HOL1_YEAST
ID HOL1_YEAST Reviewed; 586 AA.
AC P53389; D6W1N0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein HOL1;
GN Name=HOL1; OrderedLocusNames=YNR055C; ORFNames=N3494;
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].
RX PubMed=8955402; DOI=10.1128/jb.178.24.7197-7205.1996;
RA Wright M.B., Howell E.A., Gaber R.F.;
RT "Amino acid substitutions in membrane-spanning domains of Hol1, a member of
RT the major facilitator superfamily of transporters, confer nonselective
RT cation uptake in Saccharomyces cerevisiae.";
RL J. Bacteriol. 178:7197-7205(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Seems to be involved in the uptake of several cations and of
CC histidinol.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {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; L42348; AAB47713.1; -; Genomic_DNA.
DR EMBL; Z71670; CAA96336.1; -; Genomic_DNA.
DR EMBL; Z71671; CAA96338.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10596.1; -; Genomic_DNA.
DR PIR; S63386; S63386.
DR RefSeq; NP_014453.3; NM_001183232.3.
DR AlphaFoldDB; P53389; -.
DR BioGRID; 35881; 87.
DR DIP; DIP-7266N; -.
DR IntAct; P53389; 1.
DR STRING; 4932.YNR055C; -.
DR TCDB; 2.A.1.2.33; the major facilitator superfamily (mfs).
DR CarbonylDB; P53389; -.
DR iPTMnet; P53389; -.
DR MaxQB; P53389; -.
DR PaxDb; P53389; -.
DR PRIDE; P53389; -.
DR EnsemblFungi; YNR055C_mRNA; YNR055C; YNR055C.
DR GeneID; 855792; -.
DR KEGG; sce:YNR055C; -.
DR SGD; S000005338; HOL1.
DR VEuPathDB; FungiDB:YNR055C; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_13_3_1; -.
DR InParanoid; P53389; -.
DR OMA; GWDWPVP; -.
DR BioCyc; YEAST:G3O-33361-MON; -.
DR PRO; PR:P53389; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53389; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015665; F:alcohol transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IMP:SGD.
DR GO; GO:0015850; P:organic hydroxy compound transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..586
FT /note="Protein HOL1"
FT /id="PRO_0000084026"
FT TOPO_DOM 1..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..544
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 510
FT /note="L -> F (in Ref. 1; AAB47713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 65348 MW; BEB6415256C3600F CRC64;
MDKYTNRDHP DYIPGTFNIY SSQNLENGII YESKLKKTSS GVVLIPQPSY SPNDPLNWSS
WRKLAHFGLM AFITAFTAAT SNDAGAAQDS LNEIYGISYD SMNTGAGVLF LGIGWSTLFL
APFANLYGRK ITYIVCTTLG LFGALWFALA KRTSDTIWSQ LFVGISESCA EAQVQLSLSD
IFFQHQLGSV LTVYIMCTSI GTFLGPLIAG YISAFTNFRW VGWVAVIISG GLLITIIFGC
EETYFDRGQY MTPLTSCQSG YEDGTTLQNS DNTAVSRRKR HLDAKLSTPG AMGEKGVDLS
ETAEFEVNNE EEVTIPETRE LIDGSKEHLK PYPKRVAILT KATNLKGYGF KQYFKYLKIN
LRMFLFPPVW LSGMFWGIQD VFLTFYLTTQ ESAYYEPPWN YSDFGVAIMN VPTLIGAVIG
CICAGIVSDY FVLWMARHNR GILEAEFRLY FSIATAIIGP AGLLMFGIGT ARQWPWQAIY
VGLGFVGFAW GCSGDIAMAY LMDCYPDMVL EGMVCTAIIN NTISCIFTFT CSDWLAASGT
ENTYIALAVI NFGITAFALP MYYYGKRIRL WTKRWYLQSV NLRDGV
