X-ray; 1.86 A; A/B=4-135.
DR PDB; 4Y1Z; X-ray; 2.23 A; A/B=3-135.
DR PDB; 4Y20; X-ray; 2.20 A; A/B=3-135.
DR PDB; 4Y22; X-ray; 2.50 A; A/B=3-135.
DR PDB; 4Y24; X-ray; 2.32 A; A/B=3-135.
DR PDB; 5MWT; X-ray; 1.71 A; A/B=3-135.
DR PDB; 5MWX; X-ray; 1.29 A; A/B=3-135.
DR PDB; 6B94; X-ray; 1.80 A; A/B=2-135.
DR PDB; 6F83; X-ray; 2.20 A; A/B=2-135.
DR PDB; 6M5Y; X-ray; 1.38 A; A=1-135.
DR PDB; 7LTA; X-ray; 1.53 A; A/B=3-135.
DR PDB; 7NML; X-ray; 1.43 A; A/B=3-135.
DR PDBsum; 1GZW; -.
DR PDBsum; 1W6M; -.
DR PDBsum; 1W6N; -.
DR PDBsum; 1W6O; -.
DR PDBsum; 1W6P; -.
DR PDBsum; 1W6Q; -.
DR PDBsum; 2KM2; -.
DR PDBsum; 2ZKN; -.
DR PDBsum; 3OY8; -.
DR PDBsum; 3OYW; -.
DR PDBsum; 3T2T; -.
DR PDBsum; 3W58; -.
DR PDBsum; 3W59; -.
DR PDBsum; 4Q1P; -.
DR PDBsum; 4Q1R; -.
DR PDBsum; 4Q26; -.
DR PDBsum; 4Q27; -.
DR PDBsum; 4Q2F; -.
DR PDBsum; 4XBL; -.
DR PDBsum; 4Y1U; -.
DR PDBsum; 4Y1V; -.
DR PDBsum; 4Y1X; -.
DR PDBsum; 4Y1Y; -.
DR PDBsum; 4Y1Z; -.
DR PDBsum; 4Y20; -.
DR PDBsum; 4Y22; -.
DR PDBsum; 4Y24; -.
DR PDBsum; 5MWT; -.
DR PDBsum; 5MWX; -.
DR PDBsum; 6B94; -.
DR PDBsum; 6F83; -.
DR PDBsum; 6M5Y; -.
DR PDBsum; 7LTA; -.
DR PDBsum; 7NML; -.
DR AlphaFoldDB; P09382; -.
DR BMRB; P09382; -.
DR SMR; P09382; -.
DR BioGRID; 110147; 285.
DR ComplexPortal; CPX-92; Galectin-1 complex.
DR CORUM; P09382; -.
DR DIP; DIP-46153N; -.
DR IntAct; P09382; 63.
DR MINT; P09382; -.
DR STRING; 9606.ENSP00000215909; -.
DR BindingDB; P09382; -.
DR ChEMBL; CHEMBL4915; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB03345; Mercaptoethanol.
DR DrugBank; DB04396; Thiodigalactoside.
DR MoonDB; P09382; Curated.
DR UniLectin; P09382; -.
DR GlyGen; P09382; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P09382; -.
DR MetOSite; P09382; -.
DR PhosphoSitePlus; P09382; -.
DR SwissPalm; P09382; -.
DR BioMuta; LGALS1; -.
DR DMDM; 126155; -.
DR DOSAC-COBS-2DPAGE; P09382; -.
DR REPRODUCTION-2DPAGE; IPI00219219; -.
DR REPRODUCTION-2DPAGE; P09382; -.
DR SWISS-2DPAGE; P09382; -.
DR UCD-2DPAGE; P09382; -.
DR CPTAC; CPTAC-1436; -.
DR CPTAC; CPTAC-1437; -.
DR CPTAC; CPTAC-1438; -.
DR CPTAC; CPTAC-1439; -.
DR CPTAC; CPTAC-1440; -.
DR CPTAC; CPTAC-706; -.
DR EPD; P09382; -.
DR jPOST; P09382; -.
DR MassIVE; P09382; -.
DR MaxQB; P09382; -.
DR PaxDb; P09382; -.
DR PeptideAtlas; P09382; -.
DR PRIDE; P09382; -.
DR ProteomicsDB; 52215; -.
DR TopDownProteomics; P09382; -.
DR ABCD; P09382; 3 sequenced antibodies.
DR Antibodypedia; 269; 1008 antibodies from 46 providers.
DR CPTC; P09382; 1 antibody.
DR DNASU; 3956; -.
DR Ensembl; ENST00000215909.10; ENSP00000215909.5; ENSG00000100097.12.
DR GeneID; 3956; -.
DR KEGG; hsa:3956; -.
DR MANE-Select; ENST00000215909.10; ENSP00000215909.5; NM_002305.4; NP_002296.1.
DR UCSC; uc003atn.4; human.
DR CTD; 3956; -.
DR DisGeNET; 3956; -.
DR GeneCards; LGALS1; -.
DR HGNC; HGNC:6561; LGALS1.
DR HPA; ENSG00000100097; Low tissue specificity.
DR MIM; 150570; gene.
DR neXtProt; NX_P09382; -.
DR OpenTargets; ENSG00000100097; -.
DR PharmGKB; PA30337; -.
DR VEuPathDB; HostDB:ENSG00000100097; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155534; -.
DR HOGENOM; CLU_037794_5_0_1; -.
DR InParanoid; P09382; -.
DR OMA; KIKCMAF; -.
DR OrthoDB; 1429018at2759; -.
DR PhylomeDB; P09382; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; P09382; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P09382; -.
DR SIGNOR; P09382; -.
DR BioGRID-ORCS; 3956; 13 hits in 1084 CRISPR screens.
DR ChiTaRS; LGALS1; human.
DR EvolutionaryTrace; P09382; -.
DR GeneWiki; Galectin-1; -.
DR GeneWiki; LGALS1; -.
DR GenomeRNAi; 3956; -.
DR Pharos; P09382; Tchem.
DR PRO; PR:P09382; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P09382; protein.
DR Bgee; ENSG00000100097; Expressed in stromal cell of endometrium and 205 other tissues.
DR ExpressionAtlas; P09382; baseline and differential.
DR Genevisible; P09382; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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:BHF-UCL.
DR GO; GO:1990724; C:galectin complex; IPI:ComplexPortal.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ComplexPortal.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:ComplexPortal.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 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; Apoptosis; Cytoplasm; Direct protein sequencing;
KW Extracellular matrix; Lectin; Phosphoprotein; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:3065332, ECO:0000269|Ref.14,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..135
FT /note="Galectin-1"
FT /id="PRO_0000076917"
FT DOMAIN 4..135
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 45..49
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT BINDING 53
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT BINDING 62
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT BINDING 69..72
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 30
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 108
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 108
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4Y1U"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4Q27"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4Q27"
FT STRAND 116..133
FT /evidence="ECO:0007829|PDB:4Q27"
SQ SEQUENCE 135 AA; 14716 MW; 2FBB8D7A1FC0F1F9 CRC64;
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY
MAADGDFKIK CVAFD
