LEG12_HUMAN
ID LEG12_HUMAN Reviewed; 336 AA.
AC Q96DT0; B2R9N2; G5E970; Q96DS9; Q96PR9; Q9H258; Q9H259; Q9NZ02;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Galectin-12;
DE Short=Gal-12;
DE AltName: Full=Galectin-related inhibitor of proliferation;
GN Name=LGALS12; Synonyms=GRIP1;
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] (ISOFORMS A; B; C; D AND G), AND
RP CHARACTERIZATION.
RC TISSUE=Adipose tissue;
RX PubMed=11435439; DOI=10.1074/jbc.m105097200;
RA Hotta K., Funahashi T., Matsukawa Y., Takahashi M., Nishizawa H.,
RA Kishida K., Matsuda M., Kuriyama H., Kihara S., Nakamura T., Tochino Y.,
RA Bodkin N.L., Hansen B.C., Matsuzawa Y.;
RT "Galectin-12, an adipose-expressed galectin-like molecule possessing
RT apoptosis-inducing activity.";
RL J. Biol. Chem. 276:34089-34097(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; E AND F).
RC TISSUE=Retina;
RX PubMed=11283015; DOI=10.1074/jbc.m010914200;
RA Yang R.-Y., Hsu D.K., Yu L., Ni J., Liu F.-T.;
RT "Cell cycle regulation by galectin-12, a new member of the galectin
RT superfamily.";
RL J. Biol. Chem. 276:20252-20260(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Rectum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Blood;
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).
CC -!- FUNCTION: Binds lactose. May participate in the apoptosis of
CC adipocytes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=A;
CC IsoId=Q96DT0-1; Sequence=Displayed;
CC Name=B; Synonyms=GRIP1a;
CC IsoId=Q96DT0-2; Sequence=VSP_003100;
CC Name=C;
CC IsoId=Q96DT0-3; Sequence=VSP_003102;
CC Name=D;
CC IsoId=Q96DT0-4; Sequence=VSP_003100, VSP_003102;
CC Name=E; Synonyms=1;
CC IsoId=Q96DT0-5; Sequence=VSP_003099;
CC Name=F; Synonyms=2;
CC IsoId=Q96DT0-6; Sequence=VSP_003099, VSP_003101;
CC Name=G;
CC IsoId=Q96DT0-7; Sequence=VSP_003101;
CC -!- TISSUE SPECIFICITY: Not widely expressed. Predominantly expressed in
CC adipose tissue.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-12;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_278";
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DR EMBL; AF244974; AAK77328.1; -; mRNA.
DR EMBL; AF244975; AAK77329.1; -; mRNA.
DR EMBL; AF244976; AAK77330.1; -; mRNA.
DR EMBL; AF244977; AAK77331.1; -; mRNA.
DR EMBL; AF310686; AAG40863.1; -; mRNA.
DR EMBL; AF310687; AAG40864.1; -; mRNA.
DR EMBL; AK313851; BAG36579.1; -; mRNA.
DR EMBL; AF222695; AAF34677.1; -; mRNA.
DR EMBL; AP001591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74151.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW74152.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW74155.1; -; Genomic_DNA.
DR EMBL; BC028222; AAH28222.1; -; mRNA.
DR CCDS; CCDS44633.1; -. [Q96DT0-6]
DR CCDS; CCDS44634.1; -. [Q96DT0-2]
DR CCDS; CCDS44635.1; -. [Q96DT0-4]
DR CCDS; CCDS8045.1; -. [Q96DT0-5]
DR RefSeq; NP_001136007.1; NM_001142535.1. [Q96DT0-6]
DR RefSeq; NP_001136008.1; NM_001142536.1.
DR RefSeq; NP_001136009.1; NM_001142537.1. [Q96DT0-2]
DR RefSeq; NP_001136010.1; NM_001142538.1. [Q96DT0-4]
DR RefSeq; NP_149092.2; NM_033101.3. [Q96DT0-5]
DR AlphaFoldDB; Q96DT0; -.
DR SMR; Q96DT0; -.
DR BioGRID; 124475; 16.
DR IntAct; Q96DT0; 3.
DR STRING; 9606.ENSP00000339374; -.
DR iPTMnet; Q96DT0; -.
DR PhosphoSitePlus; Q96DT0; -.
DR BioMuta; LGALS12; -.
DR DMDM; 20138669; -.
DR EPD; Q96DT0; -.
DR MassIVE; Q96DT0; -.
DR PaxDb; Q96DT0; -.
DR PeptideAtlas; Q96DT0; -.
DR PRIDE; Q96DT0; -.
DR ProteomicsDB; 33850; -.
