LEGL_HUMAN
ID LEGL_HUMAN Reviewed; 172 AA.
AC Q3ZCW2; B2RBG8; D6W5E8; Q6P5T6; Q9P005;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Galectin-related protein;
DE AltName: Full=Galectin-like protein;
DE AltName: Full=Lectin galactoside-binding-like protein;
GN Name=LGALSL; Synonyms=GRP; ORFNames=HSPC159;
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 [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP CRYSTALLIZATION.
RX PubMed=16682780; DOI=10.1107/s1744309106012875;
RA Zhou D., Sun J., Zhao W., Zhang X., Shi Y., Teng M., Niu L., Dong Y.,
RA Liu P.;
RT "Expression, purification, crystallization and preliminary X-ray
RT characterization of the GRP carbohydrate-recognition domain from Homo
RT sapiens.";
RL Acta Crystallogr. F 62:474-476(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP IDENTIFICATION BY 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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 35-172, FUNCTION, AND SUBUNIT.
RX PubMed=18320588; DOI=10.1002/prot.22003;
RA Zhou D., Ge H., Sun J., Gao Y., Teng M., Niu L.;
RT "Crystal structure of the C-terminal conserved domain of human GRP, a
RT galectin-related protein, reveals a function mode different from those of
RT galectins.";
RL Proteins 71:1582-1588(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-171, FUNCTION, AND SUBUNIT.
RX PubMed=18433051; DOI=10.1002/prot.22078;
RA Waelti M.A., Thore S., Aebi M., Kuenzler M.;
RT "Crystal structure of the putative carbohydrate recognition domain of human
RT galectin-related protein.";
RL Proteins 72:804-808(2008).
CC -!- FUNCTION: Does not bind lactose, and may not bind carbohydrates.
CC {ECO:0000269|PubMed:18320588, ECO:0000269|PubMed:18433051}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:18320588,
CC ECO:0000305|PubMed:18433051}.
CC -!- INTERACTION:
CC Q3ZCW2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10241423, EBI-742054;
CC Q3ZCW2; P50458: LHX2; NbExp=3; IntAct=EBI-10241423, EBI-12179869;
CC Q3ZCW2; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-10241423, EBI-742610;
CC Q3ZCW2; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-10241423, EBI-717399;
CC -!- CAUTION: Most of the residues in the galectin domain that have been
CC shown to be critical for carbohydrate-binding in other galectins are
CC not conserved. {ECO:0000305}.
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DR EMBL; AF161508; AAF29123.1; -; mRNA.
DR EMBL; AK314656; BAG37215.1; -; mRNA.
DR EMBL; CH471053; EAW99942.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99943.1; -; Genomic_DNA.
DR EMBL; BC036082; AAH36082.1; -; mRNA.
DR EMBL; BC062691; AAH62691.1; -; mRNA.
DR CCDS; CCDS1877.1; -.
DR RefSeq; NP_054900.2; NM_014181.2.
DR PDB; 2JJ6; X-ray; 2.00 A; A/B=38-171.
DR PDB; 3B9C; X-ray; 1.90 A; A/B/C/D=38-172.
DR PDBsum; 2JJ6; -.
DR PDBsum; 3B9C; -.
DR AlphaFoldDB; Q3ZCW2; -.
DR SMR; Q3ZCW2; -.
DR BioGRID; 118863; 32.
DR IntAct; Q3ZCW2; 7.
DR STRING; 9606.ENSP00000238875; -.
DR GlyGen; Q3ZCW2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q3ZCW2; -.
DR PhosphoSitePlus; Q3ZCW2; -.
DR BioMuta; LGALSL; -.
DR DMDM; 166223243; -.
DR REPRODUCTION-2DPAGE; IPI00023549; -.
DR EPD; Q3ZCW2; -.
DR jPOST; Q3ZCW2; -.
DR MassIVE; Q3ZCW2; -.
DR MaxQB; Q3ZCW2; -.
DR PaxDb; Q3ZCW2; -.
DR PeptideAtlas; Q3ZCW2; -.
DR PRIDE; Q3ZCW2; -.
DR ProteomicsDB; 61919; -.
DR Antibodypedia; 30823; 108 antibodies from 17 providers.
DR DNASU; 29094; -.
DR Ensembl; ENST00000238875.10; ENSP00000238875.4; ENSG00000119862.13.
DR GeneID; 29094; -.
DR KEGG; hsa:29094; -.
DR MANE-Select; ENST00000238875.10; ENSP00000238875.4; NM_014181.3; NP_054900.2.
DR UCSC; uc002scy.5; human.
DR CTD; 29094; -.
DR DisGeNET; 29094; -.
DR GeneCards; LGALSL; -.
DR HGNC; HGNC:25012; LGALSL.
DR HPA; ENSG00000119862; Tissue enhanced (retina, skin).
DR MIM; 617902; gene.
DR neXtProt; NX_Q3ZCW2; -.
DR OpenTargets; ENSG00000119862; -.
DR VEuPathDB; HostDB:ENSG00000119862; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155337; -.
DR HOGENOM; CLU_037794_2_1_1; -.
DR InParanoid; Q3ZCW2; -.
DR OMA; CISGEKG; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; Q3ZCW2; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; Q3ZCW2; -.
DR SignaLink; Q3ZCW2; -.
DR BioGRID-ORCS; 29094; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; LGALSL; human.
DR EvolutionaryTrace; Q3ZCW2; -.
DR GeneWiki; HSPC159; -.
DR GenomeRNAi; 29094; -.
DR Pharos; Q3ZCW2; Tbio.
DR PRO; PR:Q3ZCW2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q3ZCW2; protein.
DR Bgee; ENSG00000119862; Expressed in upper leg skin and 183 other tissues.
DR ExpressionAtlas; Q3ZCW2; baseline and differential.
DR Genevisible; Q3ZCW2; HS.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030651; Galectin-rel.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF98; PTHR11346:SF98; 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; Lectin; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..172
FT /note="Galectin-related protein"
FT /id="PRO_0000315766"
FT DOMAIN 39..168
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT 132
FT /note="H -> Y (in Ref. 1; AAF29123)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="R -> G (in Ref. 4; AAH36082)"
FT /evidence="ECO:0000305"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:3B9C"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3B9C"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3B9C"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3B9C"
FT STRAND 159..172
FT /evidence="ECO:0007829|PDB:3B9C"
SQ SEQUENCE 172 AA; 18986 MW; E2D41EA68EF44DEC CRC64;
MAGSVADSDA VVKLDDGHLN NSLSSPVQAD VYFPRLIVPF CGHIKGGMRP GKKVLVMGIV
DLNPESFAIS LTCGDSEDPP ADVAIELKAV FTDRQLLRNS CISGERGEEQ SAIPYFPFIP
DQPFRVEILC EHPRFRVFVD GHQLFDFYHR IQTLSAIDTI KINGDLQITK LG
