MDR5_TRIRC
ID MDR5_TRIRC Reviewed; 1292 AA.
AC F2SQT8;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 3.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=ABC multidrug transporter MDR5 {ECO:0000303|PubMed:31501141};
DE AltName: Full=Multidrug resistance protein 5 {ECO:0000303|PubMed:31501141};
GN Name=MDR5 {ECO:0000303|PubMed:31501141}; ORFNames=TERG_04952;
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
RN [2]
RP IDENTIFICATION, GENE MODEL REVISION, FUNCTION, INDUCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=31501141; DOI=10.1128/aac.00863-19;
RA Monod M., Feuermann M., Salamin K., Fratti M., Makino M., Alshahni M.M.,
RA Makimura K., Yamada T.;
RT "Trichophyton rubrum azole resistance mediated by a new ABC transporter,
RT TruMDR3.";
RL Antimicrob. Agents Chemother. 0:0-0(2019).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the modulation
CC susceptibility to itraconazole. {ECO:0000269|PubMed:31501141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out)
CC + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:31501141};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504;
CC Evidence={ECO:0000269|PubMed:31501141};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31501141};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Is slightly over-expressed in strain TIMM20092, and azole-
CC resistant strain isolated in Switzerland.
CC {ECO:0000269|PubMed:31501141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGD88706.2; Type=Erroneous gene model prediction; Evidence={ECO:0000269|PubMed:31501141};
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DR EMBL; GG700652; EGD88706.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003234359.1; XM_003234311.1.
DR AlphaFoldDB; F2SQT8; -.
DR SMR; F2SQT8; -.
DR STRING; 559305.F2SQT8; -.
DR EnsemblFungi; EGD88706; EGD88706; TERG_04952.
DR GeneID; 10372913; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; F2SQT8; -.
DR Proteomes; UP000008864; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1292
FT /note="ABC multidrug transporter MDR5"
FT /id="PRO_0000448445"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 81..370
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 405..650
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 725..1012
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1048..1285
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1083..1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1292 AA; 141281 MW; 86BFB7CECA990CE6 CRC64;
MTEEPKPVTP VLRDGEAGLD TTAPTEAGSL GEEAPKKEAD GIVDVPDAEQ QKQEAPQQGF
SAYVKLWAWC EPIDVVLRIC GFFAAVASGT ALPLMTIIFG KFVNIFNDFG VGKISGDDFR
AQISKNALWF VYLFIGKFAL VYIHTICFNI TAIRSVRKLR LQYIRAILRQ EMAYFDTYTP
GSVATRISNN ANLIQTGMSE KVGTCCQGVA MLISAFVVAF TQSWRLTLPV ATSIPTAVTL
VGITVALDAK LEAKILDIYS KAGGLVEETL GSIRVVVAFG AGDRLSKKYD NHLEAAKGFG
VKKGPVLGIQ YSSEFFIMYC AYALAFWYGI KLLLQGKIGS GGDILTVLFS IVIGTSSLTM
IAPTLGEFTK AGAAANDVLN MINRVPEIDS LSAEGLKPSS VKGDLELSNA VFSYPARPTI
RVLDGVNLKI PARKVTALVG ASGSGKSTII GLLERWYDPA SGSITLDGVD IKDLNVGWLR
RQIGLVQQEP VLFNDTIYTN VLYGLPPDEI AQMDEEKKRE LVRQACIESN ADDFIQGFPK
GYDTIVGERG SLLSGGQRQR VAIARSIISN PPILLLDEAT SALDPTAEAI VQAALDKVSQ
SRTTVLIAHK LSTVKKADNI IVMNKGQVIE QGTHESLLDT KGQYWSLVNA QSLSLASDDS
SSDTDKETDT QPAEILEKHA TTKSTHSKVP HEVAAESEDV ARKFSLFKCL LIIFYEQRRH
WLFFLLGGIA SVVSGGAFPA QAILFSRIVT TFQLPRDQWQ EKGDFWALMF FVLALCILLT
YASIGFFLTV AAFRSSKFYR SEYFKAMISQ DIAYFDKPAN SSGSLTARLS TDPQNLQDLL
SSNIGLILIV IVSLLAVSLL ALVTGWKLAL VSLFGCLPPL FLAGFIRMRM EMQAQDKNAK
LYLESARFAS EAVNSIRTVS SLTLESTVYN NYGDRLKRPV ARSLKYTAIA MIFFGFSDSV
DTAAMALAFW YGGRLMSYGE YDAQQFFVIF IAVIFGGQAA GFIFGFTMNT TKAHAAANHI
IHLRGQVAPI NGSTGEEPAS TEDSDVAVEF RNVSFSYPTR PDQPVLRKIN LNIRHGQNVG
LVGPSGCGKT TMIALLERFY DVTSGDILIN GKPLTDIDVT KYRETASLVS QETTLYQGTI
RENILLGVTR DVPDEEIHQA CKDANIHDFI ISLPEGYNTE AGSRGLSFSG GQRQRLATAR
ALLRNPDFLF LDEATSALDT ESERVVQAAL EHAKRGRTTI AVAHRLSTVQ DCDAIFVLEA
GKIVEQGTHQ ELLRRKGRYF EMCKAQSLDR EA
