PNS1_KLULA
ID PNS1_KLULA Reviewed; 553 AA.
AC Q6CY85;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein PNS1;
GN Name=PNS1; OrderedLocusNames=KLLA0A02343g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH02692.1; -; Genomic_DNA.
DR RefSeq; XP_451104.1; XM_451104.1.
DR AlphaFoldDB; Q6CY85; -.
DR STRING; 28985.XP_451104.1; -.
DR EnsemblFungi; CAH02692; CAH02692; KLLA0_A02343g.
DR GeneID; 2896692; -.
DR KEGG; kla:KLLA0_A02343g; -.
DR eggNOG; KOG1362; Eukaryota.
DR HOGENOM; CLU_026724_0_0_1; -.
DR InParanoid; Q6CY85; -.
DR OMA; FTKQFIW; -.
DR Proteomes; UP000000598; Chromosome A.
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..553
FT /note="Protein PNS1"
FT /id="PRO_0000191736"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 553 AA; 61452 MW; 25B479F48C2BDD20 CRC64;
MFGEGNKPTE PVPAYDAGQD PFQGPNASKN QYQGSAADYN GAPPPPASQP GNQYQFRQDQ
YYNLNAEGEG APIGSFEEKF PVEGEDSKPK WNDWPFTIFF AGCVIAFIVV AAITLRAWSQ
NSSSQGSGVY DGANTGTLTT NSAIMLAISC IIAFVFSIIG IVLARMFPKF FIIAGILFNI
IAGLATAIMY LSLKYYSAGI VFLVFTAICA LFYWRMRHRI PFTVAVLKTV MDVMKSYPQT
WFVTLIGSII ATAFSILFSA VIVATYMKYD DKANNPGCST NGGSCSNAKL IGLLVLVFFC
GYYIAEVIRN VIHCTVSGIF GAWYYFSKSD QGMPKWPGFG ALKRSLTYSF GSICFGSLIV
TIIETLKAVL RLAVDGVMGG GGADNGWMQC LALIANWIFS FLEWLARYFN HYAYVFIALY
GKPYLRAAKE TWYMLREKGI DALINDNLVN VALSFFTLFT CYITTLFAYL YLRYTDPNYN
DNNNFTPALM AFAFVIAMEI CNVITETIRS GTATFFVALG NDPEVFHLSY PERFDEIFRA
YPEVLKKLSH QNV
