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Multiple drug resistance-associated protein-like transporter 1 (MRP-like transporter 1) (Vacuolar multi-drug resistance ABC transporter MTL1)

 MLT1_CANAL              Reviewed;        1606 AA.
Q5A762; A0A1D8PEB9;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
22-NOV-2017, entry version 110.
RecName: Full=Multiple drug resistance-associated protein-like transporter 1 {ECO:0000303|PubMed:11929516};
Short=MRP-like transporter 1 {ECO:0000303|PubMed:11929516};
AltName: Full=Vacuolar multi-drug resistance ABC transporter MTL1 {ECO:0000305};
Name=MLT1; Synonyms=ABC1, BPT1, YCF1 {ECO:0000303|PubMed:16254441};
OrderedLocusNames=CAALFM_C108210CA; ORFNames=CaO19.12566, CaO19.5100;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
INDUCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11929516; DOI=10.1046/j.1365-2958.2002.02769.x;
Theiss S., Kretschmar M., Nichterlein T., Hof H., Agabian N.,
Hacker J., Kohler G.A.;
"Functional analysis of a vacuolar ABC transporter in wild-type
Candida albicans reveals its involvement in virulence.";
Mol. Microbiol. 43:571-584(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16254441; DOI=10.1159/000088141;
Gaur M., Choudhury D., Prasad R.;
"Complete inventory of ABC proteins in human pathogenic yeast, Candida
albicans.";
J. Mol. Microbiol. Biotechnol. 9:3-15(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=22662216; DOI=10.1371/journal.pone.0037768;
Wang L., Jia Y., Tang R.J., Xu Z., Cao Y.B., Jia X.M., Jiang Y.Y.;
"Proteomic analysis of Rta2p-dependent raft-association of detergent-
resistant membranes in Candida albicans.";
PLoS ONE 7:E37768-E37768(2012).
-!- FUNCTION: Vacuolar multi-drug resistance ABC transporter that may
be involved in the transport of bilirubin and glutathione
conjugates (By similarity). Plays an important role in virulence.
{ECO:0000250|UniProtKB:P39109, ECO:0000269|PubMed:11929516,
ECO:0000303|PubMed:16254441}.
-!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane
protein {ECO:0000269|PubMed:11929516,
ECO:0000269|PubMed:16254441}. Note=Associates with lipid rafts in
a RTA2-dependent manner. {ECO:0000269|PubMed:22662216}.
-!- INDUCTION: Is 10-fold down-regulated during log phase and strongly
induced at the diauxic shift. Expression remains high during the
postdiauxic phase and continues into stationary phase. Is also up-
regulated during the presence of cadmium ions.
{ECO:0000269|PubMed:11929516}.
-!- DISRUPTION PHENOTYPE: Leads to decreased sublethal intraperitoneal
infection in mice. {ECO:0000269|PubMed:11929516}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily.
{ECO:0000255|RuleBase:RU000684}.
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EMBL; CP017623; AOW26461.1; -; Genomic_DNA.
RefSeq; XP_717637.1; XM_712544.2.
ProteinModelPortal; Q5A762; -.
PRIDE; Q5A762; -.
EnsemblFungi; AOW26461; AOW26461; CAALFM_C108210CA.
GeneID; 3640748; -.
KEGG; cal:CAALFM_C108210CA; -.
CGD; CAL0000178329; MLT1.
InParanoid; Q5A762; -.
OrthoDB; EOG092C0QQU; -.
PRO; PR:Q5A762; -.
Proteomes; UP000000559; Chromosome 1.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:CGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:CGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
GO; GO:0030447; P:filamentous growth; IMP:CGD.
GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Membrane; Nucleotide-binding;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Vacuole; Virulence.
CHAIN 1 1606 Multiple drug resistance-associated
protein-like transporter 1.
/FTId=PRO_0000430555.
TRANSMEM 67 87 Helical; Name=1. {ECO:0000255}.
TRANSMEM 111 131 Helical; Name=2. {ECO:0000255}.
TRANSMEM 134 154 Helical; Name=3. {ECO:0000255}.
TRANSMEM 159 179 Helical; Name=4. {ECO:0000255}.
TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.
TRANSMEM 325 345 Helical; Name=6. {ECO:0000255}.
TRANSMEM 365 385 Helical; Name=7. {ECO:0000255}.
TRANSMEM 438 458 Helical; Name=8. {ECO:0000255}.
TRANSMEM 470 490 Helical; Name=9. {ECO:0000255}.
TRANSMEM 548 568 Helical; Name=10. {ECO:0000255}.
TRANSMEM 588 608 Helical; Name=11. {ECO:0000255}.
