STE6_YEAST
ID STE6_YEAST Reviewed; 1290 AA.
AC P12866; D6VWZ4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Alpha-factor-transporting ATPase;
DE EC=7.4.2.7;
DE AltName: Full=Mating factor A secretion protein STE6;
DE AltName: Full=Multiple drug resistance protein homolog;
DE AltName: Full=P-glycoprotein;
GN Name=STE6; OrderedLocusNames=YKL209C;
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 204508 / S288c;
RX PubMed=2569166; DOI=10.1038/340400a0;
RA McGrath J.P., Varshavsky A.;
RT "The yeast STE6 gene encodes a homologue of the mammalian multidrug
RT resistance P-glycoprotein.";
RL Nature 340:400-404(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2686977; DOI=10.1002/j.1460-2075.1989.tb08580.x;
RA Kuchler K., Sterne R.E., Thorner J.W.;
RT "Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein
RT export in eukaryotic cells.";
RL EMBO J. 8:3973-3984(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RX PubMed=3517872; DOI=10.1073/pnas.83.8.2536;
RA Wilson K.L., Herskowitz I.;
RT "Sequences upstream of the STE6 gene required for its expression and
RT regulation by the mating type locus in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2536-2540(1986).
RN [6]
RP MUTAGENESIS.
RX PubMed=1935899; DOI=10.1002/j.1460-2075.1991.tb04947.x;
RA Berkover C., Michaelis S.;
RT "Mutational analysis of the yeast a-factor transporter STE6, a member of
RT the ATP binding cassette (ABC) protein superfamily.";
RL EMBO J. 10:3777-3785(1991).
RN [7]
RP DEGRADATION BY UBIQUITINATION.
RX PubMed=8045256; DOI=10.1002/j.1460-2075.1994.tb06627.x;
RA Koelling R., Hollenberg C.;
RT "The ABC-transporter Ste6 accumulates in the plasma membrane in a
RT ubiquitinated form in endocytosis mutants.";
RL EMBO J. 13:3261-3271(1994).
RN [8]
RP TOPOLOGY.
RX PubMed=8662764; DOI=10.1074/jbc.271.23.13746;
RA Geller D., Taglicht D., Edgar R., Tam A., Pines O., Michaelis S., Bibi E.;
RT "Comparative topology studies in Saccharomyces cerevisiae and in
RT Escherichia coli. The N-terminal half of the yeast ABC protein Ste6.";
RL J. Biol. Chem. 271:13746-13753(1996).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [10]
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: STE6 is required in yeast MATA cells for production of A-
CC factor pheromone. STE6 is involved in the transport of the farnesyl-
CC derivation of the A-factor pheromone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [alpha-factor](in) + ATP + H2O = ADP + an [alpha-
CC factor](out) + H(+) + phosphate; Xref=Rhea:RHEA:10848, Rhea:RHEA-
CC COMP:11611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.7;
CC -!- INTERACTION:
CC P12866; P40318: SSM4; NbExp=3; IntAct=EBI-18383, EBI-18208;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Degraded via the ubiquitin system. {ECO:0000269|PubMed:8045256}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Alpha-factor
CC sex pheromone exporter (TC 3.A.1.206) family. {ECO:0000305}.
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DR EMBL; X15428; CAA33467.1; -; Genomic_DNA.
DR EMBL; M26376; AAA35116.1; -; Genomic_DNA.
DR EMBL; Z28209; CAA82054.1; -; Genomic_DNA.
DR EMBL; M12842; AAA35117.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08960.1; -; Genomic_DNA.
DR PIR; S05789; DVBYS6.
DR RefSeq; NP_012713.1; NM_001179774.1.
DR AlphaFoldDB; P12866; -.
DR SMR; P12866; -.
DR BioGRID; 33956; 125.
DR DIP; DIP-2594N; -.
DR IntAct; P12866; 10.
DR MINT; P12866; -.
DR STRING; 4932.YKL209C; -.
DR TCDB; 3.A.1.206.1; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P12866; -.
DR MaxQB; P12866; -.
DR PaxDb; P12866; -.
DR PRIDE; P12866; -.
DR EnsemblFungi; YKL209C_mRNA; YKL209C; YKL209C.
DR GeneID; 853671; -.
DR KEGG; sce:YKL209C; -.
DR SGD; S000001692; STE6.
DR VEuPathDB; FungiDB:YKL209C; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; P12866; -.
DR OMA; QNGEDMR; -.
DR BioCyc; YEAST:G3O-31968-MON; -.
