FUN26_YEAST
ID FUN26_YEAST Reviewed; 517 AA.
AC P31381; D6VPJ6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nucleoside transporter FUN26;
GN Name=FUN26; OrderedLocusNames=YAL022C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10827169; DOI=10.1074/jbc.m000239200;
RA Vickers M.F., Yao S.Y., Baldwin S.A., Young J.D., Cass C.E.;
RT "Nucleoside transporter proteins of Saccharomyces cerevisiae. Demonstration
RT of a transporter (FUI1) with high uridine selectivity in plasma membranes
RT and a transporter (FUN26) with broad nucleoside selectivity in
RT intracellular membranes.";
RL J. Biol. Chem. 275:25931-25938(2000).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Has broad nucleoside selectivity (uridine, adenosine and
CC cytidine) and most likely functions to transport nucleosides across
CC intracellular membranes.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; L05146; AAC04935.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06966.1; -; Genomic_DNA.
DR PIR; S36712; S36712.
DR RefSeq; NP_009380.1; NM_001178167.1.
DR AlphaFoldDB; P31381; -.
DR SMR; P31381; -.
DR BioGRID; 31744; 55.
DR DIP; DIP-5495N; -.
DR IntAct; P31381; 6.
DR MINT; P31381; -.
DR STRING; 4932.YAL022C; -.
DR TCDB; 2.A.57.3.1; the equilibrative nucleoside transporter (ent) family.
DR iPTMnet; P31381; -.
DR MaxQB; P31381; -.
DR PaxDb; P31381; -.
DR PRIDE; P31381; -.
DR EnsemblFungi; YAL022C_mRNA; YAL022C; YAL022C.
DR GeneID; 851211; -.
DR KEGG; sce:YAL022C; -.
DR SGD; S000000020; FUN26.
DR VEuPathDB; FungiDB:YAL022C; -.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_3_0_1; -.
DR InParanoid; P31381; -.
DR OMA; FWNLGDL; -.
DR BioCyc; YEAST:G3O-28834-MON; -.
DR Reactome; R-SCE-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-SCE-9748787; Azathioprine ADME.
DR PRO; PR:P31381; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31381; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0034257; F:nicotinamide riboside transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:SGD.
DR GO; GO:0034258; P:nicotinamide riboside transport; IMP:SGD.
DR GO; GO:0015851; P:nucleobase transport; IDA:SGD.
DR GO; GO:0015858; P:nucleoside transport; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR InterPro; IPR034764; ENT1/ENT2.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00939; 2a57; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..517
FT /note="Nucleoside transporter FUN26"
FT /id="PRO_0000209346"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 517 AA; 58317 MW; 43C92A3E9A3D8D50 CRC64;
MSTSADTDTI KKPILAVPEP ALADTHSEEI SRSGEEHESE NNEHSDEEGD NYSEREQSVS
TEPLDTLPLR KKLKNLSYIT FFAIGIGLLW PWNCILSASQ YFKHDIFKDT SIWAKIFTSS
MMSFSTISSM LFNIYLAKRQ YKYSRRVING LVWEIIVFTV MCFFTILHFL LPKWFNFMFI
MMLVVISSMG TAMTQNGIMA IANVFGSEYS QGVMVGQAVA GVLPSLVLFA LAFIENSSVS
TTGGILLYFF TTTLVVTICV VMFSVSKISR KVNENWNVED GHITDVLLGS LRSNEEEIRI
VGRIDQMEDE DHRRTNGTRD DNDEGEELQL KVPFEVLFAK LKYLVLSIFT TFVVTLVFPV
FASATYVTGL PLSNAQYIPL IFTLWNLGDL YGRVIADWPM FRDQKFTPRK TFIYSLLRVA
AIPLFLMFTA ITSSSSGDEE HNGSVIVDLC YMLLQFLFGV TNGHVISMSF MKVPEQLDND
DEKEAAGGFT NIFVSTGLAL GSIISYVFVF IIDFIIR