MOT3_RAT
ID MOT3_RAT Reviewed; 490 AA.
AC O70461; G3V7K8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Monocarboxylate transporter 3;
DE Short=MCT 3;
DE AltName: Full=Solute carrier family 16 member 8;
GN Name=Slc16a8; Synonyms=Mct3;
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RX PubMed=9841555; DOI=10.1152/ajpregu.1998.274.6.r1824;
RA Philp N.J., Yoon H., Grollman E.F.;
RT "Monocarboxylate transporter MCT1 is located in the apical membrane and
RT MCT3 in the basal membrane of rat RPE.";
RL Am. J. Physiol. 274:R1824-R1828(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable retinal pigment epithelium (RPE)-specific proton-
CC coupled L-lactate transporter (By similarity). May facilitate transport
CC of lactate and H(+) out of the retina and could therefore play a role
CC in pH and ion homeostasis of the outer retina (By similarity).
CC {ECO:0000250|UniProtKB:O35308, ECO:0000250|UniProtKB:Q90632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651;
CC Evidence={ECO:0000250|UniProtKB:Q90632};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:9841555}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Basolateral sorting signals (BLSS) in C-terminal
CC cytoplasmic tail ensure its basolateral expression (By similarity).
CC Colocalizes with BSG in basolateral cell membrane of the retinal
CC pigment epithelium (By similarity). {ECO:0000250|UniProtKB:O35308,
CC ECO:0000250|UniProtKB:O95907}.
CC -!- TISSUE SPECIFICITY: Retinal pigment epithelium.
CC {ECO:0000269|PubMed:9841555}.
CC -!- DOMAIN: The two basolateral sorting signal (BSS) are required to direct
CC SLC16A8 to the basolateral membrane. {ECO:0000250|UniProtKB:O95907}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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; AF059258; AAC18120.1; -; mRNA.
DR EMBL; AABR07073327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473950; EDM15812.1; -; Genomic_DNA.
DR RefSeq; NP_113932.2; NM_031744.2.
DR RefSeq; XP_017450592.1; XM_017595103.1.
DR AlphaFoldDB; O70461; -.
DR SMR; O70461; -.
DR STRING; 10116.ENSRNOP00000016248; -.
DR PhosphoSitePlus; O70461; -.
DR PaxDb; O70461; -.
DR Ensembl; ENSRNOT00000016247.4; ENSRNOP00000016248.1; ENSRNOG00000012090.4.
DR GeneID; 65200; -.
DR KEGG; rno:65200; -.
DR UCSC; RGD:69282; rat.
DR CTD; 23539; -.
DR RGD; 69282; Slc16a8.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000161934; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; O70461; -.
DR OMA; VYFKELM; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; O70461; -.
DR TreeFam; TF313792; -.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-RNO-70268; Pyruvate metabolism.
DR PRO; PR:O70461; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000012090; Expressed in ovary and 1 other tissue.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
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; IBA:GO_Central.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015355; F:secondary active monocarboxylate transmembrane transporter activity; TAS:RGD.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR030759; MCT3.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF26; PTHR11360:SF26; 2.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00892; 2A0113; 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..490
FT /note="Monocarboxylate transporter 3"
FT /id="PRO_0000211392"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 426..460
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250|UniProtKB:O95907"
FT REGION 461..480
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250|UniProtKB:O95907"
FT COMPBIAS 427..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 397
FT /note="V -> A (in Ref. 1; AAC18120)"
FT CONFLICT 411
FT /note="Q -> L (in Ref. 1; AAC18120)"
FT CONFLICT 416..421
FT /note="DIPPGP -> NISSGR (in Ref. 1; AAC18120)"
FT CONFLICT 427..430
FT /note="TSDT -> ASDP (in Ref. 1; AAC18120)"
FT CONFLICT 466
FT /note="E -> EQE (in Ref. 1; AAC18120)"
FT CONFLICT 474..480
FT /note="DLSHESV -> ELDHESI (in Ref. 1; AAC18120)"
FT CONFLICT 486..489
FT /note="HGQN -> RGQK (in Ref. 1; AAC18120)"
SQ SEQUENCE 490 AA; 51283 MW; 9604B3719121BE92 CRC64;
MGAGGPRRGA GPPDGGWGWV VLGACFVITG FAYGFPKAVS VFFRELKRDF GAGYSDTAWV
SSIMLAMLYG TGPLSSILVT RFGCRPVMLA GGLLASAGMI LASFASRLLE LYLTAGVLTG
LGLALNFQPS LIMLGLYFER RRPLANGLAA AGSPVFLSTL SPLGQLLGER FGWRGGFLLF
GGLLLHCCAC GAVMRPPPGP QPRPDPAPPG GRARHRQLLD LAVCTDRTFM VYMVTKFLMA
LGLFVPAILL VNYAKDAGVP DAEAAFLLSI VGFVDIVARP ACGALAGLGR LRPHVPYLFS
LALLANGLTD LISARARSYG TLVAFCIAFG LSYGMVGALQ FEVLMATVGA PRFPSALGLV
LLVEAVAVLI GPPSAGRLVD ALKNYEIIFY LAGSEVVLAG VFMAVTTYCC QRCSKDIPPG
PSAEGGTSDT EDVEAERDSE PMPASTEEPG SLEALEVLSP RAGSPEPEEE AVPDLSHESV
GGHEAHGQNA