DR ProteomicsDB; 76313; -. [Q96DT0-1]
DR ProteomicsDB; 76314; -. [Q96DT0-2]
DR ProteomicsDB; 76315; -. [Q96DT0-3]
DR ProteomicsDB; 76316; -. [Q96DT0-4]
DR ProteomicsDB; 76317; -. [Q96DT0-5]
DR ProteomicsDB; 76318; -. [Q96DT0-6]
DR Antibodypedia; 28944; 122 antibodies from 15 providers.
DR DNASU; 85329; -.
DR Ensembl; ENST00000340246.10; ENSP00000339374.6; ENSG00000133317.16. [Q96DT0-6]
DR Ensembl; ENST00000394618.9; ENSP00000378116.4; ENSG00000133317.16. [Q96DT0-5]
DR Ensembl; ENST00000415491.6; ENSP00000394659.2; ENSG00000133317.16. [Q96DT0-2]
DR Ensembl; ENST00000425950.2; ENSP00000399093.2; ENSG00000133317.16. [Q96DT0-4]
DR Ensembl; ENST00000674247.1; ENSP00000501500.1; ENSG00000133317.16. [Q96DT0-7]
DR GeneID; 85329; -.
DR KEGG; hsa:85329; -.
DR MANE-Select; ENST00000394618.9; ENSP00000378116.4; NM_033101.4; NP_149092.3. [Q96DT0-5]
DR UCSC; uc001nxa.3; human. [Q96DT0-1]
DR CTD; 85329; -.
DR DisGeNET; 85329; -.
DR GeneCards; LGALS12; -.
DR HGNC; HGNC:15788; LGALS12.
DR HPA; ENSG00000133317; Tissue enhanced (adipose tissue, breast).
DR MIM; 606096; gene.
DR neXtProt; NX_Q96DT0; -.
DR OpenTargets; ENSG00000133317; -.
DR PharmGKB; PA30338; -.
DR VEuPathDB; HostDB:ENSG00000133317; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000161499; -.
DR HOGENOM; CLU_037794_1_0_1; -.
DR InParanoid; Q96DT0; -.
DR PhylomeDB; Q96DT0; -.
DR PathwayCommons; Q96DT0; -.
DR SignaLink; Q96DT0; -.
DR BioGRID-ORCS; 85329; 3 hits in 1075 CRISPR screens.
DR ChiTaRS; LGALS12; human.
DR GenomeRNAi; 85329; -.
DR Pharos; Q96DT0; Tbio.
DR PRO; PR:Q96DT0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96DT0; protein.
DR Bgee; ENSG00000133317; Expressed in adipose tissue and 86 other tissues.
DR ExpressionAtlas; Q96DT0; baseline and differential.
DR Genevisible; Q96DT0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0030395; F:lactose binding; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:1904977; P:lymphatic endothelial cell migration; IBA:GO_Central.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:InterPro.
DR GO; GO:0050994; P:regulation of lipid catabolic process; IEA:InterPro.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030649; Galectin_12.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF111; PTHR11346:SF111; 1.
DR Pfam; PF00337; Gal-bind_lectin; 2.
DR SMART; SM00908; Gal-bind_lectin; 2.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS51304; GALECTIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Lectin; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..336
FT /note="Galectin-12"
FT /id="PRO_0000076949"
FT DOMAIN 49..183
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 212..336
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform B and isoform D)"
FT /evidence="ECO:0000303|PubMed:11283015,
FT ECO:0000303|PubMed:11435439"
FT /id="VSP_003100"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform E and isoform F)"
FT /evidence="ECO:0000303|PubMed:11283015"
FT /id="VSP_003099"
FT VAR_SEQ 74
FT /note="H -> HS (in isoform F and isoform G)"
FT /evidence="ECO:0000303|PubMed:11283015,
FT ECO:0000303|PubMed:11435439"
FT /id="VSP_003101"
FT VAR_SEQ 200..208
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:11435439"
FT /id="VSP_003102"
SQ SEQUENCE 336 AA; 37542 MW; F35D0A0CE509E795 CRC64;
MSQPSGGRAP GTRIYSWSCP TVMSPGEKLD PIPDSFILQP PVFHPVVPYV TTIFGGLHAG
KMVMLQGVVP LDAHRFQVDF QCGCSLCPRP DIAFHFNPRF HTTKPHVICN TLHGGRWQRE
ARWPHLALRR GSSFLILFLF GNEEVKVSVN GQHFLHFRYR LPLSHVDTLG IFGDILVEAV
GFLNINPFVE GSREYPAGHP FLLMSPRLEV PCSHALPQGL SPGQVIIVRG LVLQEPKHFT
VSLRDQAAHA PVTLRASFAD RTLAWISRWG QKKLISAPFL FYPQRFFEVL LLFQEGGLKL
ALNGQGLGAT SMNQQALEQL RELRISGSVQ LYCVHS
