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AZR1_YEAST
ID   AZR1_YEAST              Reviewed;         613 AA.
AC   P50080; D6VV06;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Azole resistance protein 1;
GN   Name=AZR1; OrderedLocusNames=YGR224W; ORFNames=G8537;
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=8701610;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA   van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT   "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT   region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 12:385-390(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11113970;
RX   DOI=10.1002/1097-0061(200012)16:16<1469::aid-yea640>3.0.co;2-a;
RA   Tenreiro S., Rosa P.C., Viegas C.A., Sa-Correia I.;
RT   "Expression of the AZR1 gene (ORF YGR224w), encoding a plasma membrane
RT   transporter of the major facilitator superfamily, is required for
RT   adaptation to acetic acid and resistance to azoles in Saccharomyces
RT   cerevisiae.";
RL   Yeast 16:1469-1481(2000).
RN   [5]
RP   INDUCTION.
RX   PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA   Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT   "A general strategy to uncover transcription factor properties identifies a
RT   new regulator of drug resistance in yeast.";
RL   J. Biol. Chem. 278:11427-11432(2003).
RN   [6]
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: Transporter protein required for adaptation to high stress
CC       imposed by low-chain organic acids, in particular by acetic acid, and
CC       for resistance to azoles, especially to ketoconazole and fluconazole.
CC       {ECO:0000269|PubMed:11113970}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11113970};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11113970}.
CC   -!- INDUCTION: Transcriptionally regulated by PDR8.
CC       {ECO:0000269|PubMed:12529331}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; X87941; CAA61172.1; -; Genomic_DNA.
DR   EMBL; Z73009; CAA97252.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08317.1; -; Genomic_DNA.
DR   PIR; S57687; S57687.
DR   RefSeq; NP_011740.3; NM_001181353.3.
DR   AlphaFoldDB; P50080; -.
DR   BioGRID; 33477; 83.
DR   DIP; DIP-7543N; -.
DR   IntAct; P50080; 2.
DR   STRING; 4932.YGR224W; -.
DR   TCDB; 2.A.1.3.53; the major facilitator superfamily (mfs).
DR   CarbonylDB; P50080; -.
DR   PaxDb; P50080; -.
DR   PRIDE; P50080; -.
DR   EnsemblFungi; YGR224W_mRNA; YGR224W; YGR224W.
DR   GeneID; 853139; -.
DR   KEGG; sce:YGR224W; -.
DR   SGD; S000003456; AZR1.
DR   VEuPathDB; FungiDB:YGR224W; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000176547; -.
DR   HOGENOM; CLU_000960_22_1_1; -.
DR   InParanoid; P50080; -.
DR   OMA; HLTWRWA; -.
DR   BioCyc; YEAST:G3O-30905-MON; -.
DR   PRO; PR:P50080; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P50080; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:1901474; F:azole transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0045117; P:azole transmembrane transport; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 2.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..613
FT                   /note="Azole resistance protein 1"
FT                   /id="PRO_0000173426"
FT   TOPO_DOM        1..70
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..134
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..375
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        465..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..581
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        603..613
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  67169 MW;  CF65C211E81D3FFF CRC64;
     MKGEPKTYSM SDLSYYGEKA QQQNEKQQKQ YVVRRNSTQS TSKQNVSVVL EDNASESNEL
     PKGFILYASL IALALSLFLA ALDIMIVSTI IEEVAKQFGS YSEIGWLFTG YSLPNALLAL
     IWGRIATPIG FKETMLFAIV IFEIGSLISA LANSMSMLIG GRVIAGVGGC GIQSLSFVIG
     STLVEESQRG ILIAVLSCSF AIASVVGPFL GGVFTSSVTW RWCFYVNLPI GGLAFFLFLF
     FYNPGLSTFQ ETMDNIRKFP SQFIEIVRNV AYHLLKIKGF SKLNGWRKPF MELIFMYDII
     EFVFCSAGFT CILLAFTFGG NRYAWNSASI IILFIIGIVL VVLAGIYDFL VFPKFNIVKA
     TPHYQPLMSW TNIKKPGIFT VNIALFLTCA GYISQFTYIV QYFQLIYNDS AWRAAVHLVA
     CIISTVVTAI LCGAITDKTR QIKPIIVISS IFGVVGAGIL TLLNNNANNS AHIGLLILPG
     VAFGGLAQSS MLASQIQLDK KSPTFRSDFV SITTFNTFCK NLGQALGGVI SNTVFSAAAI
     KKLTKANIQL PDGTTVDNLV IYRQTNFDGS HSKLGNIISE SLTDVFYMAL GFYALSLIFA
     VFASNKKVTA SLR
 
 
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