ID MOT3_CHICK Reviewed; 542 AA. AC Q90632; A0A1D5NV56; O13151; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 03-AUG-2022, sequence version 3. DT 03-AUG-2022, entry version 130. DE RecName: Full=Monocarboxylate transporter 3; DE Short=MCT 3; DE AltName: Full=Retinal epithelial membrane protein {ECO:0000303|PubMed:7628551}; DE AltName: Full=Solute carrier family 16 member 8; GN Name=SLC16A8; GN Synonyms=MCT3 {ECO:0000303|PubMed:9168967}, GN REMP {ECO:0000303|PubMed:7628551}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC TISSUE=Retinal pigment epithelium; RX PubMed=7628551; DOI=10.1006/excr.1995.1205; RA Philp N.J., Chu P., Pan T.C., Zhang R.Z., Chu M.L., Stark K., Boettiger D., RA Yoon H., Kieber-Emmons T.; RT "Developmental expression and molecular cloning of REMP, a novel retinal RT epithelial membrane protein."; RL Exp. Cell Res. 219:64-73(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Retinal pigment epithelium; RX PubMed=9168967; DOI=10.1006/bbrc.1997.6588; RA Yoon H., Fanelli A., Grollman E.F., Philp N.J.; RT "Identification of a unique monocarboxylate transporter (MCT3) in retinal RT pigment epithelium."; RL Biochem. Biophys. Res. Commun. 234:90-94(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Leghorn; RX PubMed=9820789; DOI=10.1006/exer.1998.0533; RA Yoon H., Philp N.J.; RT "Genomic structure and developmental expression of the chicken RT monocarboxylate transporter MCT3 gene."; RL Exp. Eye Res. 67:417-424(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl; RX PubMed=15592404; DOI=10.1038/nature03154; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V., RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., RA Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide unique RT perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [5] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TRANSPORTER ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=10924129; DOI=10.1021/bi000464+; RA Grollman E.F., Philp N.J., McPhie P., Ward R.D., Sauer B.; RT "Determination of transport kinetics of chick MCT3 monocarboxylate RT transporter from retinal pigment epithelium by expression in genetically RT modified yeast."; RL Biochemistry 39:9351-9357(2000). CC -!- FUNCTION: Probable retinal pigment epithelium (RPE)-specific proton- CC coupled L-lactate transporter (Probable). May facilitate transport of CC lactate and H(+) out of the retina and could therefore play a role in CC pH and ion homeostasis of the outer retina (By similarity). CC {ECO:0000250|UniProtKB:O35308, ECO:0000305|PubMed:10924129, CC ECO:0000305|PubMed:9168967}. 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:0000305|PubMed:10924129}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6 mM for L-lactate {ECO:0000269|PubMed:10924129}; CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane CC {ECO:0000269|PubMed:10924129, ECO:0000269|PubMed:7628551}; Multi-pass CC membrane protein {ECO:0000255}. Note=Basolateral sorting signals (BLSS) CC in C-terminal cytoplasmic tail ensure its basolateral expression (By CC similarity). Colocalizes with BSG in basolateral cell membrane of the CC retinal pigment epithelium (By similarity). CC {ECO:0000250|UniProtKB:O35308, ECO:0000250|UniProtKB:O95907}. CC -!- TISSUE SPECIFICITY: Retinal pigment epithelium. CC {ECO:0000269|PubMed:7628551, ECO:0000269|PubMed:9168967}. CC -!- DEVELOPMENTAL STAGE: First detected at embryonic day 5 (E5) in both CC apical and basolateral membranes. By E14 the distribution is restricted CC to the basolateral surface of retinal pigment epithelium. Restricted to CC the basolateral membrane in adult. {ECO:0000269|PubMed:7628551}. CC -!