VMR1_YEAST
ID VMR1_YEAST Reviewed; 1592 AA.
AC P38735; D3DKT3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=ABC transporter ATP-binding protein/permease VMR1;
DE AltName: Full=Vacuolar multidrug resistance protein 1;
GN Name=VMR1; OrderedLocusNames=YHL035C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP PROTEIN FAMILY.
RX PubMed=9020838; DOI=10.1038/ng0297-137;
RA Decottignies A., Goffeau A.;
RT "Complete inventory of the yeast ABC proteins.";
RL Nat. Genet. 15:137-145(1997).
RN [4]
RP INDUCTION.
RX PubMed=12756250; DOI=10.1074/jbc.m300076200;
RA Rutherford J.C., Jaron S., Winge D.R.;
RT "Aft1p and Aft2p mediate iron-responsive gene expression in yeast through
RT related promoter elements.";
RL J. Biol. Chem. 278:27636-27643(2003).
RN [5]
RP INDUCTION.
RX PubMed=15886332; DOI=10.1152/physiolgenomics.00055.2005;
RA van Bakel H., Strengman E., Wijmenga C., Holstege F.C.P.;
RT "Gene expression profiling and phenotype analyses of S. cerevisiae in
RT response to changing copper reveals six genes with new roles in copper and
RT iron metabolism.";
RL Physiol. Genomics 22:356-367(2005).
RN [6]
RP INDUCTION.
RX PubMed=15942929; DOI=10.1002/yea.1231;
RA Lahue E., Heckathorn J., Meyer Z., Smith J., Wolfe C.;
RT "The Saccharomyces cerevisiae Sub2 protein suppresses heterochromatic
RT silencing at telomeres and subtelomeric genes.";
RL Yeast 22:537-551(2005).
CC -!- SUBUNIT: ABC transporter which may be involved in multidrug resistance.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Under the control of the iron homeostasis regulating AFT1
CC and AFT2 transcription factors. Up-regulated upon SUB2 overexpression.
CC {ECO:0000269|PubMed:12756250, ECO:0000269|PubMed:15886332,
CC ECO:0000269|PubMed:15942929}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U11583; AAB65047.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06650.1; -; Genomic_DNA.
DR PIR; S48933; S48933.
DR RefSeq; NP_011828.1; NM_001179115.1.
DR AlphaFoldDB; P38735; -.
DR SMR; P38735; -.
DR BioGRID; 36387; 29.
DR DIP; DIP-6477N; -.
DR IntAct; P38735; 5.
DR MINT; P38735; -.
DR STRING; 4932.YHL035C; -.
DR MaxQB; P38735; -.
DR PaxDb; P38735; -.
DR PRIDE; P38735; -.
DR EnsemblFungi; YHL035C_mRNA; YHL035C; YHL035C.
DR GeneID; 856350; -.
DR KEGG; sce:YHL035C; -.
DR SGD; S000001027; VMR1.
DR VEuPathDB; FungiDB:YHL035C; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000176323; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; P38735; -.
DR OMA; EEGWLKC; -.
DR BioCyc; YEAST:G3O-31054-MON; -.
DR Reactome; R-SCE-189483; Heme degradation.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-9749641; Aspirin ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR Reactome; R-SCE-9754706; Atorvastatin ADME.
DR PRO; PR:P38735; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38735; 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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISA: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:0010038; P:response to metal ion; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:SGD.
DR Gene3D; 1.20.1560.10; -; 2.
