SNQ2_YEAST
ID SNQ2_YEAST Reviewed; 1501 AA.
AC P32568; D6VRZ7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein SNQ2;
GN Name=SNQ2; OrderedLocusNames=YDR011W; ORFNames=YD8119.16;
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=8437567; DOI=10.1007/bf00277115;
RA Servos J., Haase E., Brendel M.;
RT "Gene SNQ2 of Saccharomyces cerevisiae, which confers resistance to 4-
RT nitroquinoline-N-oxide and other chemicals, encodes a 169 kDa protein
RT homologous to ATP-dependent permeases.";
RL Mol. Gen. Genet. 236:214-218(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1243-1247.
RX PubMed=7629127; DOI=10.1074/jbc.270.30.18150;
RA Decottignies A., Lambert L., Catty P., Degand H., Epping E.A.,
RA Moye-Rowley W.S., Balzi E., Goffeau A.;
RT "Identification and characterization of SNQ2, a new multidrug ATP binding
RT cassette transporter of the yeast plasma membrane.";
RL J. Biol. Chem. 270:18150-18157(1995).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-64; SER-80; SER-86
RP AND THR-1153, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-80 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-80 AND THR-1153, 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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Could be an ATP-dependent permease. Confers hyper-resistance
CC to the mutagens 4-nitroquinoline-N-oxide (4-NQO) and triaziquone, as
CC well as to the chemicals sulphomethuron methyl phenanthroline when
CC present in multiple copies. Exhibits nucleoside triphosphatase
CC activity.
CC -!- INTERACTION:
CC P32568; P36062: AVT3; NbExp=2; IntAct=EBI-17590, EBI-20799445;
CC P32568; P33302: PDR5; NbExp=4; IntAct=EBI-17590, EBI-13038;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; X66732; CAA47270.1; -; Genomic_DNA.
DR EMBL; X95966; CAA65203.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88071.1; -; Genomic_DNA.
DR EMBL; Z74307; CAA98831.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11857.1; -; Genomic_DNA.
DR PIR; S50992; S50992.
DR RefSeq; NP_010294.1; NM_001180319.1.
DR AlphaFoldDB; P32568; -.
DR SMR; P32568; -.
DR BioGRID; 32062; 113.
DR IntAct; P32568; 35.
DR MINT; P32568; -.
DR STRING; 4932.YDR011W; -.
DR TCDB; 3.A.1.205.2; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P32568; -.
DR MaxQB; P32568; -.
DR PaxDb; P32568; -.
DR PRIDE; P32568; -.
DR EnsemblFungi; YDR011W_mRNA; YDR011W; YDR011W.
DR GeneID; 851574; -.
DR KEGG; sce:YDR011W; -.
DR SGD; S000002418; SNQ2.
DR VEuPathDB; FungiDB:YDR011W; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176297; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P32568; -.
DR OMA; NGARRCE; -.
DR BioCyc; YEAST:G3O-29630-MON; -.
DR PRO; PR:P32568; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32568; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030003; P:cellular cation homeostasis; IMP:SGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00956; 3a01205; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Direct protein sequencing; Glycoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1501
FT /note="Protein SNQ2"
FT /id="PRO_0000093441"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1190..1212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1216..1236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1277..1296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1333..1352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1455..1475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 161..410
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 853..1095
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 889..896
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1153
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 78
FT /note="V -> E (in Ref. 1; CAA47270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1501 AA; 168767 MW; 96BE3D30CCFB76AC CRC64;
MSNIKSTQDS SHNAVARSSS ASFAASEESF TGITHDKDEQ SDTPADKLTK MLTGPARDTA
SQISATVSEM APDVVSKVES FADALSRHTT RSGAFNMDSD SDDGFDAHAI FESFVRDADE
QGIHIRKAGV TIEDVSAKGV DASALEGATF GNILCLPLTI FKGIKAKRHQ KMRQIISNVN
ALAEAGEMIL VLGRPGAGCS SFLKVTAGEI DQFAGGVSGE VAYDGIPQEE MMKRYKADVI
YNGELDVHFP YLTVKQTLDF AIACKTPALR VNNVSKKEYI ASRRDLYATI FGLRHTYNTK
VGNDFVRGVS GGERKRVSIA EALAAKGSIY CWDNATRGLD ASTALEYAKA IRIMTNLLKS
TAFVTIYQAS ENIYETFDKV TVLYSGKQIY FGLIHEAKPY FAKMGYLCPP RQATAEFLTA
LTDPNGFHLI KPGYENKVPR TAEEFETYWL NSPEFAQMKK DIAAYKEKVN TEKTKEVYDE
SMAQEKSKYT RKKSYYTVSY WEQVKLCTQR GFQRIYGNKS YTVINVCSAI IQSFITGSLF
YNTPSSTSGA FSRGGVLYFA LLYYSLMGLA NISFEHRPIL QKHKGYSLYH PSAEAIGSTL
ASFPFRMIGL TCFFIILFFL SGLHRTAGSF FTIYLFLTMC SEAINGLFEM VSSVCDTLSQ
ANSISGILMM SISMYSTYMI QLPSMHPWFK WISYVLPIRY AFESMLNAEF HGRHMDCANT
LVPSGGDYDN LSDDYKVCAF VGSKPGQSYV LGDDYLKNQF QYVYKHTWRN FGILWCFLLG
YVVLKVIFTE YKRPVKGGGD ALIFKKGSKR FIAHADEESP DNVNDIDAKE QFSSESSGAN
DEVFDDLEAK GVFIWKDVCF TIPYEGGKRM LLDNVSGYCI PGTMTALMGE SGAGKTTLLN
TLAQRNVGII TGDMLVNGRP IDASFERRTG YVQQQDIHIA ELTVRESLQF SARMRRPQHL
PDSEKMDYVE KIIRVLGMEE YAEALVGEVG CGLNVEQRKK LSIGVELVAK PDLLLFLDEP
TSGLDSQSSW AIIQLLRKLS KAGQSILCTI HQPSATLFEE FDRLLLLRKG GQTVYFGDIG
KNSATILNYF ERNGARKCDS SENPAEYILE AIGAGATASV KEDWHEKWLN SVEFEQTKEK
VQDLINDLSK QETKSEVGDK PSKYATSYAY QFRYVLIRTS TSFWRSLNYI MSKMMLMLVG
GLYIGFTFFN VGKSYVGLQN AMFAAFISII LSAPAMNQIQ GRAIASRELF EVRESQSNMF
HWSLVLITQY LSELPYHLFF STIFFVSSYF PLRIFFEASR SAVYFLNYCI MFQLYYVGLG
LMILYMSPNL PSANVILGLC LSFMLSFCGV TQPVSLMPGF WTFMWKASPY TYFVQNLVGI
MLHKKPVVCK KKELNYFNPP NGSTCGEYMK PFLEKATGYI ENPDATSDCA YCIYEVGDNY
LTHISSKYSY LWRNFGIFWI YIFFNIIAMV CVYYLFHVRQ SSFLSPVSIL NKIKNIRKKK
Q
