MLT1_CANAL
ID MLT1_CANAL Reviewed; 1606 AA.
AC Q5A762; A0A1D8PEB9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Multiple drug resistance-associated protein-like transporter 1 {ECO:0000303|PubMed:11929516};
DE Short=MRP-like transporter 1 {ECO:0000303|PubMed:11929516};
DE AltName: Full=Vacuolar multi-drug resistance ABC transporter MTL1 {ECO:0000305};
GN Name=MLT1; Synonyms=ABC1, BPT1, YCF1 {ECO:0000303|PubMed:16254441};
GN OrderedLocusNames=CAALFM_C108210CA; ORFNames=CaO19.12566, CaO19.5100;
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 [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 [2]
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 [3]
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).
RN [4]
RP INDUCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11929516; DOI=10.1046/j.1365-2958.2002.02769.x;
RA Theiss S., Kretschmar M., Nichterlein T., Hof H., Agabian N., Hacker J.,
RA Kohler G.A.;
RT "Functional analysis of a vacuolar ABC transporter in wild-type Candida
RT albicans reveals its involvement in virulence.";
RL Mol. Microbiol. 43:571-584(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16254441; DOI=10.1159/000088141;
RA Gaur M., Choudhury D., Prasad R.;
RT "Complete inventory of ABC proteins in human pathogenic yeast, Candida
RT albicans.";
RL J. Mol. Microbiol. Biotechnol. 9:3-15(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22662216; DOI=10.1371/journal.pone.0037768;
RA Wang L., Jia Y., Tang R.J., Xu Z., Cao Y.B., Jia X.M., Jiang Y.Y.;
RT "Proteomic analysis of Rta2p-dependent raft-association of detergent-
RT resistant membranes in Candida albicans.";
RL PLoS ONE 7:E37768-E37768(2012).
CC -!- FUNCTION: Vacuolar multi-drug resistance ABC transporter that may be
CC involved in the transport of bilirubin and glutathione conjugates (By
CC similarity). Plays an important role in virulence.
CC {ECO:0000250|UniProtKB:P39109, ECO:0000269|PubMed:11929516,
CC ECO:0000303|PubMed:16254441}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11929516, ECO:0000269|PubMed:16254441}.
CC Note=Associates with lipid rafts in a RTA2-dependent manner.
CC {ECO:0000269|PubMed:22662216}.
CC -!- INDUCTION: Is 10-fold down-regulated during log phase and strongly
CC induced at the diauxic shift. Expression remains high during the
CC postdiauxic phase and continues into stationary phase. Is also up-
CC regulated during the presence of cadmium ions.
CC {ECO:0000269|PubMed:11929516}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased sublethal intraperitoneal
CC infection in mice. {ECO:0000269|PubMed:11929516}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC {ECO:0000255|RuleBase:RU000684}.
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DR EMBL; CP017623; AOW26461.1; -; Genomic_DNA.
DR RefSeq; XP_717637.1; XM_712544.2.
DR AlphaFoldDB; Q5A762; -.
DR SMR; Q5A762; -.
DR STRING; 237561.Q5A762; -.
DR PRIDE; Q5A762; -.
DR GeneID; 3640748; -.
DR KEGG; cal:CAALFM_C108210CA; -.
DR CGD; CAL0000178329; MLT1.
DR VEuPathDB; FungiDB:C1_08210C_A; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; Q5A762; -.
DR OrthoDB; 138195at2759; -.
DR PRO; PR:Q5A762; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IMP:CGD.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015127; F:bilirubin transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:CGD.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole; Virulence.
FT CHAIN 1..1606
FT /note="Multiple drug resistance-associated protein-like
FT transporter 1"
FT /id="PRO_0000430555"
FT TRANSMEM 67..87
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 1015..1035
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TRANSMEM 1132..1152
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TRANSMEM 1154..1174
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TRANSMEM 1252..1272
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TRANSMEM 1276..1296
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT DOMAIN 326..613
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 672..905
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1042..1308
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1345..1600
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 908..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 704..711
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1379..1386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ 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
