ID   PNS1_USTMA              Reviewed;         529 AA.
AC   Q4PIP8; A0A0D1E6Q3;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Protein PNS1;
GN   Name=PNS1; ORFNames=UMAG_12080;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably involved in transport through the plasma membrane.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC       {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; CM003140; KIS71569.1; -; Genomic_DNA.
DR   RefSeq; XP_011386824.1; XM_011388522.1.
DR   AlphaFoldDB; Q4PIP8; -.
DR   SMR; Q4PIP8; -.
DR   STRING; 5270.UM00015P0; -.
DR   EnsemblFungi; KIS71569; KIS71569; UMAG_12080.
DR   GeneID; 23567847; -.
DR   KEGG; uma:UMAG_12080; -.
DR   VEuPathDB; FungiDB:UMAG_12080; -.
DR   eggNOG; KOG1362; Eukaryota.
DR   HOGENOM; CLU_026724_0_0_1; -.
DR   InParanoid; Q4PIP8; -.
DR   OrthoDB; 1276753at2759; -.
DR   Proteomes; UP000000561; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR007603; Choline_transptr-like.
DR   PANTHER; PTHR12385; PTHR12385; 1.
DR   Pfam; PF04515; Choline_transpo; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..529
FT                   /note="Protein PNS1"
FT                   /id="PRO_0000191738"
FT   TOPO_DOM        1..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..132
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..271
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..325
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        347..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..427
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..464
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        486..529
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   529 AA;  57785 MW;  4229946AF7FBB3D8 CRC64;
     MSQQYSYGGG GGAGYPPPQM QPPNSYAQAN YQGQPQGAQN QYYNGQQPHH NAPQQYYGND
     YKQPLKPEGF EGERLQPKPK FRDPIFLVLF LLVFAGFIAL SVICLRSYSN ADVNVSIGRA
     NVAGSTLNGH TAIMFMICCA VALVLSFVYI LLVRTFPKII LEATLLLTTL SNVAFCVYLW
     VRGNTAAAII FTIFAVLSVI AYFFMRKRIP LAKLILVTVI RTAEQYKSVY VVALGGLIVE
     TAFSAWTSWV VVAAYQRFEP SGQAAGSSSS NASIIGIMVF IVFAYYWISE VIKNIAFTTV
     AGIFGVAYYN ANKVANAAWG AFRRSMTYSL GSICFGSLIV AILDLLRALF NILQSQAASD
     GDMTGQILAC VAGCCVSCIQ GLVDYFNRYA YINIALYGNG YITAAKETWA LLKDRGIDAI
     INDSLVNIVF NCGAFIIGLL TALFAFIYEQ LTNPRYLQND AGYYSIVLLV AFGLGFNIAL
     SVGAGSIASG VSTYFVALAE DPYILQGKNP ELFEMIRQQY PQVVQGVNH