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Alpha-factor-transporting ATPase (EC 3.6.3.48) (Mating factor A secretion protein STE6) (Multiple drug resistance protein homolog) (P-glycoprotein)

 STE6_YEAST              Reviewed;        1290 AA.
P12866; D6VWZ4;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
27-SEP-2017, entry version 175.
RecName: Full=Alpha-factor-transporting ATPase;
EC=3.6.3.48;
AltName: Full=Mating factor A secretion protein STE6;
AltName: Full=Multiple drug resistance protein homolog;
AltName: Full=P-glycoprotein;
Name=STE6; OrderedLocusNames=YKL209C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=2569166; DOI=10.1038/340400a0;
McGrath J.P., Varshavsky A.;
"The yeast STE6 gene encodes a homologue of the mammalian multidrug
resistance P-glycoprotein.";
Nature 340:400-404(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2686977;
Kuchler K., Sterne R.E., Thorner J.W.;
"Saccharomyces cerevisiae STE6 gene product: a novel pathway for
protein export in eukaryotic cells.";
EMBO J. 8:3973-3984(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
PubMed=3517872; DOI=10.1073/pnas.83.8.2536;
Wilson K.L., Herskowitz I.;
"Sequences upstream of the STE6 gene required for its expression and
regulation by the mating type locus in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 83:2536-2540(1986).
[6]
MUTAGENESIS.
PubMed=1935899;
Berkover C., Michaelis S.;
"Mutational analysis of the yeast a-factor transporter STE6, a member
of the ATP binding cassette (ABC) protein superfamily.";
EMBO J. 10:3777-3785(1991).
[7]
DEGRADATION BY UBIQUITINATION.
PubMed=8045256;
Koelling R., Hollenberg C.;
"The ABC-transporter Ste6 accumulates in the plasma membrane in a
ubiquitinated form in endocytosis mutants.";
EMBO J. 13:3261-3271(1994).
[8]
TOPOLOGY.
PubMed=8662764; DOI=10.1074/jbc.271.23.13746;
Geller D., Taglicht D., Edgar R., Tam A., Pines O., Michaelis S.,
Bibi E.;
"Comparative topology studies in Saccharomyces cerevisiae and in
Escherichia coli. The N-terminal half of the yeast ABC protein Ste6.";
J. Biol. Chem. 271:13746-13753(1996).
[9]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1022, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=SUB592;
PubMed=12872131; DOI=10.1038/nbt849;
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[10]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
-!- FUNCTION: STE6 is required in yeast MATA cells for production of
A-factor pheromone. STE6 is involved in the transport of the
farnesyl-derivation of the A-factor pheromone.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + alpha-factor(In) = ADP +
phosphate + alpha-factor(Out).
-!- INTERACTION:
P40318:SSM4; NbExp=2; IntAct=EBI-18383, EBI-18208;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- PTM: Degraded via the ubiquitin system.
{ECO:0000269|PubMed:8045256}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. Alpha-
factor sex pheromone exporter (TC 3.A.1.206) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15428; CAA33467.1; -; Genomic_DNA.
EMBL; M26376; AAA35116.1; -; Genomic_DNA.
EMBL; Z28209; CAA82054.1; -; Genomic_DNA.
EMBL; M12842; AAA35117.1; -; Genomic_DNA.
EMBL; BK006944; DAA08960.1; -; Genomic_DNA.
PIR; S05789; DVBYS6.
RefSeq; NP_012713.1; NM_001179774.1.
ProteinModelPortal; P12866; -.
BioGrid; 33956; 75.
DIP; DIP-2594N; -.
IntAct; P12866; 10.
MINT; MINT-427396; -.
STRING; 4932.YKL209C; -.
TCDB; 3.A.1.206.1; the atp-binding cassette (abc) superfamily.
iPTMnet; P12866; -.
MaxQB; P12866; -.
PRIDE; P12866; -.
EnsemblFungi; YKL209C; YKL209C; YKL209C.
GeneID; 853671; -.
KEGG; sce:YKL209C; -.
EuPathDB; FungiDB:YKL209C; -.
SGD; S000001692; STE6.
GeneTree; ENSGT00530000062896; -.
HOGENOM; HOG000093959; -.
InParanoid; P12866; -.
KO; K05658; -.
OMA; FVQAFWF; -.
OrthoDB; EOG092C02C4; -.
BioCyc; YEAST:G3O-31968-MONOMER; -.
BRENDA; 3.6.3.48; 984.
Reactome; R-SCE-159418; Recycling of bile acids and salts.
Reactome; R-SCE-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-SCE-382556; ABC-family proteins mediated transport.
PRO; PR:P12866; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015440; F:peptide-transporting ATPase activity; IDA:SGD.
GO; GO:0000770; P:peptide pheromone export; IMP:SGD.
GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR030246; Ste6/Hst6.
PANTHER; PTHR24223:SF264; PTHR24223:SF264; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Glycoprotein; Hydrolase;
Isopeptide bond; Membrane; Nucleotide-binding; Pheromone response;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 1290 Alpha-factor-transporting ATPase.
/FTId=PRO_0000093370.
TOPO_DOM 1 25 Cytoplasmic. {ECO:0000305}.
TRANSMEM 26 46 Helical. {ECO:0000305}.
TOPO_DOM 47 75 Extracellular. {ECO:0000305}.
TRANSMEM 76 96 Helical. {ECO:0000305}.
TOPO_DOM 97 150 Cytoplasmic. {ECO:0000305}.
TRANSMEM 151 171 Helical. {ECO:0000305}.
TOPO_DOM 172 173 Extracellular. {ECO:0000305}.
TRANSMEM 174 194 Helical. {ECO:0000305}.
TOPO_DOM 195 262 Cytoplasmic. {ECO:0000305}.
TRANSMEM 263 283 Helical. {ECO:0000305}.
TOPO_DOM 284 296 Extracellular. {ECO:0000305}.
TRANSMEM 297 317 Helical. {ECO:0000305}.
TOPO_DOM 318 715 Cytoplasmic. {ECO:0000305}.
TRANSMEM 716 736 Helical. {ECO:0000305}.
TOPO_DOM 737 763 Extracellular. {ECO:0000305}.
TRANSMEM 764 784 Helical. {ECO:0000305}.
TOPO_DOM 785 838 Cytoplasmic. {ECO:0000305}.
TRANSMEM 839 859 Helical. {ECO:0000305}.
TOPO_DOM 860 865 Extracellular. {ECO:0000305}.
TRANSMEM 866 886 Helical. {ECO:0000305}.
TOPO_DOM 887 945 Cytoplasmic. {ECO:0000305}.
TRANSMEM 946 966 Helical. {ECO:0000305}.
TOPO_DOM 967 981 Extracellular. {ECO:0000305}.
TRANSMEM 982 1002 Helical. {ECO:0000305}.
TOPO_DOM 1003 1290 Cytoplasmic. {ECO:0000305}.
DOMAIN 27 319 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 357 603 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 717 1007 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1052 1287 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 392 399 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1087 1094 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 1022 1022 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12872131}.
MUTAGEN 392 392 G->V: 0.8% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 398 398 K->A: 25% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 398 398 K->R: 1% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 509 509 G->D: 0.5% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 1087 1087 G->V: 0.3% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 1093 1093 K->A: 26% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 1093 1093 K->R: 15% mating activity.
{ECO:0000269|PubMed:1935899}.
MUTAGEN 1193 1193 G->D: 6% mating activity.
{ECO:0000269|PubMed:1935899}.
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


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