CDR2_CANAL
ID CDR2_CANAL Reviewed; 1499 AA.
AC P78595; A0A1D8PK27; Q5ANE5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Multidrug resistance protein CDR2;
GN Name=CDR2; OrderedLocusNames=CAALFM_C304890WA;
GN ORFNames=CaO19.13379, CaO19.5958;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=9043118; DOI=10.1099/00221287-143-2-405;
RA Sanglard D., Ischer F., Monod M., Bille J.;
RT "Cloning of Candida albicans genes conferring resistance to azole
RT antifungal agents: characterization of CDR2, a new multidrug ABC
RT transporter gene.";
RL Microbiology 143:405-416(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Multidrug efflux transporter. Confers resistance to azole
CC antifungal agents, to other antifungals (terbinafine, amorolfine) and
CC to a variety of metabolic inhibitors.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; U63812; AAB96797.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28505.1; -; Genomic_DNA.
DR RefSeq; XP_723169.1; XM_718076.2.
DR AlphaFoldDB; P78595; -.
DR SMR; P78595; -.
DR BioGRID; 1218359; 9.
DR STRING; 237561.P78595; -.
DR BindingDB; P78595; -.
DR ChEMBL; CHEMBL1163105; -.
DR TCDB; 3.A.1.205.5; the atp-binding cassette (abc) superfamily.
DR PRIDE; P78595; -.
DR GeneID; 3635265; -.
DR KEGG; cal:CAALFM_C304890WA; -.
DR CGD; CAL0000197349; CDR2.
DR VEuPathDB; FungiDB:C3_04890W_A; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P78595; -.
DR OMA; VYGWKVF; -.
DR OrthoDB; 324553at2759; -.
DR PRO; PR:P78595; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
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:0090554; F:phosphatidylcholine floppase activity; IGI:CGD.
DR GO; GO:0140341; F:phosphatidylethanolamine floppase activity; IGI:CGD.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IGI:CGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:CGD.
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 3: Inferred from homology;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1499
FT /note="Multidrug resistance protein CDR2"
FT /id="PRO_0000093436"
FT TOPO_DOM 1..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..1193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1229..1249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1279..1299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1354..1374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1465..1485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 148..402
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 857..1101
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 893..900
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 15
FT /note="K -> N (in Ref. 1; AAB96797)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="A -> G (in Ref. 1; AAB96797)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="M -> S (in Ref. 1; AAB96797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1499 AA; 168965 MW; E91C5A2C303A516A CRC64;
MSTANTSLSQ QLDEKPWVDA SDNSSVQEYQ GFDATASHNI QDLARKLTHG STNGDHHSAN
DLARYLSHMS DIPGVSPFNG NISHEQLDPD SENFNAKYWV KNLKKLFESD SDYYKPSKLG
VAYRNLRAYG IANDSDYQPT VTNALWKFTT EAINKLKKPD DSKYFDILKS MDAIMRPGEL
TVVLGRPGAG CSTLLKTIAV NTYGFHIGKE SQITYDGLSP HDIERHYRGD VIYSAETDVH
FPHLSVGDTL EFAARLRTPQ NRGEGIDRET YAKHMASVYM ATYGLSHTRN TNVGNDFVRG
VSGGERKRVS IAEASLSGAN IQCWDNATRG LDSATALEFI RALKTSATIL DTTPLIAIYQ
CSQDAYELFD NVVVLYEGYQ IFFGKASKAK EYFENMGWKC PQRQTTADFL TSLTNPAERE
PLPGYEDKVP RTAQEFETFW KNSPEYAELT KEIDEYFVEC ERSNTGETYR ESHVAKQSNN
TRPSSPYTVS FFMQVRYVIA RNFLRMKGDP SIPLISILSQ LVMGLILASV FFNLRKSTDT
FYFRGGALFF SVLFNAFSSL LEILSLYEAR PIVEKHRKYA LYRPSADALA SIISELPVKL
LMTMSFNIVY YFMVNLRRTA GNFFFYWLMC ASCTLVMSHM FRSIGAVTTT IATAMSLSTV
FLLAMIIYAG FVLPIPYILG WSRWIRYINP VTYIFESLMV NEFHGREFEC GQYIPSGPGF
ENLPVENKVC TTVGSTPGST VVQGTEYIKL AYQFYSSHKW RNFGITVAFA VFFLGVYVAL
TEFNKGAMQK GEIVLFLKGS LKKHKRKTAA SNKGDIEAGP VAGKLDYQDE AEAVNNEKFT
EKGSTGSVDF PENREIFFWR DLTYQVKIKK EDRVILDHVD GWVKPGQITA LMGASGAGKT
TLLNCLSERV TTGIITDGER LVNGHALDSS FQRSIGYVQQ QDVHLETTTV REALQFSAYL
RQSNKISKKE KDDYVDYVID LLEMTDYADA LVGVAGEGLN VEQRKRLTIG VELVAKPKLL
LFLDEPTSGL DSQTAWSICK LMRKLADHGQ AILCTIHQPS ALIMAEFDKL LFLQKGGRTA
YFGELGENCQ TMINYFEKYG ADPCPKEANP AEWMLQVVGA APGSHAKQDY FEVWRNSSEY
QAVREEINRM EAELSKLPRD NDPEALLKYA APLWKQYLLV SWRTIVQDWR SPGYIYSKLI
LVISSSLFIG FSFFKSKNNL QGLQSQMLAV FMFFVPFTTF IDQMLPYFVK HRAVYEVREA
PSRTFSWFAF IAGQITSEIP FQIVVGTISY FCWYYPVGLY ANAEPTDSVN SRGVLMWMLL
TAFYVYTSTM GQLAISLNEL IDNAANLATT LFTLCLMFCG VLAGPNVIPG FWIFMYRCNP
FTYLIQAILS TGLANAKVTC APRELVTLKP PMGETCSSFI GPYTEAAGGY FSTNSDGTCS
VCRIDSTNQF LESINALFSQ RWRNFGIFVA FIGINIILTI FFYWLARVPK GNREKKMKK