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 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 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..1592
FT /note="ABC transporter ATP-binding protein/permease VMR1"
FT /id="PRO_0000093465"
FT TOPO_DOM 1..33
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 96..100
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 122..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 153..170
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 192..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..350
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 351..379
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 380..400
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 401..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 466..486
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 487..489
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 490..510
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 511..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 573..593
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 594..614
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 615..635
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 636..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 990..1010
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1011..1051
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 1052..1072
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1073..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1116..1136
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1137
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 1138..1158
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1159..1229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1230..1250
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1251..1252
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 1253..1273
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1274..1592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 338..632
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 664..908
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 981..1282
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1323..1572
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 702..709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1357..1364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1592 AA; 180926 MW; 055FB0399992ACE8 CRC64;
MGTDPLIIRN NGSFWEVDDF TRLGRTQLLS YYLPLAIIAS IGIFALCRSG LSRYVRSAEC
DLVNEYLFGA QEERKEDNSI ERLLRNSNTQ ANYVNVKKQG RILKLRHFDI TTIDVKQIDA
KNHGGLTFSR PSTSDHLRKS SEIVLMSLQI IGLSFLRVTK INIELTNRDV TTLLLFWLIL
LSLSILRVYK RSTNLWAICF TAHTTIWIST WIPIRSVYIG NIDDVPSQIF YIFEFVITST
LQPIKLTSPI KDNSSIIYVR DDHTSPSREH ISSILSCITW SWITNFIWEA QKNTIKLKDI
WGLSMEDYSI FILKGFTRRN KHINNLTLAL FESFKTYLLI GMLWVLVNSI VNLLPTILMK
RFLEIVDNPN RSSSCMNLAW LYIIGMFICR LTLAICNSQG QFVSDKICLR IRAILIGEIY
AKGLRRRLFT SPKTSSDSDS ISANLGTIIN LISIDSFKVS ELANYLYVTV QAVIMIIVVV
GLLFNFLGVS AFAGISIILV MFPLNFLLAN LLGKFQKQTL KCTDQRISKL NECLQNIRIV
KYFAWERNII NEIKSIRQKE LRSLLKKSLV WSVTSFLWFV TPTLVTGVTF AICTFVQHED
LNAPLAFTTL SLFTLLKTPL DQLSNMLSFI NQSKVSLKRI SDFLRMDDTE KYNQLTISPD
KNKIEFKNAT LTWNENDSDM NAFKLCGLNI KFQIGKLNLI LGSTGSGKSA LLLGLLGELN
LISGSIIVPS LEPKHDLIPD CEGLTNSFAY CSQSAWLLND TVKNNIIFDN FYNEDRYNKV
IDACGLKRDL EILPAGDLTE IGEKGITLSG GQKQRISLAR AVYSSAKHVL LDDCLSAVDS
HTAVWIYENC ITGPLMKNRT CILVTHNVSL TLRNAHFAIV LENGKVKNQG TITELQSKGL
FKEKYVQLSS RDSINEKNAN RLKAPRKNDS QKIEPVTENI NFDANFVNDG QLIEEEEKSN
GAISPDVYKW YLKFFGGFKA LTALFALYIT AQILFISQSW WIRHWVNDTN VRINAPGFAM
DTLPLKGMTD SSKNKHNAFY YLTVYFLIGI IQAMLGGFKT MMTFLSGMRA SRKIFNNLLD
LVLHAQIRFF DVTPVGRIMN RFSKDIEGVD QELIPYLEVT IFCLIQCASI IFLITVITPR
FLTVAVIVFV LYFFVGKWYL TASRELKRLD SITKSPIFQH FSETLVGVCT IRAFGDERRF
ILENMNKIDQ NNRAFFYLSV TVKWFSFRVD MIGAFIVLAS GSFILLNIAN IDSGLAGISL
TYAILFTDGA LWLVRLYSTF EMNMNSVERL KEYSSIEQEN YLGHDEGRIL LLNEPSWPKD
GEIEIENLSL RYAPNLPPVI RNVSFKVDPQ SKIGIVGRTG AGKSTIITAL FRLLEPITGC
IKIDGQDISK IDLVTLRRSI TIIPQDPILF AGTIKSNVDP YDEYDEKKIF KALSQVNLIS
SHEFEEVLNS EERFNSTHNK FLNLHTEIAE GGLNLSQGER QLLFIARSLL REPKIILLDE
ATSSIDYDSD HLIQGIIRSE FNKSTILTIA HRLRSVIDYD RIIVMDAGEV KEYDRPSELL
KDERGIFYSM CRDSGGLELL KQIAKQSSKM MK
