MOT12_RAT
ID MOT12_RAT Reviewed; 486 AA.
AC D4A734;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 81.
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|RGD:1311468};
GN Name=Slc16a12 {ECO:0000312|RGD:1311468};
GN Synonyms=Mct12 {ECO:0000303|PubMed:21778275};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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: Detected in kidney, choroid plexus, testis, lung,
CC stomach, large and small intestine, spleen, fat and parotid gland
CC (PubMed:21778275). In eye, expressed in cornea, ciliary epithelium,
CC lens epithelium and lens fiber (PubMed:21778275).
CC {ECO:0000269|PubMed:21778275}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout rats are born to expected
CC Mendelian ratios and no obvious ocular phenotype is observed.
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; AC098155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178566.1; NM_001191637.1.
DR RefSeq; XP_017444788.1; XM_017589299.1.
DR RefSeq; XP_017444789.1; XM_017589300.1.
DR RefSeq; XP_017444790.1; XM_017589301.1.
DR RefSeq; XP_017444791.1; XM_017589302.1.
DR RefSeq; XP_017444792.1; XM_017589303.1.
DR AlphaFoldDB; D4A734; -.
DR SMR; D4A734; -.
DR STRING; 10116.ENSRNOP00000038838; -.
DR PaxDb; D4A734; -.
DR PeptideAtlas; D4A734; -.
DR Ensembl; ENSRNOT00000030024; ENSRNOP00000038838; ENSRNOG00000021916.
DR GeneID; 309525; -.
DR KEGG; rno:309525; -.
DR UCSC; RGD:1311468; rat.
DR CTD; 387700; -.
DR RGD; 1311468; Slc16a12.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000156169; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; D4A734; -.
DR OMA; WVLASHQ; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; D4A734; -.
DR TreeFam; TF313792; -.
DR PRO; PR:D4A734; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021916; Expressed in adult mammalian kidney and 17 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005308; F:creatine transmembrane transporter activity; ISO:RGD.
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; ISO:RGD.
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; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript 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_0000445618"
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 REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 52840 MW; CDF569B40E60B82D CRC64;
MTKITRVGSA SPPDGGWGWM IVAGCFLVTI CTRAVTRCIS IFFVEFQTYF AQDYSQTAWI
HSIVDCMTML CAPLGSVVSN QLSCQAGIML GGLLASTGLI LGSFATSLKH LYLSLGVLTG
LGFALCYSPA IAMVGKYFSR RKAFAYGIAM SGSGIGTFIL APVVQLLIEQ FSWRGALLIL
GGFVLNLCVC GALMRPITLK EDPSGPEKSH DRDAQREDCK QASPYSPLTK EWTETRLCCS
LQQGYGFLLM SDFVVLAVSV LFMAYGCSPL FVYLVPYALS VGVSHHQAAF LMSILGVIDI
VGNITFGWLT DRRCLKNYRY VCYLFAVALD GLCYLCLPML QSFPLLVPFS CTFGYFDGAY
VTLIPVVTAE IVGTTSLSSA LGVVYFLHAV PYLVSPPIAG WLVDTTGSYT AAFLLCGFAM
IFSSILLGFA KIAKRMKRTQ VPFLVKDSDP KLHLWTNGSV AYSIAKELDQ KDEESLAKAR
TGCNLT
