MOT4_CHICK
ID MOT4_CHICK Reviewed; 473 AA.
AC P57788; A0A0C3SFZ3; Q9DEY5; Q9DG24;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Monocarboxylate transporter 4;
DE Short=MCT 4;
DE AltName: Full=Solute carrier family 16 member 3;
GN Name=SLC16A3; Synonyms=MCT4;
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 [GENOMIC DNA / MRNA].
RA Yoon H., Philp N.;
RT "Characterization of the chicken and mouse MCT4 genes: tissue distribution
RT and relationship to other monocarboxylate transporters.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- FUNCTION: Proton-dependent transporter of monocarboxylates such as L-
CC lactate and pyruvate (By similarity). Plays a predominant role in the
CC transport of L-lactate efflux from highly glycolytic cells (By
CC similarity). {ECO:0000250|UniProtKB:O15427,
CC ECO:0000250|UniProtKB:O35910}.
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:O15427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29416;
CC Evidence={ECO:0000250|UniProtKB:O15427};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417;
CC Evidence={ECO:0000250|UniProtKB:O15427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in);
CC Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:O15427};
CC -!- SUBUNIT: Interacts with BSG; interaction mediates SLC16A3 targeting to
CC the plasma membrane. {ECO:0000250|UniProtKB:O15427}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15427};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Plasma membrane localization is dependent upon the
CC BSG/MCT4 interaction. Basolateral sorting signals (BLSS) in C-terminal
CC cytoplasmic tail ensure its basolateral expression in polarised
CC epithelial cells. {ECO:0000250|UniProtKB:O15427}.
CC -!- DOMAIN: Two basolateral sorting signals (BSS) in its C-terminal
CC cytoplasmic tail are required to direct SLC16A3 to the basolateral
CC membrane. {ECO:0000250|UniProtKB:O15427}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to be considered to be a low affinity
CC lactate transporter with negligible affinity for pyruvate (By
CC similarity). However, it was later shown that SLC16A3 is a high
CC affinity lactate transporter with physiologically relevant affinity for
CC pyruvate (By similarity). {ECO:0000250|UniProtKB:O15427}.
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DR EMBL; AF204396; AAF67524.1; -; mRNA.
DR EMBL; AF308452; AAG25703.1; -; Genomic_DNA.
DR EMBL; AADN05000628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989994.1; NM_204663.1.
DR AlphaFoldDB; P57788; -.
DR SMR; P57788; -.
DR STRING; 9031.ENSGALP00000004297; -.
DR PaxDb; P57788; -.
DR Ensembl; ENSGALT00000004306; ENSGALP00000004297; ENSGALG00000002728.
DR GeneID; 395383; -.
DR KEGG; gga:395383; -.
DR CTD; 9123; -.
DR VEuPathDB; HostDB:geneid_395383; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000158181; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR OMA; IFARPLC; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; P57788; -.
DR TreeFam; TF313792; -.
DR Reactome; R-GGA-373920; Pyruvate metabolism.
DR PRO; PR:P57788; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000002728; Expressed in granulocyte and 11 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR030756; MCT4.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF27; PTHR11360:SF27; 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..473
FT /note="Monocarboxylate transporter 4"
FT /id="PRO_0000211397"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 421..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..449
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250|UniProtKB:O15427"
FT REGION 449..473
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250|UniProtKB:O15427"
FT CONFLICT 103
FT /note="V -> A (in Ref. 1; AAF67524)"
SQ SEQUENCE 473 AA; 51069 MW; 1A23FA31FB317707 CRC64;
MGAVVVDDGP SGVKAPDGGW GWAVLFGCFI ITGFSYAFPK AVSVFFKELI REFGVGYSDT
AWISSILLAM LYGTGPLCSV CVNRFGCRPV MLVGGLFASM GMVIASFCTS IVQIYLTAGV
ITGLGLALNF QPSLIMLNRY FDKRRPLANG LSAAGSPVFL CALSPLGQIL QHEYGWRGGF
LILGGMLLNC CVCGALMRPL EPPKKSEATK EPAEKKAKKK LLDFSVFKDG GFVIYTLAAS
IMVLGLFVPP VFVVSYAKDL GYQDTKAAFL LTILGFIDIF ARPICGMVAG LKWVRPRCVY
LFSFAMIFNG FTDLMGSMSV DYGGLVVFCI FFGISYGMVG ALQFEVLMAI VGTQKFSSAI
GLVLLAEAMA VLIGPPSAGK LLDLTRRYMF VFIIAGIEVT TSALVLALGN FFCIKKKPAE
PHTKEAAAER EELNKSEDKT PEDAKVDSIE VEQFLKDEPE KNGEVVTNPE TCV
