PNS1_DEBHA
ID PNS1_DEBHA Reviewed; 513 AA.
AC Q6BIV4; B5RV47;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein PNS1;
GN Name=PNS1; OrderedLocusNames=DEHA2G07326g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382139; CAR65928.1; -; Genomic_DNA.
DR RefSeq; XP_002770593.1; XM_002770547.1.
DR AlphaFoldDB; Q6BIV4; -.
DR STRING; 4959.XP_002770593.1; -.
DR EnsemblFungi; CAR65928; CAR65928; DEHA2G07326g.
DR GeneID; 8999141; -.
DR KEGG; dha:DEHA2G07326g; -.
DR VEuPathDB; FungiDB:DEHA2G07326g; -.
DR eggNOG; KOG1362; Eukaryota.
DR HOGENOM; CLU_026724_0_0_1; -.
DR InParanoid; Q6BIV4; -.
DR OMA; FTKQFIW; -.
DR OrthoDB; 1276753at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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..513
FT /note="Protein PNS1"
FT /id="PRO_0000191734"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 513 AA; 57661 MW; 93E8CF277791BAC8 CRC64;
MSNNNYPPPP NPPNYQGEEQ VHNVQPDLEN NQEKYYAEQP QPSQQFEESF KIDKPKWNDW
PFTVFFLLTV AGFIAIAGIT LNALKKTYGL QGSSIYNSTD TFTLNTNTII LFGFIIVVGV
VLSVLIIVYA RMAPRVFITT GLILNIILGL GTCIYYFVAH YYSAAIVFLV FTLFTAWCYW
SCRHRIPFSA TVLEITIDVM KRYPSTLITS FIGIIVSGLF STLFSVVIVA TYVKYDPDSQ
GCDVAGGGCS QSKLIGVLVF VFFAGYYISE VIKNVIHITI AGIYGTWYYL SNSDQGEPKH
PALGAFKRAM TYCFGSVCFG SLIVSIIQLI RSFVQILKQN AFGSGDNCAG CGFLILDFVL
GFIDWIVRYF NHYAYCYVAL YGKSYLKSAR DTFDLIRFKG MDALINDCFI NTSLNLYSMF
VGYVVALLAY FYLKFTDPAY NSSGTFYAPV VAFSFLISGQ ITRIALTVIS SGISTFFVAL
AKDPEVFQMT NRDRFDEIFR NYPQVLQKIT SDH
