ID MOT3_CHICK Reviewed; 542 AA. AC Q90632; O13151; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 02-MAR-2010, entry version 69. DE RecName: Full=Monocarboxylate transporter 3; DE Short=MCT 3; DE AltName: Full=Solute carrier family 16 member 8; DE AltName: Full=Retinal epithelial membrane protein; GN Name=SLC16A3; Synonyms=MCT3, REMP; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retinal pigment epithelium; RX MEDLINE=95354777; 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., RA Boettiger D., Yoon H., Kieber-Emmons T.; RT "Developmental expression and molecular cloning of REMP, a novel RT retinal epithelial membrane protein."; RL Exp. Cell Res. 219:64-73(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 RT retinal pigment epithelium."; RL Biochem. Biophys. Res. Commun. 234:90-94(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Leghorn; RX MEDLINE=99040073; 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). CC -!- FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the CC rapid transport across the plasma membrane of many CC monocarboxylates such as lactate, pyruvate, branched-chain oxo CC acids derived from leucine, valine and isoleucine, and the ketone CC bodies acetoacetate, beta-hydroxybutyrate and acetate (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Retinal pigment epithelium. CC -!- DEVELOPMENTAL STAGE: First detected at embryonic day 5 (E5) in CC both apical and basolateral membranes. By E14 the distribution is CC restricted to the basolateral surface of retinal pigment CC epithelium. Restricted to the basolateral membrane in adult. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. 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 IPI; IPI00571027; -. DR PIR; JC5507; JC5507. DR RefSeq; NP_990471.1; -. DR UniGene; Gga.612; -. DR SMR; Q90632; 10-438. DR Ensembl; ENSGALT00000020081; ENSGALP00000020054; ENSGALG00000012288; Gallus gallus. DR GeneID; 396041; -. DR KEGG; gga:396041; -. DR CTD; 396041; -. DR eggNOG; veNOG09298; -. DR HOGENOM; HBG444740; -. DR HOVERGEN; HBG006384; -. DR InParanoid; Q90632; -. DR PhylomeDB; Q90632; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015355; F:secondary active monocarboxylate transmembr...; IEA:InterPro. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0015711; P:organic anion transport; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS_1. DR InterPro; IPR016196; MFS_general_subst_transpt. DR InterPro; IPR004743; Monocarb_transpt. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1. DR TIGRFAMs; TIGR00892; 2A0113; 1. DR PROSITE; PS50850; MFS; 1. PE 2: Evidence at transcript level; KW Cell membrane; Membrane; Symport; Transmembrane; Transport. FT CHAIN 1 542 Monocarboxylate transporter 3. FT /FTId=PRO_0000211393. FT TOPO_DOM 1 19 Cytoplasmic (Potential). FT TRANSMEM 20 40 Potential. FT TOPO_DOM 41 63 Extracellular (Potential). FT TRANSMEM 64 84 Potential. FT TOPO_DOM 85 93 Cytoplasmic (Potential). FT TRANSMEM 94 114 Potential. FT TOPO_DOM 115 119 Extracellular (Potential). FT TRANSMEM 120 140 Potential. FT TOPO_DOM 141 152 Cytoplasmic (Potential). FT TRANSMEM 153 173 Potential. FT TOPO_DOM 174 181 Extracellular (Potential). FT TRANSMEM 182 202 Potential. FT TOPO_DOM 203 265 Cytoplasmic (Potential). FT TRANSMEM 266 286 Potential. FT TOPO_DOM 287 301 Extracellular (Potential). FT TRANSMEM 302 322 Potential. FT TOPO_DOM 323 330 Cytoplasmic (Potential). FT TRANSMEM 331 351 Potential. FT TOPO_DOM 352 357 Extracellular (Potential). FT TRANSMEM 358 378 Potential. FT TOPO_DOM 379 392 Cytoplasmic (Potential). FT TRANSMEM 393 413 Potential. FT TOPO_DOM 414 423 Extracellular (Potential). FT TRANSMEM 424 444 Potential. FT TOPO_DOM 445 542 Cytoplasmic (Potential). FT CONFLICT 6 6 R -> P (in Ref. 2; AAB61338). FT CONFLICT 225 225 I -> M (in Ref. 2; AAB61338). FT CONFLICT 291 291 P -> A (in Ref. 2; AAB61338). FT CONFLICT 345 345 S -> L (in Ref. 2; AAB61338). FT CONFLICT 441 442 PW -> AM (in Ref. 2; AAB61338). FT CONFLICT 525 525 A -> V (in Ref. 2; AAB61338). SQ SEQUENCE 542 AA; 58179 MW; 4E8B71A140FA09B0 CRC64; MGRADREEGQ LPAPVKPPDG GWGWIVLFGC FVITGFSYAF PKAVSVYFKE LMKDFHVGYS DTAWISSIML AMLYGTGPVC SIMVNQFGCR PVMLIGGLLA SSGMILASFT TNIIELYLTA GVLTGLGMAL NFQPSLIMLG TYFDKRRPLA NGLAAAGSPV FLSSLSPLGQ VLLEKFGWRG GFLIMGGLLL NCCTCGAVMR PLDAGMKRKT EKAQDKYEAK EMLPIGGKSE EGISTTDGTK KTKKAKKKPK KGKKLLDFSI FSNRGFIIYT ISKFILVLGL FVPPILLVNY PKDTGVPDTE AAFLLSIIGF IDIFARPACG MVAGLKWVRP HVAYLFSFAM LFNGSTDICS ARASNYTGLV IFCVFFGISY GMVGALQFEV LMAIVGSQKF SSAIGLVLLI EAFAVLIGPP SAGRLVDALK NYEVIFYLAG SEVVLSALFL PWATYCCLNR GKKTPPPEKN PSAGGGSDTE EAESDVQEAE EHSSDNHQPA HGTDKATVAA NEEANHVEDE QSGEGGRCPE ADGEASSRAG CNADQTVERD SF //