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MFS54_ALTAL
ID   MFS54_ALTAL             Reviewed;         538 AA.
AC   A0A4Q4NMP3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=MFS-type transporter MFS54 {ECO:0000303|PubMed:30279684};
GN   Name=MFS54 {ECO:0000303|PubMed:30279684}; ORFNames=AA0117_g3624;
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FERA 1177;
RX   PubMed=32038562; DOI=10.3389/fmicb.2019.03124;
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.R.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and asian pear pathotypes.";
RL   Front. Microbiol. 10:3124-3124(2019).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=30279684; DOI=10.3389/fmicb.2018.02229;
RA   Lin H.C., Yu P.L., Chen L.H., Tsai H.C., Chung K.R.;
RT   "A Major Facilitator Superfamily Transporter Regulated by the Stress-
RT   Responsive Transcription Factor Yap1 Is Required for Resistance to
RT   Fungicides, Xenobiotics, and Oxidants and Full Virulence in Alternaria
RT   alternata.";
RL   Front. Microbiol. 9:2229-2229(2018).
CC   -!- FUNCTION: MFS-type efflux pump involved in the modulation
CC       susceptibility to various compounds including the xenobiotics 2,3,5-
CC       triiodobenzoic acid (TIBA) and 2-chloro-5-hydroxypyridine (CHP),
CC       CuCl(2) several fungicides (clotrimazole, fludioxonil, vinclozolin, and
CC       iprodione), potassium superoxide KO(2), and the singlet oxygen-
CC       generating compound hematoporphyrin. {ECO:0000269|PubMed:30279684}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30279684};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is down-regulated in the presence of TIBA or CHP,
CC       and induced in the presence of H(2)O(2), clotrimazole, or vinclozolin
CC       (PubMed:30279684). Expression is regulated by the stress-responsive
CC       transcription regulator Yap1 but not the Hog1 MAP kinase
CC       (PubMed:30279684). {ECO:0000269|PubMed:30279684}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a decreased production of conidia and a
CC       reduced radial growth by about 20% on potato dextrose agar plates
CC       (PubMed:30279684). Leads also to increased sensitivity to the
CC       xenobiotics 2,3,5-triiodobenzoic acid (TIBA) and 2-chloro-5-
CC       hydroxypyridine (CHP), CuCl(2) and several fungicides including
CC       clotrimazole, fludioxonil, vinclozolin, and iprodione
CC       (PubMed:30279684). Increases also the sensitivity to potassium
CC       superoxide KO(2) and the singlet oxygen-generating compound
CC       hematoporphyrin (PubMed:30279684). Does not affect the sensitivity to
CC       H(2)O(2), singlet oxygen-generating compounds rose Bengal and eosin Y,
CC       or to the cell wall disturbing compound Congo red (PubMed:30279684).
CC       {ECO:0000269|PubMed:30279684}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; PDXD01000005; RYN79724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4NMP3; -.
DR   SMR; A0A4Q4NMP3; -.
DR   Proteomes; UP000291422; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..538
FT                   /note="MFS-type transporter MFS54"
FT                   /id="PRO_0000452753"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  57832 MW;  DB0C920D9C6234E1 CRC64;
     MKEGVVTPPD SEKDLQNVEG SLNTEEEKAE EAHIQLSKGR FVLVLVGLVL AIFLASLDFT
     IISTAIPKIT DEFHSLQDIG WYGSAFFITT AATTAHWGRL YTFFPLKWTY LTSIFFFELG
     SVICGAAPSS TALIIGRAIC GIGAAGLFSG SYTIIAVLVP SADRPKYSGL MGASYGLASV
     VGPLIGGAFT SHVSWRWCFY INLPVGGVSC LFILLFFANE PPKSRPDWRG MLRQLDMLGL
     VLIVGAITCF ILALQWGGVS KAWDSGAVIG TLVAFVVCMI LFVIEQWWLG ENAMVHSVMI
     KRRTIWVGSM FSFLINSAFL VTFYYLPIYF QSVQGVSAST SGVRTVPFIL AVTFCVVIVG
     QIITKTGYAF PWMIVGAAIT TIGSGMIYTF DTHSPAGKWI GYQILCGIGV GVSFQVPVML
     IQATTKDADV PLATATLLFI QTLGGAFGVS SAQAAFQNTL LKQLAITAPG LNPQIVLDAG
     ASELKRVIPE QFLQGVLEAY VSGFRECLIV GIAFGGAAFL AAFGFRFTNI KRTAAAEA
 
 
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