- DOMAIN: The two basolateral sorting signals (BSS) are required to CC direct SLC16A8 to the basolateral membrane. CC {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; U15685; AAB52367.1; -; mRNA. DR EMBL; AF000240; AAB61338.1; -; Genomic_DNA. DR EMBL; AADN05000523; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; JC5507; JC5507. DR RefSeq; NP_990471.2; NM_205140.2. DR AlphaFoldDB; Q90632; -. DR SMR; Q90632; -. DR STRING; 9031.ENSGALP00000020054; -. DR PaxDb; Q90632; -. DR Ensembl; ENSGALT00000052449; ENSGALP00000044229; ENSGALG00000036897. DR GeneID; 396041; -. DR KEGG; gga:396041; -. DR CTD; 23539; -. DR VEuPathDB; HostDB:geneid_396041; -. DR eggNOG; KOG2504; Eukaryota. DR GeneTree; ENSGT00940000161934; -. DR HOGENOM; CLU_001265_59_1_1; -. DR InParanoid; Q90632; -. DR OMA; VYFKELM; -. DR OrthoDB; 916876at2759; -. DR PhylomeDB; Q90632; -. DR TreeFam; TF313792; -. DR Reactome; R-GGA-210991; Basigin interactions. DR Reactome; R-GGA-433692; Proton-coupled monocarboxylate transport. DR Reactome; R-GGA-70268; Pyruvate metabolism. DR PRO; PR:Q90632; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000036897; Expressed in cerebellum. 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: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; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00892; 2A0113; 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..542 FT /note="Monocarboxylate transporter 3" FT /id="PRO_0000211393" FT TOPO_DOM 1..19 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 41..63 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 64..84 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 85..93 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 94..114 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 115..119 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 120..140 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 141..152 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 153..173 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 174..181 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 182..202 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 203..265 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 287..301 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 302..322 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 323..330 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 331..351 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 352..357 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 358..378 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 379..392 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 393..413 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 414..423 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 424..444 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 445..542 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 453..542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 465..510 FT /note="Basolateral sorting signal" FT /evidence="ECO:0000250|UniProtKB:O95907" FT REGION 511..532 FT /note="Basolateral sorting signal" FT /evidence="ECO:0000250|UniProtKB:O95907" FT COMPBIAS 501..517 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 6 FT /note="P -> R (in Ref. 1; AAB52367)" FT CONFLICT 225 FT /note="M -> I (in Ref. 1; AAB52367)" FT CONFLICT 291 FT /note="A -> P (in Ref. 1; AAB52367)" FT CONFLICT 345 FT /note="L -> S (in Ref. 1; AAB52367)" FT CONFLICT 441..442 FT /note="AM -> PW (in Ref. 1; AAB52367)" FT CONFLICT 525 FT /note="V -> A (in Ref. 1; AAB52367)" SQ SEQUENCE 542 AA; 58085 MW; F5ACAAABFD351C21 CRC64; MGRADPEEGQ LPAPVKPPDG GWGWIVLFGC FVITGFSYAF PKAVSVYFKE LMKDFHVGYS DTAWISSIML AMLYGTGPVC SIMVNQFGCR PVMLIGGLLA SSGMILASFT TNIIELYLTA GVLTGLGMAL NFQPSLIMLG TYFDKRRPLA NGLAAAGSPV FLSSLSPLGQ VLLEKFGWRG GFLIMGGLLL NCCTCGAVMR PLDAGMKRKT EKAQDKYEAK EMLPMGGKSE EGISTTDGTK KTKKAKKKPK KGKKLLDFSI FSNRGFIIYT ISKFILVLGL FVPPILLVNY AKDTGVPDTE AAFLLSIIGF IDIFARPACG MVAGLKWVRP HVAYLFSFAM LFNGLTDICS ARASNYTGLV IFCVFFGISY GMVGALQFEV LMAIVGSQKF SSAIGLVLLI EAFAVLIGPP SAGRLVDALK NYEVIFYLAG SEVVLSALFL AMATYCCLNR GKKTPPPEKN PSAGGGSDTE EAESDVQEAE EHSSDNHQPA HGTDKATVAA NEEANHVEDE QSGEGGRCPE ADGEVSSRAG CNADQTVERD SF //