LEG12_MOUSE
ID LEG12_MOUSE Reviewed; 314 AA.
AC Q91VD1; Q3UW90; Q8CCA4; Q8K2L7; Q9JKX2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Galectin-12;
DE Short=Gal-12;
GN Name=Lgals12;
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] (ISOFORM 1), AND CHARACTERIZATION.
RC STRAIN=C57BL/KsK; 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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Colon;
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 MRNA] (ISOFORM 1).
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=2;
CC Name=1;
CC IsoId=Q91VD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VD1-2; Sequence=VSP_010321;
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_mou_Stlect_289";
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; AF244979; AAK77327.1; -; mRNA.
DR EMBL; AF244978; AAK77326.1; -; mRNA.
DR EMBL; AF223223; AAF34682.1; -; mRNA.
DR EMBL; AK033535; BAC28345.1; -; mRNA.
DR EMBL; AK136526; BAE23026.1; -; mRNA.
DR EMBL; BC030890; AAH30890.1; -; mRNA.
DR CCDS; CCDS29529.1; -. [Q91VD1-1]
DR CCDS; CCDS89332.1; -. [Q91VD1-2]
DR RefSeq; NP_062389.1; NM_019516.3. [Q91VD1-1]
DR RefSeq; XP_006527282.1; XM_006527219.3.
DR AlphaFoldDB; Q91VD1; -.
DR SMR; Q91VD1; -.
DR STRING; 10090.ENSMUSP00000097318; -.
DR PhosphoSitePlus; Q91VD1; -.
DR MaxQB; Q91VD1; -.
DR PaxDb; Q91VD1; -.
DR PRIDE; Q91VD1; -.
DR ProteomicsDB; 264730; -. [Q91VD1-1]
DR ProteomicsDB; 264731; -. [Q91VD1-2]
DR Antibodypedia; 28944; 122 antibodies from 15 providers.
DR DNASU; 56072; -.
DR Ensembl; ENSMUST00000079902; ENSMUSP00000078824; ENSMUSG00000024972. [Q91VD1-2]
DR Ensembl; ENSMUST00000099729; ENSMUSP00000097318; ENSMUSG00000024972. [Q91VD1-1]
DR Ensembl; ENSMUST00000159983; ENSMUSP00000124610; ENSMUSG00000024972. [Q91VD1-1]
DR GeneID; 56072; -.
DR KEGG; mmu:56072; -.
DR UCSC; uc008glk.1; mouse. [Q91VD1-1]
DR UCSC; uc012bhx.1; mouse. [Q91VD1-2]
DR CTD; 85329; -.
DR MGI; MGI:1929094; Lgals12.
DR VEuPathDB; HostDB:ENSMUSG00000024972; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000161499; -.
DR HOGENOM; CLU_037794_1_0_1; -.
DR InParanoid; Q91VD1; -.
DR OMA; EYPVGHP; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; Q91VD1; -.
DR BioGRID-ORCS; 56072; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q91VD1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91VD1; protein.
DR Bgee; ENSMUSG00000024972; Expressed in epididymal fat pad and 92 other tissues.
DR Genevisible; Q91VD1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO: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..314
FT /note="Galectin-12"
FT /id="PRO_0000076950"
FT DOMAIN 27..161
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 190..314
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT VAR_SEQ 167..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010321"
FT CONFLICT 228
FT /note="V -> A (in Ref. 1; AAK77327/AAK77326)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> K (in Ref. 4; AAH30890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35460 MW; 9C9D33A7583DD09D CRC64;
MSTDEHLDPI PDSFILQPPV FHPVIPYGTT IFGGLYAGKM VTLQGVVPLH ARRFQVDFQC
GCCLHPQPDV AFRFSPRFYT VKPHVICNTH QGGLWQKEIR WPGVALQRGD SFLILFLFEN
EEVKVSVNGQ HFLHYRYRLP LSRVDTLDIS GDILVKAVGF LNINPFVEGS REYPVGYPFL
LYSPRLEVPC SRALPRGLWP GQVIVVRGLV LKEPKDFTLS LKDGTTHVPV TLRASFTDRT
LAWVSSWGRK KLISAPFLFH PQRFFEVLLL CQEGGLKLAL NGQGLGATSL DQKALEQLRE
LRISGNVHLY CVHC