TRANSMEM 1015 1035 Helical; Name=12. {ECO:0000255}.
TRANSMEM 1071 1091 Helical; Name=13. {ECO:0000255}.
TRANSMEM 1132 1152 Helical; Name=14. {ECO:0000255}.
TRANSMEM 1154 1174 Helical; Name=15. {ECO:0000255}.
TRANSMEM 1252 1272 Helical; Name=16. {ECO:0000255}.
TRANSMEM 1276 1296 Helical; Name=17. {ECO:0000255}.
DOMAIN 326 613 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 672 905 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1042 1308 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1345 1600 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 704 711 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1379 1386 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
SEQUENCE 1606 AA; 180693 MW; 8A22999D3B480EA3 CRC64;
MNESNRELIL GLSPVHLSLF NSESLLHTFN FFGVGDGQAN IASNYVTASK FVIPQPLYSP
HGNALNPAFV ELIGQAVNTF FAIFMLFQLT RLLLTKKKSH RIYTPTPFSQ TLKISLVLLQ
VILVASLYFL NKNSYFIGGI AATVLALILH LVEFRRSPIA IESLLTYWSA NTAFTFAVFI
QDSYSKHKIY ANSGPAYVIE IISLVNSFLI FVFEVGYYKP GFEITNEKFL DTVNLFSYFT
FYYLQPLINK IYATDDVQLT DLPDILGNIT CDDTKAKVAK AWEEELKRTK KPGLVSKVWS
FVTRRKVNSK PQMFLAIAKA FFDKFAISIT LAIIVTGLSF LQPFLLRKFI QFFSTYFYSV
EKPPIIIGYF WASVMFLTSV ANFIAFNQAF KTQFDLGYEI QSSLTTLIYE KALRLSPQSR
KNKPTGDIIN HITMDIDIIF WFCWQLGEYL ASPLKLAVCL AALYKLFSNA TWAGVITAII
VAPLATLVNA SMSKNYIQLM KDKDERTSLI TEILNSAKSI KFYSWEKPML ARLSHIRNDR
ELNNIKKIGV VSALAQFLWS CIPFFISCAT YATYAYFYNV PLTPDIVFPA LALFDLLSEP
MLLIPSFIVE VIEVSTSLAR IGELLCLDEL ADDQHGYVKR DPEPNDNSIY SVIVKDATFV
WSEETQQKQY TDEESEVQEV PASNVALKNI NFSARKGELA CIVGKVGSGK STLIKAILGD
VPIKIPSYSD DSTNPTPSVE TFGSIAYCPQ NPWILNGTVK ENILFGHKYD AEFYQKTIDA
CELISDFKNL PDGDQTVVGE KGISLSGGQK ARISLARSVY TRADIYLLDD ILSAVDAHVG
KNIIKKVLSN EGLIGNRCRI LATNSVPVLH EANDIYLIAG GAFVEHGKFK EVMKRNGDLA
KLIKEYGRKK DEPTEEETTE ASTEPKEEDH SNGKSDTAVH DELDTDELVD EIVDYVGEQN
RGVVEQAILR RASVVSYGHN YENDEADNGQ IRKTRHEQEE SRKGTVPWDI FKQYIIACDY
KYFSFYVAAT FSVVLISAGE KYLLSYWSQL NSEQNDTVEP VFFLGTYATL GVVSGFLTYM
GALVIWSYCI VKGSTYFHNK MAESVLRSPM SFFDTTPIGR ILNRFTEDIG KIDMNLPWTI
ISFITTLLNG FVTFGVILSF LPLMLVVIVS LLFVYNYFRI RFVPTTRELK RLESIAKSPV
LATIQESING VETIKAFHQR ERFVYKSKKL IDEKTLIGVV QQNCNRWLSM RLQTISSSIM
FFTALLAVVT LGGKHPILPS ILGFVMTYSM SITYILNSLV RIWAEMQAGG VAIERIIEYC
DLPSEAPMII EDKRPQDSWP AHGVVKFKKY STAYRKHLDP VLREIELTIN SKEKVGIVGR
TGAGKSSLTL ALFRIIEATG GNIEIDGVDT SQIGLYDLRH HLTIIPQEAH TFRASVRENL
DPFGEYSDDK LWKVLELAHL KEHVTKMETD PTEEEKKASK NPDELSKKVG LDAQIEEGGS
NLSSGQKQLL CLARALLNET SKILVLDEAT AAVDFQTDKI IQETIRTEFK DKTILTIAHR
IDTIMDSDKI LVLDSGKVAE FDSPQNLLKN KDSIFYSLAK EGGYID


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