PNS1_CANGA
ID PNS1_CANGA Reviewed; 557 AA.
AC Q6FLC9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein PNS1;
GN Name=PNS1; OrderedLocusNames=CAGL0L04378g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR380958; CAG61935.1; -; Genomic_DNA.
DR RefSeq; XP_448965.1; XM_448965.1.
DR AlphaFoldDB; Q6FLC9; -.
DR STRING; 5478.XP_448965.1; -.
DR EnsemblFungi; CAG61935; CAG61935; CAGL0L04378g.
DR GeneID; 2890635; -.
DR KEGG; cgr:CAGL0L04378g; -.
DR CGD; CAL0135642; CAGL0L04378g.
DR VEuPathDB; FungiDB:CAGL0L04378g; -.
DR eggNOG; KOG1362; Eukaryota.
DR HOGENOM; CLU_026724_0_0_1; -.
DR InParanoid; Q6FLC9; -.
DR OMA; FTKQFIW; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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..557
FT /note="Protein PNS1"
FT /id="PRO_0000191732"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 557 AA; 62610 MW; F4F72FEFD23BE910 CRC64;
MSTEKQYQPQ QPPPAYTGQG PDNGNAYGYP ESYGKTETHS GDSCSGDTSM NPQQQGQQYQ
FRKDDEFYNL NHEGAGAPIG SYAEVFPTED NNKPKFNDWP FIIVFLLTLC GFIVVASLTL
RAWSQTYSST GSGIYHDFDT GTLNTNSVIL LVFSVVIAIF FAFIGIVLCR AYPKFFIYAG
MIVNILAALG TAIMYMSLKY WSAGIVFLIF TFMTAWCYWG MRSRIPLTVA ILRVIVLAMK
NCPQSLFVSF FGTIVASAFA MLFSTVVVAT YMKYDPSNTN SGCNVSGGDC SHAKLIGVLV
VVFFCGYYIS EVIRNVMHCT VSGVFGSWYY RYKSDQGMPK WPAMGAFKRA MTYSFGSICF
GSLIVSIIET FRQLLQLGKQ AAIASTDNAN WIRIIFWLID MLVGFIQWIA QYFNHYAYCI
IALYGKPYLK AAKQTWYMFR EKGIDALIND NLVNVALGFY SLFASYMSCL FAFLYLRFTK
PGYNSDGDFN APLMAFAFVI ALQLTNIANE TIRSGCATFF TALGHDPEVF QAQYPDRFDE
IFRSYPQVLN KLTHQDV
