CDR4_CANAX
ID CDR4_CANAX Reviewed; 1490 AA.
AC O74676;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ABC transporter CDR4;
GN Name=CDR4;
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=1161;
RX PubMed=9767132; DOI=10.1016/s0378-1119(98)00412-0;
RA Franz R., Michel S., Morschhaeuser J.;
RT "A fourth gene from the Candida albicans CDR family of ABC transporters.";
RL Gene 220:91-98(1998).
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; AF044921; AAC72295.1; -; Genomic_DNA.
DR PIR; T30550; T30550.
DR AlphaFoldDB; O74676; -.
DR SMR; O74676; -.
DR VEuPathDB; FungiDB:C1_08070W_A; -.
DR VEuPathDB; FungiDB:CAWG_00616; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; 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; IPR043926; ABCG_dom.
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; PF19055; ABC2_membrane_7; 1.
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; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1490
FT /note="ABC transporter CDR4"
FT /id="PRO_0000093438"
FT TOPO_DOM 1..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..1182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1304..1324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1333..1353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1370..1390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1455..1475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 151..407
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 846..1090
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 882..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 1291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1490 AA; 169342 MW; 8E8676C872A4F5C5 CRC64;
MADADTSSNS SKTNEDRSQE GFGTYQGYTD RVASEVQELA RIISHASIQQ LKLKRQHSRQ
ESQKSNEQES ELSGKLGVIP VDENGNFVDQ RLNPNSPEFN AAYWIQNAHK LVSSDIDYFK
PVTIGVAYKN LRAYGSASDA DYQSTLVNLI PKYLSLFFRE YILRHTGPTF DILKPMDGLI
KPGELTVVLG RPGAGCSTFL KTIASQTYGY HIDKDSVIRY NSLTPHEIKK HYRGEVVYCA
ETENHFPQLT VGDTLEFAAK MRTPQNRPLG VSRDAYARHL AAVVMAVYGL SHTRNTKVGN
DFIRGVSGGE RKRVSIAEIT LNNAMVQCWD NSTRGLDSAT ALEFIRALKA SADIVHTTPL
VAIYQCSQDA YDLFDKVVLM YQGYQIYFGS AKKAKQYFID MGYECPQRQT TADFLTSLTN
PAERIVRQGF EGKVPQTPQE FYEYWKKSPE GQQIVADVDQ YLTEHSSAAE KEAIKEAHQA
RQSDHLKPAS PYTVSFFMQV RYIAHRNILR IKGNPSIHLF QIFGNIGMSF ILSSIFYNLP
TATSSFYHRT AALFFAVLFN AFSCLLEIFS LYEARSIVEK HKKYALYHPA ADAFASIVTE
LPTKFIIAIG FNLVYYFMVN FRRTPGNFFF YLLINFSATL AMSHIFRTIG AATKTLQEAM
TPAAILLLAL TIFTGFVIPT PNMHGWCRWI NYLDPLAYAF ESLIANEFHN RDFECSQYVP
SGGSYPTAGP NRICTPVGSV PGQDFVDGTR YMEMSFDYRN SHKWRNFGIV IGFIVFFFCT
YILLCEINKG AMQKGEILLF QQRALKKRKK ANNDIESGEI EKVTPEFDNE YENNQDKMLQ
SGGDTFFWRD LTYQVKIKSE DRVILDHVSG WVKPGQVTAL MGASGAGKTT LLNALSDRLT
TGVVTEGIRL VNGRPLDSSF QRSIGYVQQQ DLHLETSTVR EALEFAAYLR QPKSVSRKEK
NEYVDYIIRL LEMEQYADAV VGVSGEGLNV EQRKRLSIGV ELVAKPKLLV FLDEPTSGLD
SQTAWSICKL IRKLADNGQA ILCTIHQPSA ILLAEFDRLL FLQRGGQTVY FGDLGKNFTT
LINYFEKYGA PKCPPEANPA EWMLEVIGAA PGSKANQDYY DVWLKSSEFQ EMNSELDLMS
EELVKKPLDD DPDRLKPYAA PYWEQYLFVT KRVFEQNWRT PSYLYSKFLL VVTSSLFNGF
SFYKADRSLQ GLQNQMFSVF MFLVILHTLI QQYLPTFVSQ RDLYEVRERP SKTFSWITFI
AAQVTAEIPW NIICGTLGYF CWYYPVGLYQ NATYTNTVHQ RGAFMWFAIV LFFIYTSTLA
QLCISFLEID DNAANLSVLL FTMCLAFCGV LVTKEQLPGF WVFMYRCSPF TYLVSVMLSV
GLVDAPVTCA AKEYLRFSPP QGYTCMQYME PYMKVAGGYL LNENSTTECE FCTMKVTNVF
LKMIGSDYSK RGRDIGIYIA FIGINIIGTF ILYWFARVPK NFDIKLRRKR
