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Reviewed, UniProtKB/Swiss-Prot P38735 (VMR1_YEAST)

Last modified November 24, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ABC transporter ATP-binding protein/permease VMR1
Alternative name(s):
    Vacuolar multidrug resistance protein 1
Gene names
Name: VMR1
Ordered Locus Names: YHL035C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Subunit structure

ABC transporter which may be involved in multidrug resistance By similarity.

Subcellular location

Vacuole membrane; Multi-pass membrane protein Probable.

Induction

Under the controle of the iron homeostasis regulating AFT1 and AFT2 transcription factors. Up-regulated upon SUB2 overexpression. Ref.3 Ref.4 Ref.5

Sequence similarities

Belongs to the ABC transporter superfamily.

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
Vacuole
   DomainRepeat
Transmembrane
   LigandATP-binding
Nucleotide-binding
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtransmembrane transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay. Source: SGD

vacuole

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of substances

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15921592ABC transporter ATP-binding protein/permease VMR1
PRO_0000093465

Regions

Topological domain1 – 3333Vacuolar By similarity
Transmembrane34 – 54211 By similarity
Topological domain55 – 7420Cytoplasmic By similarity
Transmembrane75 – 95212 By similarity
Topological domain96 – 1005Vacuolar By similarity
Transmembrane101 – 121213 By similarity
Topological domain122 – 13110Cytoplasmic By similarity
Transmembrane132 – 152214 By similarity
Topological domain153 – 17018Vacuolar By similarity
Transmembrane171 – 191215 By similarity
Topological domain192 – 329138Cytoplasmic By similarity
Transmembrane330 – 350216 By similarity
Topological domain351 – 37929Vacuolar By similarity
Transmembrane380 – 400217 By similarity
Topological domain401 – 46565Cytoplasmic By similarity
Transmembrane466 – 486218 By similarity
Topological domain487 – 4893Vacuolar By similarity
Transmembrane490 – 510219 By similarity
Topological domain511 – 57262Cytoplasmic By similarity
Transmembrane573 – 5932110 By similarity
Topological domain594 – 61421Vacuolar By similarity
Transmembrane615 – 6352111 By similarity
Topological domain636 – 989354Cytoplasmic By similarity
Transmembrane990 – 10102112 By similarity
Topological domain1011 – 105141Vacuolar By similarity
Transmembrane1052 – 10722113 By similarity
Topological domain1073 – 111543Cytoplasmic By similarity
Transmembrane1116 – 11362114 By similarity
Topological domain11371Vacuolar By similarity
Transmembrane1138 – 11582115 By similarity
Topological domain1159 – 122971Cytoplasmic By similarity
Transmembrane1230 – 12502116 By similarity
Topological domain1251 – 12522Vacuolar By similarity
Transmembrane1253 – 12732117 By similarity
Topological domain1274 – 1592319Cytoplasmic By similarity
Domain338 – 632295ABC transmembrane type-1 1
Domain664 – 908245ABC transporter 1
Domain981 – 1282302ABC transmembrane type-1 2
Domain1323 – 1572250ABC transporter 2
Nucleotide binding702 – 7098ATP 1 Potential
Nucleotide binding1357 – 13648ATP 2 Potential

Amino acid modifications

Glycosylation111N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P38735-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 055FB0399992ACE8

FASTA1,592180,926
        10         20         30         40         50         60 
MGTDPLIIRN NGSFWEVDDF TRLGRTQLLS YYLPLAIIAS IGIFALCRSG LSRYVRSAEC 

        70         80         90        100        110        120 
DLVNEYLFGA QEERKEDNSI ERLLRNSNTQ ANYVNVKKQG RILKLRHFDI TTIDVKQIDA 

       130        140        150        160        170        180 
KNHGGLTFSR PSTSDHLRKS SEIVLMSLQI IGLSFLRVTK INIELTNRDV TTLLLFWLIL 

       190        200        210        220        230        240 
LSLSILRVYK RSTNLWAICF TAHTTIWIST WIPIRSVYIG NIDDVPSQIF YIFEFVITST 

       250        260        270        280        290        300 
LQPIKLTSPI KDNSSIIYVR DDHTSPSREH ISSILSCITW SWITNFIWEA QKNTIKLKDI 

       310        320        330        340        350        360 
WGLSMEDYSI FILKGFTRRN KHINNLTLAL FESFKTYLLI GMLWVLVNSI VNLLPTILMK 

       370        380        390        400        410        420 
RFLEIVDNPN RSSSCMNLAW LYIIGMFICR LTLAICNSQG QFVSDKICLR IRAILIGEIY 

       430        440        450        460        470        480 
AKGLRRRLFT SPKTSSDSDS ISANLGTIIN LISIDSFKVS ELANYLYVTV QAVIMIIVVV 

       490        500        510        520        530        540 
GLLFNFLGVS AFAGISIILV MFPLNFLLAN LLGKFQKQTL KCTDQRISKL NECLQNIRIV 

       550        560        570        580        590        600 
KYFAWERNII NEIKSIRQKE LRSLLKKSLV WSVTSFLWFV TPTLVTGVTF AICTFVQHED 

