ID   YL47_SCHPO              Reviewed;         533 AA.
AC   Q9UT92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Uncharacterized transporter C323.07c;
GN   ORFNames=SPAC323.07c;
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 [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   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; TYR-25 AND
RP   SER-26, 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   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB53410.1; -; Genomic_DNA.
DR   PIR; T38644; T38644.
DR   RefSeq; NP_594377.1; NM_001019798.2.
DR   AlphaFoldDB; Q9UT92; -.
DR   SMR; Q9UT92; -.
DR   BioGRID; 278128; 2.
DR   STRING; 284812.Q9UT92; -.
DR   iPTMnet; Q9UT92; -.
DR   PaxDb; Q9UT92; -.
DR   PRIDE; Q9UT92; -.
DR   EnsemblFungi; SPAC323.07c.1; SPAC323.07c.1:pep; SPAC323.07c.
DR   GeneID; 2541632; -.
DR   KEGG; spo:SPAC323.07c; -.
DR   PomBase; SPAC323.07c; -.
DR   VEuPathDB; FungiDB:SPAC323.07c; -.
DR   eggNOG; KOG1347; Eukaryota.
DR   HOGENOM; CLU_012893_1_2_1; -.
DR   InParanoid; Q9UT92; -.
DR   OMA; AAWFELF; -.
DR   PhylomeDB; Q9UT92; -.
DR   Reactome; R-SPO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR   PRO; PR:Q9UT92; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR   CDD; cd13132; MATE_eukaryotic; 1.
DR   InterPro; IPR045069; MATE_euk.
DR   InterPro; IPR002528; MATE_fam.
DR   Pfam; PF01554; MatE; 2.
DR   TIGRFAMs; TIGR00797; matE; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..533
FT                   /note="Uncharacterized transporter C323.07c"
FT                   /id="PRO_0000316590"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         25
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   533 AA;  58597 MW;  4BADBC5DB9D88D4A CRC64;
     MKRFFSKLFS KSPTSGRVPS PDSDYSEEEQ RLLAEENGYF QDSNEYVEPN IPAVYGSMIP
     VAQQLQQHHV HTPGESFADN ASGYPVIKHE LSELLRLGSP TVIAYLLQSS EQFSTVFTLG
     HLGKEYLAAS SLSTMTAAIS AFSIFQGVIS SLDTLATQAF GANKPYNVAI YLQRCLLILA
     VLHIPVALIW LNLEHILIFL HQDPMVAHLC GRYMRVFILA APGYAVFEAL KRYLQAQGIF
     TPITYVLCFA APLNILLNYL LVWHPTIGFG FLGAPVAVAT TFWFQSICLI LYICFSSTPI
     PWPGFSRQAL KNLSPMLHFS FHGMLMIVTE WAAYEMTSLG AGYLGTAPLA SQSILLTSTS
     LLFQIPFAFA VASSTRVGHL IGSGRANLAR LCSRVAYSLA LCISIFDGSL IFCFRDVWGS
     LFTSDPEVLA VVKDIFPILS LFIVTDGLNA VGGGLLRGTG KQYIGGLISI GSSYLFALPV
     TVFVVVYFNT GLKGIWCGMI LSSVTAITCQ FTVLFNTDWH RVLQEARHRL THV