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 23-FEB-2022, entry version 128. DE RecName: Full=Monocarboxylate transporter 3; DE Short=MCT 3; DE AltName: Full=Retinal epithelial membrane protein; DE AltName: Full=Solute carrier family 16 member 8; GN Name=SLC16A3; Synonyms=MCT3, REMP; 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]. 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]. 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). CC -!- FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the CC rapid transport across the plasma membrane of many monocarboxylates CC such as lactate, pyruvate, branched-chain oxo acids derived from CC leucine, valine and isoleucine, and the ketone bodies acetoacetate, CC beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}. 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 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. 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 PIR; JC5507; JC5507. DR RefSeq; NP_990471.2; NM_205140.2. DR SMR; Q90632; -. DR STRING; 9031.ENSGALP00000020054; -. DR PaxDb; Q90632; -. DR GeneID; 396041; -. DR KEGG; gga:396041; -. DR CTD; 23539; -. DR eggNOG; KOG2504; Eukaryota. DR HOGENOM; CLU_001265_59_1_1; -. DR InParanoid; Q90632; -. DR OrthoDB; 916876at2759; -. DR PhylomeDB; Q90632; -. DR TreeFam; TF313792; -. DR PRO; PR:Q90632; -. DR Proteomes; UP000000539; Unplaced. DR Bgee; ENSGALG00000012288; Expressed in cerebellum and 4 other tissues. 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 2: Evidence at transcript 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 COMPBIAS 501..517 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 6 FT /note="R -> P (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="I -> M (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" FT CONFLICT 291 FT /note="P -> A (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" FT CONFLICT 345 FT /note="S -> L (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" FT CONFLICT 441..442 FT /note="PW -> AM (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" FT CONFLICT 525 FT /note="A -> V (in Ref. 2; AAB61338)" FT /evidence="ECO:0000305" 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 //