MAE1_SCHPO
ID MAE1_SCHPO Reviewed; 438 AA.
AC P50537; A1EGU0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Malic acid transport protein;
DE AltName: Full=Malate permease;
GN Name=mae1; ORFNames=SPAPB8E5.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8750236; DOI=10.1002/yea.320111503;
RA Grobler J., Bauer F., Subden R.E., van Vuuren H.J.J.;
RT "The mae1 gene of Schizosaccharomyces pombe encodes a permease for malate
RT and other C4 dicarboxylic acids.";
RL Yeast 11:1485-1491(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li A., Su X.;
RT "Sequencing and analysis of malate degradation related enzyme gene from
RT Schizosaccharomyces pombe.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-423; SER-428;
RP SER-432; SER-433 AND SER-437, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Permease for malate and other C4 dicarboxylic acids.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) 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; U21002; AAC49149.1; -; Genomic_DNA.
DR EMBL; EF125015; ABL67724.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC37422.1; -; Genomic_DNA.
DR PIR; S61876; S61876.
DR RefSeq; NP_594777.1; NM_001020205.2.
DR AlphaFoldDB; P50537; -.
DR SMR; P50537; -.
DR BioGRID; 279757; 3.
DR STRING; 4896.SPAPB8E5.03.1; -.
DR TCDB; 2.A.16.2.1; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR iPTMnet; P50537; -.
DR MaxQB; P50537; -.
DR PaxDb; P50537; -.
DR PRIDE; P50537; -.
DR EnsemblFungi; SPAPB8E5.03.1; SPAPB8E5.03.1:pep; SPAPB8E5.03.
DR GeneID; 2543334; -.
DR KEGG; spo:SPAPB8E5.03; -.
DR PomBase; SPAPB8E5.03; mae1.
DR VEuPathDB; FungiDB:SPAPB8E5.03; -.
DR eggNOG; ENOG502QV03; Eukaryota.
DR HOGENOM; CLU_030057_2_0_1; -.
DR InParanoid; P50537; -.
DR OMA; LPCREHR; -.
DR PhylomeDB; P50537; -.
DR PRO; PR:P50537; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015366; F:malate:proton symporter activity; IDA:PomBase.
DR GO; GO:1901239; F:malonate(1-) transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0097434; F:succinate:proton symporter activity; IDA:PomBase.
DR GO; GO:0098714; P:malate import across plasma membrane; IDA:PomBase.
DR GO; GO:0098715; P:malonic acid import across plasma membrane; IMP:PomBase.
DR GO; GO:0098720; P:succinate import across plasma membrane; IMP:PomBase.
DR CDD; cd09317; TDT_Mae1_like; 1.
DR Gene3D; 1.50.10.150; -; 1.
DR InterPro; IPR030185; Mae1.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR InterPro; IPR011552; TehA/Mae1.
DR InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR PANTHER; PTHR31162; PTHR31162; 1.
DR Pfam; PF03595; SLAC1; 1.
DR TIGRFAMs; TIGR00816; tdt; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..438
FT /note="Malic acid transport protein"
FT /id="PRO_0000084550"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 390..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 438 AA; 49304 MW; AA948E8DA4B84F36 CRC64;
MGELKEILKQ RYHELLDWNV KAPHVPLSQR LKHFTWSWFA CTMATGGVGL IIGSFPFRFY
GLNTIGKIVY ILQIFLFSLF GSCMLFRFIK YPSTIKDSWN HHLEKLFIAT CLLSISTFID
MLAIYAYPDT GEWMVWVIRI LYYIYVAVSF IYCVMAFFTI FNNHVYTIET ASPAWILPIF
PPMICGVIAG AVNSTQPAHQ LKNMVIFGIL FQGLGFWVYL LLFAVNVLRF FTVGLAKPQD
RPGMFMFVGP PAFSGLALIN IARGAMGSRP YIFVGANSSE YLGFVSTFMA IFIWGLAAWC
YCLAMVSFLA GFFTRAPLKF ACGWFAFIFP NVGFVNCTIE IGKMIDSKAF QMFGHIIGVI
LCIQWILLMY LMVRAFLVND LCYPGKDEDA HPPPKPNTGV LNPTFPPEKA PASLEKVDTH
VTSTGGESDP PSSEHESV