DR BRENDA; 7.4.2.7; 984.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-9748787; Azathioprine ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR PRO; PR:P12866; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P12866; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000770; P:peptide pheromone export; IMP:SGD.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030246; Ste6/Hst6.
DR PANTHER; PTHR24223:SF372; PTHR24223:SF372; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Isopeptide bond; Membrane; Nucleotide-binding;
KW Pheromone response; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..1290
FT /note="Alpha-factor-transporting ATPase"
FT /id="PRO_0000093370"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 47..75
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 97..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 172..173
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 195..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 284..296
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 318..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 737..763
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 764..784
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 785..838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 860..865
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 887..945
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 967..981
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 1003..1290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..319
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 357..603
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 717..1007
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1052..1287
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 392..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1087..1094
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 1022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT MUTAGEN 392
FT /note="G->V: 0.8% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 398
FT /note="K->A: 25% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 398
FT /note="K->R: 1% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 509
FT /note="G->D: 0.5% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 1087
FT /note="G->V: 0.3% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 1093
FT /note="K->A: 26% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 1093
FT /note="K->R: 15% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
FT MUTAGEN 1193
FT /note="G->D: 6% mating activity."
FT /evidence="ECO:0000269|PubMed:1935899"
SQ SEQUENCE 1290 AA; 144766 MW; B240B7E51D9680D5 CRC64;
MNFLSFKTTK HYHIFRYVNI RNDYRLLMIM IIGTVATGLV PAITSILTGR VFDLLSVFVA
NGSHQGLYSQ LVQRSMAVMA LGAASVPVMW LSLTSWMHIG ERQGFRIRSQ ILEAYLEEKP
MEWYDNNEKL LGDFTQINRC VEELRSSSAE ASAITFQNLV AICALLGTSF YYSWSLTLII
LCSSPIITFF AVVFSRMIHV YSEKENSETS KAAQLLTWSM NAAQLVRLYC TQRLERKKFK
EIILNCNTFF IKSCFFVAAN AGILRFLTLT MFVQGFWFGS AMIKKGKLNI NDVITCFHSC
IMLGSTLNNT LHQIVVLQKG GVAMEKIMTL LKDGSKRNPL NKTVAHQFPL DYATSDLTFA
NVSFSYPSRP SEAVLKNVSL NFSAGQFTFI VGKSGSGKST LSNLLLRFYD GYNGSISING
HNIQTIDQKL LIENITVVEQ RCTLFNDTLR KNILLGSTDS VRNADCSTNE NRHLIKDACQ
MALLDRFILD LPDGLETLIG TGGVTLSGGQ QQRVAIARAF IRDTPILFLD EAVSALDIVH
RNLLMKAIRH WRKGKTTIIL THELSQIESD DYLYLMKEGE VVESGTQSEL LADPTTTFST
WYHLQNDYSD AKTIVDTETE EKSIHTVESF NSQLETPKLG SCLSNLGYDE TDQLSFYEAI
YQKRSNVRTR RVKVEEENIG YALKQQKNTE SSTGPQLLSI IQIIKRMIKS IRYKKILILG
LLCSLIAGAT NPVFSYTFSF LLEGIVPSTD GKTGSSHYLA KWSLLVLGVA AADGIFNFAK
GFLLDCCSEY WVMDLRNEVM EKLTRKNMDW FSGENNKASE ISALVLNDLR DLRSLVSEFL
SAMTSFVTVS TIGLIWALVS GWKLSLVCIS MFPLIIIFSA IYGGILQKCE TDYKTSVAQL
ENCLYQIVTN IKTIKCLQAE FHFQLTYHDL KIKMQQIASK RAIATGFGIS MTNMIVMCIQ
AIIYYYGLKL VMIHEYTSKE MFTTFTLLLF TIMSCTSLVS QIPDISRGQR AASWIYRILD
EKHNTLEVEN NNARTVGIAG HTYHGKEKKP IVSIQNLTFA YPSAPTAFVY KNMNFDMFCG
QTLGIIGESG TGKSTLVLLL TKLYNCEVGK IKIDGTDVND WNLTSLRKEI SVVEQKPLLF
NGTIRDNLTY GLQDEILEIE MYDALKYVGI HDFVISSPQG LDTRIDTTLL SGGQAQRLCI
ARALLRKSKI LILDECTSAL DSVSSSIINE IVKKGPPALL TMVITHSEQM MRSCNSIAVL
KDGKVVERGN FDTLYNNRGE LFQIVSNQSS
