CDR1_CANAX
ID CDR1_CANAX Reviewed; 1501 AA.
AC P43071;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Multidrug resistance protein CDR1;
GN Name=CDR1;
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=ATCC 64385 / 1001;
RX PubMed=7614555; DOI=10.1007/bf00352101;
RA Prasad R., de Wergifosse P., Balzi E., Goffeau A.;
RT "Molecular cloning and characterization of a novel gene of Candida
RT albicans, CDR1, conferring multiple resistance to drugs and antifungals.";
RL Curr. Genet. 27:320-329(1995).
CC -!- FUNCTION: Transporter, whose physiological function is not yet
CC established. Confers resistance to the chemical cycloheximide.
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; X77589; CAA54692.1; -; Genomic_DNA.
DR PIR; S57198; S57198.
DR AlphaFoldDB; P43071; -.
DR SMR; P43071; -.
DR BindingDB; P43071; -.
DR ChEMBL; CHEMBL1163109; -.
DR TCDB; 3.A.1.205.4; the atp-binding cassette (abc) superfamily.
DR VEuPathDB; FungiDB:C3_05220W_A; -.
DR VEuPathDB; FungiDB:CAWG_02836; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cycloheximide resistance; Glycoprotein;
KW Membrane; Nucleotide-binding; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1501
FT /note="Multidrug resistance protein CDR1"
FT /id="PRO_0000093435"
FT TOPO_DOM 1..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..1195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1230..1250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1356..1376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1467..1487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 150..404
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 859..1103
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 895..902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1501 AA; 169938 MW; BB144A0BAD7ED233 CRC64;
MSDSKMSSQD ESKLEKAISQ DSSSENHSIN EYHGFDAHTS ENIQNLARTF THDSFKDDSS
AGLLKYLTHM SEVPGVNPYE HEEINNDQLN PDSENFNAKF WVKNLRKLFE SDPEYYKPSK
LGIGYRNLRA YGVANDSDYQ PTVTNALWKL ATEGFRHFQK DDDSRYFDIL KSMDAIMRPG
ELTVVLGRPG AGCSTLLKTI AVNTYGFHIG KESQITYDGL SPHDIERHYR GDVIYSAETD
VHFPHLSVGD TLEFAARLRT PQNRGEGIDR ETYAKHMASV YMATYGLSHT RNTNVGNDFV
RGVSGGERKR VSIAEASLSG ANIQCWDNAT RGLDSATALE FIRALKTSAV ILDTTPLIAI
YQCSQDAYDL FDKVVVLYEG YQIFFGKATK AKEYFEKMGW KCPQRQTTAD FLTSLTNPAE
REPLPGYEDK VPRTAQEFET YWKNSPEYAE LTKEIDEYFV ECERSNTRET YRESHVAKQS
NNTRPASPYT VSFFMQVRYG VARNFLRMKG DPSIPIFSVF GQLVMGLILS SVFYNLSQTT
GSFYYRGAAM FFAVLFNAFS SLLEIMSLFE ARPIVEKHKK YALYRPSADA LASIISELPV
KLAMSMSFNF VFYFMVNFRR NPGRFFFYWL MCIWCTFVMS HLFRSIGAVS TSISGAMTPA
TVLLLAMVIY TGFVIPTPSM LGWSRWINYI NPVGYVFESL MVNEFHGREF QCAQYVPSGP
GYENISRSNQ VCTAVGSVPG NEMVSGTNYL AGAYQYYNSH KWRNLGITIG FAVFFLAIYI
ALTEFNKGAM QKGEIVLFLK GSLKKHKRKT AASNKGDIEA GPVAGKLDYQ DEAEAVNNEK
FTEKGSTGSV DFPENREIFF WRDLTYQVKI KKEDRVILDH VDGWVKPGQI TALMGASGAG
KTTLLNCLSE RVTTGIITDG ERLVNGHALD SSFQRSIGYV QQQDVHLPTS TVREALQFSA
YLRQSNKISK KEKDDYVDYV IDLLEMTDYA DALVGVAGEG LNVEQRKRLT IGVELVAKPK
LLLFLDEPTS GLDSQTAWSI CKLMRKLADH GQAILCTIHQ PSALIMAEFD RLLFLQKGGR
TAYFGELGEN CQTMINYFEK YGADPCPKEA NPAEWMLQVV GAAPGSHAKQ DYFEVWRNSS
EYQAVREEIN RMEAELSKLP RDNDPEALLK YAAPLWKQYL LVSWRTIVQD WRSPGYIYSK
IFLVVSAALF NGFSFFKAKN NMQGLQNQMF SVFMFFIPFN TLVQQMLPYF VKQRDVYEVR
EAPSRTFSWF AFIAGQITSE IPYQVAVGTI AFFCWYYPLG LYNNATPTDS VNPRGVLMWM
LVTAFYVYTA TMGQLCMSFS ELADNAANLA TLLFTMCLNF CGVLAGPDVL PGFWIFMYRC
NPFTYLVQAM LSTGLANTFV KCAEREYVSV KPPNGESCST YLDPYIKFAG GYFETRNDGS
CAFCQMSSTN TFLKSVNSLY SERWRNFGIF IAFIAINIIL TVIFYWLARV PKGNREKKNK
K
