ID   YQD3_SCHPO              Reviewed;         570 AA.
AC   Q9C0U9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Uncharacterized transporter PB1C11.03;
GN   ORFNames=SPCPB1C11.03;
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] {ECO:0000312|EMBL:CAC36936.1}
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] {ECO:0000305}
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] {ECO:0000305}
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP   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: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC       permease family. {ECO:0000255}.
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DR   EMBL; CU329672; CAC36936.1; -; Genomic_DNA.
DR   RefSeq; NP_588426.1; NM_001023417.2.
DR   AlphaFoldDB; Q9C0U9; -.
DR   SMR; Q9C0U9; -.
DR   BioGRID; 276016; 6.
DR   STRING; 4896.SPCPB1C11.03.1; -.
DR   iPTMnet; Q9C0U9; -.
DR   MaxQB; Q9C0U9; -.
DR   PaxDb; Q9C0U9; -.
DR   PRIDE; Q9C0U9; -.
DR   EnsemblFungi; SPCPB1C11.03.1; SPCPB1C11.03.1:pep; SPCPB1C11.03.
DR   PomBase; SPCPB1C11.03; -.
DR   VEuPathDB; FungiDB:SPCPB1C11.03; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_0_5_1; -.
DR   InParanoid; Q9C0U9; -.
DR   OMA; WFDYPSN; -.
DR   PhylomeDB; Q9C0U9; -.
DR   PRO; PR:Q9C0U9; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0033229; F:cysteine transmembrane transporter activity; ISO:PomBase.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1903712; P:cysteine transmembrane transport; ISO:PomBase.
DR   GO; GO:0042883; P:cysteine transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..570
FT                   /note="Uncharacterized transporter PB1C11.03"
FT                   /id="PRO_0000372786"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   570 AA;  64329 MW;  D1B11A6F7806BBF2 CRC64;
     MTESIISSRT ASISSKEGYE IRQGSTDSSS LDLEKKENAV DTTIAKPFDS DEDIADVEKA
     GGKKINNSLI DETFAFMQDA KKLDPLTPKQ ESKLKWKLYI YLLLMLGFLD MMLFIGKATL
     SYSTILGLFD DVHITSNQYN NLNTLFYVGY IVGQFPGHYI MQTFPLGKFV GLVTFSWSVI
     VFLHCCAYNY GGLIALRFFL GFTESCLLPA MEATMGMFFT HQEQAFLQPV FWISCLSCGI
     PAGFIAYGLE FVTKSIAPWK LFMIITGGIT FFLSIFLFFY YPDNPSKARF LTDEEKLYTI
     DRVRKSTRGG IENKIFKKHQ FIEALKDPIT WLFTFAAFTL MLSNNLAYQQ NLIFTSLNVS
     DLNSTLVGVA LAGYNTVSAI IATFAMYLIP NQSAYHAMFW MLPSITGGIA FVALPWSNRI
     GELATMIIAS DFGITYIIAL GWTTATSTGY TKKLTRGLMF MVGYAIANII SPQLWQSRDA
     PRYYPAWIVQ IVVAWFVTPI IYLVARVILA RRNKQRKELK DKKIAEGSLE TIEKTYVDTV
     DEFGNPVKVL IDNSMLDLTD MENLNFVYPL