ATRC_EMEND
ID ATRC_EMEND Reviewed; 1284 AA.
AC Q9Y8G2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ABC multidrug transporter atrC;
GN Name=atrC {ECO:0000303|PubMed:10954082};
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=W6-096;
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 [2]
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; AF071410; AAD43625.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y8G2; -.
DR SMR; Q9Y8G2; -.
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 Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1284
FT /note="ABC multidrug transporter atrC"
FT /id="PRO_0000449465"
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; 139649 MW; D81BB710B50D2BE3 CRC64;
MKSTAESKET PSQDESTTSV PCTEAPLVEE GEEASFGAYK RIFTFAGRTE LILQAVAILA
ACASGAGIAL QNLIFGQFVT VITDFTNGIS TPADFRDNAA ELALYFVYLG IARLVLSYTY
NTLLTYAAYR IVRNIRHAYL KAALSQEVAY YDFGSGGSIA AQATSNGKLI QAGASDKIGL
LFQGLAAFVT LSLSRLWCKW 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