       610        620        630        640        650        660 
LNAPLAFTTL SLFTLLKTPL DQLSNMLSFI NQSKVSLKRI SDFLRMDDTE KYNQLTISPD 

       670        680        690        700        710        720 
KNKIEFKNAT LTWNENDSDM NAFKLCGLNI KFQIGKLNLI LGSTGSGKSA LLLGLLGELN 

       730        740        750        760        770        780 
LISGSIIVPS LEPKHDLIPD CEGLTNSFAY CSQSAWLLND TVKNNIIFDN FYNEDRYNKV 

       790        800        810        820        830        840 
IDACGLKRDL EILPAGDLTE IGEKGITLSG GQKQRISLAR AVYSSAKHVL LDDCLSAVDS 

       850        860        870        880        890        900 
HTAVWIYENC ITGPLMKNRT CILVTHNVSL TLRNAHFAIV LENGKVKNQG TITELQSKGL 

       910        920        930        940        950        960 
FKEKYVQLSS RDSINEKNAN RLKAPRKNDS QKIEPVTENI NFDANFVNDG QLIEEEEKSN 

       970        980        990       1000       1010       1020 
GAISPDVYKW YLKFFGGFKA LTALFALYIT AQILFISQSW WIRHWVNDTN VRINAPGFAM 

      1030       1040       1050       1060       1070       1080 
DTLPLKGMTD SSKNKHNAFY YLTVYFLIGI IQAMLGGFKT MMTFLSGMRA SRKIFNNLLD 

      1090       1100       1110       1120       1130       1140 
LVLHAQIRFF DVTPVGRIMN RFSKDIEGVD QELIPYLEVT IFCLIQCASI IFLITVITPR 

      1150       1160       1170       1180       1190       1200 
FLTVAVIVFV LYFFVGKWYL TASRELKRLD SITKSPIFQH FSETLVGVCT IRAFGDERRF 

      1210       1220       1230       1240       1250       1260 
ILENMNKIDQ NNRAFFYLSV TVKWFSFRVD MIGAFIVLAS GSFILLNIAN IDSGLAGISL 

      1270       1280       1290       1300       1310       1320 
TYAILFTDGA LWLVRLYSTF EMNMNSVERL KEYSSIEQEN YLGHDEGRIL LLNEPSWPKD 

      1330       1340       1350       1360       1370       1380 
GEIEIENLSL RYAPNLPPVI RNVSFKVDPQ SKIGIVGRTG AGKSTIITAL FRLLEPITGC 

      1390       1400       1410       1420       1430       1440 
IKIDGQDISK IDLVTLRRSI TIIPQDPILF AGTIKSNVDP YDEYDEKKIF KALSQVNLIS 

      1450       1460       1470       1480       1490       1500 
SHEFEEVLNS EERFNSTHNK FLNLHTEIAE GGLNLSQGER QLLFIARSLL REPKIILLDE 

      1510       1520       1530       1540       1550       1560 
ATSSIDYDSD HLIQGIIRSE FNKSTILTIA HRLRSVIDYD RIIVMDAGEV KEYDRPSELL 

      1570       1580       1590 
KDERGIFYSM CRDSGGLELL KQIAKQSSKM MK 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Complete inventory of the yeast ABC proteins."
Decottignies A., Goffeau A.
Nat. Genet. 15:137-145(1997) [PubMed: 9020838] [Abstract]
Cited for: PROTEIN FAMILY.
[3]"Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements."
Rutherford J.C., Jaron S., Winge D.R.
J. Biol. Chem. 278:27636-27643(2003) [PubMed: 12756250] [Abstract]
Cited for: INDUCTION.
[4]"Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism."
van Bakel H., Strengman E., Wijmenga C., Holstege F.C.P.
Physiol. Genomics 22:356-367(2005) [PubMed: 15886332] [Abstract]
Cited for: INDUCTION.
[5]"The Saccharomyces cerevisiae Sub2 protein suppresses heterochromatic silencing at telomeres and subtelomeric genes."
Lahue E., Heckathorn J., Meyer Z., Smith J., Wolfe C.
Yeast 22:537-551(2005) [PubMed: 15942929] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

U11583 Genomic DNA. Translation: AAB65047.1.
PIRS48933.
RefSeqNP_011828.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6477N.
STRINGP38735.

Proteomic databases

PRIDEP38735.

Genome annotation databases

EnsemblYHL035C; YHL035C; YHL035C; Saccharomyces cerevisiae. [Genome view]
GeneID856350.
KEGGsce:YHL035C.
NMPDRfig|4932.3.peg.2964.

Organism-specific databases

CYGDYHL035c.
SGDS000001027. VMR1.

Phylogenomic databases

HOGENOMP38735.
OMALISSHEF
OrthoDBEOG9VMGZS

Gene expression databases

ArrayExpressP38735.
GenevestigatorP38735.
GermOnlineYHL035C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011527. ABC_TM_1.
IPR001140. ABC_TM_transpt.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR003593. ATPase_AAA+_core.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio981787.

Entry information

Entry nameVMR1_YEAST
AccessionPrimary (citable) accession number: P38735
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 24, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents