MOT3_CHICK
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}.
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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
