ID   CDR3_CANAX              Reviewed;        1501 AA.
AC   O42690;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Opaque-specific ABC transporter CDR3;
GN   Name=CDR3;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1006;
RX   PubMed=9393682; DOI=10.1128/jb.179.23.7210-7218.1997;
RA   Balan I., Alarco A.-M., Raymond M.;
RT   "The Candida albicans CDR3 gene codes for an opaque-phase ABC
RT   transporter.";
RL   J. Bacteriol. 179:7210-7218(1997).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Regulated in a cell-type-specific manner with high
CC       levels in WO-1 opaque cells and undetectable levels in WO-1 white
CC       cells.
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; U89714; AAC49886.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42690; -.
DR   SMR; O42690; -.
DR   VEuPathDB; FungiDB:C1_08070W_A; -.
DR   VEuPathDB; FungiDB:CAWG_03447; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
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; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR005285; Drug-R_PDR/CDR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 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   TIGRFAMs; TIGR00956; 3a01205; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1501
FT                   /note="Opaque-specific ABC transporter CDR3"
FT                   /id="PRO_0000093437"
FT   TOPO_DOM        1..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        589..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        614..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        653..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        755..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        776..1175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1176..1196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1212..1232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1261..1281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1297..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1325..1345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1353..1375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1451..1471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          140..395
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          840..1083
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          58..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         876..883
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1501 AA;  170271 MW;  08A5C43DA97C06DE CRC64;
     MAKTSQAEGQ PYKGYYNNKS QGQPYHGYYS GFNKSASAQI HHLARSLTQG VQSHYDDTYT
     TATMHPNGIN PISDKTDPTL DPESPSFSSK RWVQNMWKLY QSDSEYYKPG KLGVAYKNLR
     VYGDAIESDY QTTVSNGVLK YARNIFNKFR KDNDDYSFDI LKPMEGLIKP GEVTVVLGRP
     GAGCSTFLKT IACRTEGFHV ADGSVISYDG ITQDEIRNHL RGEVVYCAET ETHFPNLTVG
     ETLEFAALMK TPQNRPMGVS REEYAKHVVD VVMATYGLSH TKNTKVGNDF IRGISGGERK
     RLSIAEVTLV QASIQCWDNS TRGLDAATAL EFISSLKTSA SILNDTPLIA IYQCSQNAYD
     LFDKVIVMYE GYQIFFGSSQ RAAAYFKKMG FVCQDRQTTP DFLTSITSPA ERIIKPGYER
     LVPRTPKEFY RYWRRSPERQ ALLEEIDEYL DNCENYDQKQ KIFEANNAKK AKHTYNKSSY
     TVSLPMQVRY IMKRYWDRMR GDIIVPLSTV AGNIAMALIL SSVFYNLQPN SSSFYYRTSV
     MYYALLFNAY SSVLEIYNMY EGRAIVQKHR EYALYPPMAD AIGSIISDFP LKVVCSVLFN
     LILYFMVNFK REPGAFFFYL LISFCSTLFM SHLFRTIGAF TNSLAEAMTP SSLLLFALST
     FSGFAIPVTY MLGWCKWIRW VNPLAYAYEA LISNEFHGRV FDCSNIVPSG FGYPKTGNSV
     VCASIGALPG EFKVDGDLYL KLAFDYSYSN VWRNFGVLMA FIIFLFGTTI FFVQTNKSSI
     SKGETLVFRR KNIRKMRKME EDEEAYMDGM APLDFSGSTE ISDYSYDYMD RKLLDTSNIF
     HWRNLTYTVK IKSEERVILN NIDGWVKPGE VTALMGASGA GKTTLLNALS ERLTTGVITS
     GTRMVNGGEL DSSFQRSIGY VQQQDLHLET STVREALKFS ARLRQPNSVS IAEKDSYVEK
     IIDLLEMRTY VDAIVGVPGE GLNVEQRKRL TIAVELVARP KLLVFLDEPT SGLDSQTAWS
     ICKLIRKLAN HGQAILCTIH QPSAILLEEF DRLLLLQKGE TVYFGEFGAN CHTLIEYFER
     NGASKCPQHA NPAEWMLGVI GAAPGTQANQ DYFETWRNSP EYRAVQNELH RLEEMPGLAS
     GEKEPDTNQA YAASFWKQYI FVVHRLFQQY WRTPSYIYSK FAMAVLCSLF NGFTYYKSQN
     SMQGLKNQML SIFSMFVVLT TLAQQYVPLF VTQRDLYEAR ERPSKTFSWL AFIAAQITAE
     IPYQVLAATI SFFSWYYPVG LYRNAVYSGA VTHRGVLMWL IMTLMFIYSS TLAQFCISWN
     QLADYAANWI SLLLTISMIF CGVIATKDSM PKFWVFLYRC TPLTYLTSAM MSIGLGDSFV
     KCAPTEILTF PPQTPGVQKC QDYMGAYISI AGGYLLNPEA TDNCKFCIMD KTNQFLDFMN
     ISIHNFGRDT GIFIVFIVFN MAATVFSYWL FRVPKGNREK GSFFDKLPFL NGGGDTNHEN
     V