MOT12_MOUSE
ID MOT12_MOUSE Reviewed; 486 AA.
AC Q8BGC3; Q14CF9; Q14DR7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Monocarboxylate transporter 12 {ECO:0000305};
DE Short=MCT 12 {ECO:0000305};
DE AltName: Full=Solute carrier family 16 member 12 {ECO:0000312|MGI:MGI:2147716};
GN Name=Slc16a12 {ECO:0000312|MGI:MGI:2147716};
GN Synonyms=Mct12 {ECO:0000303|PubMed:21778275};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21778275; DOI=10.1167/iovs.10-6579;
RA Castorino J.J., Gallagher-Colombo S.M., Levin A.V., Fitzgerald P.G.,
RA Polishook J., Kloeckener-Gruissem B., Ostertag E., Philp N.J.;
RT "Juvenile cataract-associated mutation of solute carrier SLC16A12 impairs
RT trafficking of the protein to the plasma membrane.";
RL Invest. Ophthalmol. Vis. Sci. 52:6774-6784(2011).
CC -!- FUNCTION: Proton-linked monocarboxylate transporter that mediates
CC creatine transport across the plasma membrane.
CC {ECO:0000250|UniProtKB:Q6ZSM3}.
CC -!- SUBUNIT: Interacts with isoform 2 of BSG.
CC {ECO:0000250|UniProtKB:Q6ZSM3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZSM3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in eye lens.
CC {ECO:0000269|PubMed:21778275}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lens at P1 and P7 (PubMed:21778275).
CC The expression levels are higher than in adult lens (PubMed:21778275).
CC Detected in the basolateral membrane of the lens epithelium, with
CC strong staining at equatorial epithelium, and in differentiating
CC secondary fiber cells at P1 (at protein level) (PubMed:21778275).
CC {ECO:0000269|PubMed:21778275}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; AK028284; BAC25857.1; -; mRNA.
DR EMBL; AK029076; BAC26279.1; -; mRNA.
DR EMBL; BC111902; AAI11903.1; -; mRNA.
DR EMBL; BC113803; AAI13804.1; -; mRNA.
DR CCDS; CCDS29767.1; -.
DR RefSeq; NP_766426.1; NM_172838.3.
DR RefSeq; XP_006527141.1; XM_006527078.3.
DR RefSeq; XP_011245548.1; XM_011247246.2.
DR AlphaFoldDB; Q8BGC3; -.
DR SMR; Q8BGC3; -.
DR STRING; 10090.ENSMUSP00000009522; -.
DR iPTMnet; Q8BGC3; -.
DR PhosphoSitePlus; Q8BGC3; -.
DR PaxDb; Q8BGC3; -.
DR PeptideAtlas; Q8BGC3; -.
DR PRIDE; Q8BGC3; -.
DR ProteomicsDB; 252595; -.
DR Antibodypedia; 16234; 119 antibodies from 24 providers.
DR DNASU; 240638; -.
DR Ensembl; ENSMUST00000009522; ENSMUSP00000009522; ENSMUSG00000009378.
DR GeneID; 240638; -.
DR KEGG; mmu:240638; -.
DR UCSC; uc008hgu.1; mouse.
DR CTD; 387700; -.
DR MGI; MGI:2147716; Slc16a12.
DR VEuPathDB; HostDB:ENSMUSG00000009378; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000156169; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; Q8BGC3; -.
DR OMA; WVLASHQ; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; Q8BGC3; -.
DR TreeFam; TF313792; -.
DR BioGRID-ORCS; 240638; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc16a12; mouse.
DR PRO; PR:Q8BGC3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BGC3; protein.
DR Bgee; ENSMUSG00000009378; Expressed in urinary bladder urothelium and 178 other tissues.
DR Genevisible; Q8BGC3; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005308; F:creatine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015881; P:creatine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..486
FT /note="Monocarboxylate transporter 12"
FT /id="PRO_0000286676"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 234
FT /note="E -> K (in Ref. 2; AAI13804/AAI11903)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> C (in Ref. 2; AAI13804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53152 MW; AA3CC9951FB28247 CRC64;
MTKITRVSLA SPPDGGWGWM IVAGCFLVTI CTRAVTRCIS IFFVEFQTYF AQDYSQTAWI
HSIVDCMTML CAPLGSVVSN QLSCQAGIML GGLLASTGFI LGSFATSLKH LYLSLGVLTG
LGFALCYSPA IAMVGKYFSR RKALAYGIAM SGSGIGTFIL APVVQLLIEQ FSWRGALLIL
GGFVLNLCVC GALMRPITLK EDRSVPEKNH NRESQREDCK QASPYSPLTK ECTETRLCCS
LQQEYGFLLM SDFVVLAVSV LFMAYGCSPL FVYLVPYALS VGVSHHQAAF LMSILGVIDI
VGNITFGWLT DRRCLKNYRY VCYLFAVALD GLCYLCLPML QTFPLLVPFS CTFGYFDGAY
VTLIPVVTAE IVGTTSLSSA LGVVYFLHAV PYLVSPPIAG WLVDTTGSYT AAFLLCGFAM
IFSSILLGFV RIVKRMKRTQ VPFPVKDSDP KLQLWTNGSV AYSVARELDQ KDEEPLPKAR
SGCNLT
