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ATRC_EMENI
ID   ATRC_EMENI              Reviewed;        1284 AA.
AC   A0A1U8QG99; C8VNF2; Q5BAT1;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=ABC multidrug transporter atrC;
GN   Name=atrC {ECO:0000303|PubMed:10954082}; ORFNames=AN2349;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10954082; DOI=10.1007/pl00008697;
RA   Andrade A.C., Van Nistelrooy J.G., Peery R.B., Skatrud P.L., De Waard M.A.;
RT   "The role of ABC transporters from Aspergillus nidulans in protection
RT   against cytotoxic agents and in antibiotic production.";
RL   Mol. Gen. Genet. 263:966-977(2000).
RN   [4]
RP   INDUCTION.
RX   PubMed=11872487; DOI=10.1128/aem.68.3.1351-1357.2002;
RA   Semighini C.P., Marins M., Goldman M.H., Goldman G.H.;
RT   "Quantitative analysis of the relative transcript levels of ABC transporter
RT   Atr genes in Aspergillus nidulans by real-time reverse transcription-PCR
RT   assay.";
RL   Appl. Environ. Microbiol. 68:1351-1357(2002).
CC   -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the protection
CC       of the cells against a wide range of toxic compounds.
CC       {ECO:0000269|PubMed:10954082}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10954082};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is strongly increased in the presence of
CC       cycloheximide, imazalil, itraconazole, hygromycin, and 4-nitroquinoline
CC       oxide (4-NQO). {ECO:0000269|PubMed:10954082,
CC       ECO:0000269|PubMed:11872487}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR   EMBL; BN001307; CBF86663.1; -; Genomic_DNA.
DR   EMBL; AACD01000038; EAA64460.1; -; Genomic_DNA.
DR   RefSeq; XP_659953.1; XM_654861.1.
DR   AlphaFoldDB; A0A1U8QG99; -.
DR   SMR; A0A1U8QG99; -.
DR   STRING; 162425.CADANIAP00009048; -.
DR   EnsemblFungi; CBF86663; CBF86663; ANIA_02349.
DR   EnsemblFungi; EAA64460; EAA64460; AN2349.2.
DR   GeneID; 2875142; -.
DR   KEGG; ani:AN2349.2; -.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   OMA; ENIKQSW; -.
DR   OrthoDB; 186078at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
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   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
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; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1284
FT                   /note="ABC multidrug transporter atrC"
FT                   /id="PRO_0000449466"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        824..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        846..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        955..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          55..346
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          381..626
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          705..992
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1027..1280
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         416..423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1062..1069
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        800
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        995
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1284 AA;  139551 MW;  6959ACA1986E806A CRC64;
     MKSTAESKET PSQDESTTSV PCTEAPLVEE GEEASFGAYK RIFTFAGRTE LILQAVAILA
     ACASGAGIAL QNLIFGQFVT VITDFTNGIS TPADFRDNAA ELALYFVYLG IARLVLSYTY
     NTLLTYAAYR IVRNIRHAYL KAALSQEVAY YDFGSGGSIA AQATSNGKLI QAGASDKIGL
     LFQGLAAFVT AFIIAFVVQW KLTLICICIP VATIGTTGVV AAVEAGHETR ILQIHAQANS
     FAEGILAGVK AVHAFGMRDS LVRKFDEYLV EAHKVGKKIS PLLGLLFSAE YTIIYLGYGL
     AFWQGIHMFG RGEIGTAGDI FTVLLSVVIA SINLTLLAPY SIEFSRAASA AAQLFRLIDR
     ESEINPYGKE GLEPERVLGD VELENVTFSY PTRPGITVLD NFSLKVPAGK VTALVGQSGS
     GKSTIVGLLE RWYNPTSGAI RLDGNLISEL NVGWLRRNVR LVQQEPVLFQ GSVFDNIRYG
     LVGTPWENAS REEQMERVQE AAKLAYAHEF ISELTDGYDT LIGERGGLLS GGQKQRVAIA
     RSVVSQPKVL LLDEATSALD PHAETIVQKA LDKAAEGRTT IVIAHKLATI RKADNIVVMS
     KGHIVEQGTH ESLIAKDGVY AGLVKIQNLA VNASAHDNVN EEGEGEDVAL LEVTETAVTR
     YPTSIRGRMN SIKDRDDYEN HKHMDMLAAL AYLVRECPEL KWAYLVVLLG CLGGCAMYPG
     QAILMSRVVE VFTLSGDAML DKGDFYASML IVLAAGCLIC YLAVGYATNT IAQHLSHWFR
     RLILHDMLRQ DIQFFDREEN TTGALVSRID SYPHAILELM GYNIALVVIA VLQVVTCGIL
     AIAFSWKLGL VVVFGGIPPL VGAGMVRIRV DSRLDRQTSK KYGTSSSIAS EAVNAIRTVS
     SLAIEETVLR RYTEELDHAV SSSVKPMAAT MICFGLTQCI EYWFQALGFW YGCRLVSLGE
     TSMYSFFVAF LSVFFAGQAS AQLFQWSTSI TKGINATNYI AWLHQLQPTV RETPENHDKG
     PGSGAPIAMD NVRFSYPLRP DAPILKGVNL KINKGQFIAF VGSSGCGKST MIAMLERFYD
     PTTGSITIDA STLTDINPIS YRNIVALVQQ EPTLFQGTIR DNISLGVFNP NTQPFFSDKD
     AVKSVSDEQI ESALRAANAW DFVSSLPQGI YTPAGSGGSQ LSGGQRQRIA IARALIRDPK
     ILLLDEATSA LDTESEKIVQ KALEGAARDG DRLTVAVAHR LSTIKDANVI CVFFGGKIAE
     MGTHQELIVR GGLYRRMCEA QALD
 
 
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