ID MDL1_YEAST Reviewed; 695 AA.
AC P33310; D6VYJ1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=ATP-dependent permease MDL1, mitochondrial;
DE AltName: Full=ABC transporter MDL1;
DE AltName: Full=Multidrug resistance-like protein 1;
DE Flags: Precursor;
GN Name=MDL1; OrderedLocusNames=YLR188W; ORFNames=L9470.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7912468; DOI=10.1002/yea.320100310;
RA Dean M.C., Allikmets R., Gerrard B.C., Stewart C., Kistler A., Shafer B.,
RA Michaelis S., Strathern J.;
RT "Mapping and sequencing of two yeast genes belonging to the ATP-binding
RT cassette superfamily.";
RL Yeast 10:377-383(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-467; SER-575 AND
RP ASP-598.
RX PubMed=11251115; DOI=10.1126/science.1056957;
RA Young L., Leonhard K., Tatsuta T., Trowsdale J., Langer T.;
RT "Role of the ABC transporter Mdl1 in peptide export from mitochondria.";
RL Science 291:2135-2138(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Mediates export of peptides with molecular masses of 2100 to
CC 600 daltons generated upon proteolysis of mitochondrial inner membrane
CC proteins. {ECO:0000269|PubMed:11251115}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11251115, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:11251115,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20681.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L16958; AAA20681.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U17246; AAB67455.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09507.1; -; Genomic_DNA.
DR PIR; S51433; S51433.
DR RefSeq; NP_013289.1; NM_001182075.1.
DR AlphaFoldDB; P33310; -.
DR SMR; P33310; -.
DR BioGRID; 31458; 137.
DR STRING; 4932.YLR188W; -.
DR TCDB; 3.A.1.212.1; the atp-binding cassette (abc) superfamily.
DR MaxQB; P33310; -.
DR PaxDb; 4932-YLR188W; -.
DR PeptideAtlas; P33310; -.
DR EnsemblFungi; YLR188W_mRNA; YLR188W; YLR188W.
DR GeneID; 850885; -.
DR KEGG; sce:YLR188W; -.
DR AGR; SGD:S000004178; -.
DR SGD; S000004178; MDL1.
DR VEuPathDB; FungiDB:YLR188W; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000176745; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; P33310; -.
DR OMA; MTWLGER; -.
DR OrthoDB; 2876209at2759; -.
DR BioCyc; YEAST:G3O-32311-MONOMER; -.
DR BioGRID-ORCS; 850885; 0 hits in 10 CRISPR screens.
DR PRO; PR:P33310; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P33310; Protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0090374; P:oligopeptide export from mitochondrion; IMP:SGD.
DR CDD; cd18573; ABC_6TM_ABCB10_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..100
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 101..695
FT /note="ATP-dependent permease MDL1, mitochondrial"
FT /id="PRO_0000045330"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 103..398
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 432..673
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 467
FT /note="G->V: Decreased release of long peptides from
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:11251115"
FT MUTAGEN 575
FT /note="S->N: Decreased release of long peptides from
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:11251115"
FT MUTAGEN 598
FT /note="D->A: Decreased release of long peptides from
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:11251115"
FT CONFLICT 22
FT /note="A -> G (in Ref. 1; AAA20681)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="F -> L (in Ref. 1; AAA20681)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..268
FT /note="GA -> WP (in Ref. 1; AAA20681)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="NE -> KQ (in Ref. 1; AAA20681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 75950 MW; 3175B17FBD779BBE CRC64;
MIVRMIRLCK GPKLLRSQFA SASALYSTKS LFKPPMYQKA EINLIIPHRK HFLLRSIRLQ
SDIAQGKKST KPTLKLSNAN SKSSGFKDIK RLFVLSKPES KYIGLALLLI LISSSVSMAV
PSVIGKLLDL ASESDGEDEE GSKSNKLYGF TKKQFFTALG AVFIIGAVAN ASRIIILKVT
GERLVARLRT RTMKAALDQD ATFLDTNRVG DLISRLSSDA SIVAKSVTQN VSDGTRAIIQ
GFVGFGMMSF LSWKLTCVMM ILAPPLGAMA LIYGRKIRNL SRQLQTSVGG LTKVAEEQLN
ATRTIQAYGG EKNEVRRYAK EVRNVFHIGL KEAVTSGLFF GSTGLVGNTA MLSLLLVGTS
MIQSGSMTVG ELSSFMMYAV YTGSSLFGLS SFYSELMKGA GAAARVFELN DRKPLIRPTI
GKDPVSLAQK PIVFKNVSFT YPTRPKHQIF KDLNITIKPG EHVCAVGPSG SGKSTIASLL
LRYYDVNSGS IEFGDEDIRN FNLRKYRRLI GYVQQEPLLF NGTILDNILY CIPPEIAEQD
DRIRRAIGKA NCTKFLANFP DGLQTMVGAR GAQLSGGQKQ RIALARAFLL DPAVLILDEA
TSALDSQSEE IVAKNLQRRV ERGFTTISIA HRLSTIKHST RVIVLGKHGS VVETGSFRDL
IAIPNSELNA LLAEQQDEEG KGGVIDLDNS VAREV
//
