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ZRA1_GIBZE
ID   ZRA1_GIBZE              Reviewed;        1489 AA.
AC   I1RL06; A0A098DKY5;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=ZEB2-regulated ABC transporter 1 {ECO:0000303|PubMed:21833740};
GN   Name=ZRA1 {ECO:0000303|PubMed:21833740};
GN   ORFNames=FGRAMPH1_01T15627, FGSG_04580;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21833740; DOI=10.1007/s00294-011-0352-4;
RA   Lee S., Son H., Lee J., Lee Y.R., Lee Y.W.;
RT   "A putative ABC transporter gene, ZRA1, is required for zearalenone
RT   production in Gibberella zeae.";
RL   Curr. Genet. 57:343-351(2011).
CC   -!- FUNCTION: ABC transporter involved in zearalenone production
CC       (PubMed:21833740). {ECO:0000269|PubMed:21833740}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21833740};
CC       Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC       {ECO:0000269|PubMed:21833740}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the zearalenone
CC       biosynthesis specific transcription factor ZEB2 (PubMed:21833740).
CC       {ECO:0000269|PubMed:21833740}.
CC   -!- DISRUPTION PHENOTYPE: Results in the loss of zearalenone production
CC       (PubMed:21833740). {ECO:0000269|PubMed:21833740}.
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; DS231664; ESU08505.1; -; Genomic_DNA.
DR   EMBL; HG970333; CEF79613.1; -; Genomic_DNA.
DR   RefSeq; XP_011321004.1; XM_011322702.1.
DR   AlphaFoldDB; I1RL06; -.
DR   SMR; I1RL06; -.
DR   STRING; 229533.I1RL06; -.
DR   EnsemblFungi; ESU08505; ESU08505; FGSG_04580.
DR   GeneID; 23551821; -.
DR   KEGG; fgr:FGSG_04580; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G15627; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; I1RL06; -.
DR   PHI-base; PHI:3697; -.
DR   PHI-base; PHI:3925; -.
DR   Proteomes; UP000070720; Chromosome 2.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106150; P:zearalenone biosynthetic process; IMP:GO_Central.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF19055; ABC2_membrane_7; 2.
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   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Vacuole.
FT   CHAIN           1..1489
FT                   /note="ZEB2-regulated ABC transporter 1"
FT                   /id="PRO_0000438787"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        628..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        662..682
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        773..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1190..1210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1218..1238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1269..1289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1307..1327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1333..1353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1457..1477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          152..408
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          846..1088
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         882..889
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        714
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1489 AA;  165923 MW;  4B43320BB81B9954 CRC64;
     MALPEANMSS TRSEQSSRSH DTIVGNEQPH SEKPAASAPG DQMSSDDEDE GPQTEEMIRR
     HSIVRDLARN YTNTSHHFTG SSADLFNAAD ANSPLNPSSE NFNARAWARA MAKTMGENGS
     GFRQSGLCFQ DMNVFGYGAE TDYQKDVGNV WLGLPDMVHQ MISPNANKRR IDILRGFDGV
     INAGEMCVVL GPPGSGCSTF LKSISGETNG IYIDDSTYFN YNGIPAEEMH KSHAGETIYT
     AEVDIHFPML SVGDTLTFAA RARCPQNLPP GIDHNLYSEH MRDVVMAMYG ISHTINTQVG
     DNYIRGVSGG ERKRVTIAEA TLSNAPFQCW DNSTRGLDSA NAIEFCKTLR LQSELFGQTC
     AVSIYQAPQT AYDLFDKALV IYEGRQIFFG PADEAKAYFI NLGFECPDRQ TTPDFLTSMT
     APSERVVRPG WENKVPRTPD EFHARWKESQ QYQIVRAEIE SYKSLYPLNG SSADAFRENK
     HSAQAKGQRL KSPFTLSYMQ QVQLCLWRGF RRLLGSPGVT IFQLIANTAV AFIASSLFYN
     MKPETGDFFK RGATLFLAVL SNAFASALEI LTQYSQRPIV EKQARYAFYH PSAEAFASIL
     VDMPYKITNS ILFNVTLYFM TNLNRDAGAF FFFLLVSFIM VLAMSGVFRS IASLSRTLSQ
     AMVPASLLIL ALVIFAGFVV PVDYMLGWCR WINYLDPVAY GFESLMVNEF SGRNFTCTAF
     VPNAQIPGYA DVGGLNRACS TVGAIPGQSY VNGDAYINLE YKYFHAHKWR NVGILIAMTI
     FNHVVYIVAT EFISAKKSKG EVLVFRRSNM PSKAKSDPEA SSSRPIPTTE KNNNEVANIQ
     GSTSVFHWND VCYDIKIKGE PRRILDHVDG WVKPGTLTAL MGVSGAGKTT LLDCLADRIS
     MGVITGEMLV DGKIRDSSFQ RRTGYVQQQD LHLETSTVRE ALTFSALLRQ PASTPREEKI
     AYVDEVIKLL DMQEYADAVV GVLGEGLNVE QRKRLTIGVE LAAKPPLLLF VDEPTSGLDS
     QTSWAILDLL EKLSKAGQSI LCTIHQPSAM LFQRFDRLLF LAKGGRTIYF GDIGKNSETL
     TNYFVKHGSQ ECPNGENPAE WMLEVIGAAP GSHTDIDWHQ TWRDSSEYQA VQTELQRLKA
     EGSANSVDQK SDPESYREFA APFGQQLLIA TKRVFEQYWR TPSYIYSKAA LCIQVGLFLG
     LVFLNAPLSL RGLQNQMFAI FQMLTVFGQL VQMQMPHFVT QRSLYEVRER PSKTYSWKVF
     MLSQIIAEIP WNTLMSVFLF VCIYYPVGFN KNAEFAGQTA ERGGLMWLLI WQFLIFTCTF
     AHAAIAITDT AEAGGNLANV VFMMSLFFCG VLAAPDKMPG FWIWMYRVSP FTYLVSAILS
     TGIANAEVKC AANELTTFNP TNGTTCGEYM DSYIKAAGGY LTNPDATSDC KFCTIKSTNV
     YLKALSASYD DRWRNFGIGM VYIVVNIVGA LFLYWLIRMP KNKNKKKTA
 
 
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