MDL2_YEAST
ID MDL2_YEAST Reviewed; 773 AA.
AC P33311; D6W3A0; Q08983;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=ATP-dependent permease MDL2, mitochondrial;
DE AltName: Full=Multidrug resistance-like protein 2;
DE Flags: Precursor;
GN Name=MDL2; Synonyms=SSH1; OrderedLocusNames=YPL270W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION.
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 [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
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 -!- 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 3390 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=AAA20682.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAT93160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA98006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L16959; AAA20682.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z73626; CAA98006.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY693141; AAT93160.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11166.1; -; Genomic_DNA.
DR PIR; S65303; S65303.
DR RefSeq; NP_015053.2; NM_001184084.1.
DR AlphaFoldDB; P33311; -.
DR SMR; P33311; -.
DR BioGRID; 35943; 276.
DR DIP; DIP-4226N; -.
DR IntAct; P33311; 2.
DR MINT; P33311; -.
DR STRING; 4932.YPL270W; -.
DR TCDB; 3.A.1.212.2; the atp-binding cassette (abc) superfamily.
DR MaxQB; P33311; -.
DR PaxDb; P33311; -.
DR PRIDE; P33311; -.
DR EnsemblFungi; YPL270W_mRNA; YPL270W; YPL270W.
DR GeneID; 855858; -.
DR KEGG; sce:YPL270W; -.
DR SGD; S000006191; MDL2.
DR VEuPathDB; FungiDB:YPL270W; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000176745; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; P33311; -.
DR OMA; WGTYLVK; -.
DR BioCyc; YEAST:G3O-34152-MON; -.
DR PRO; PR:P33311; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P33311; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:SGD.
DR GO; GO:0090374; P:oligopeptide export from mitochondrion; ISA:SGD.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR013305; ABC_Tap-like.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR030279; Mdl2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43394:SF2; PTHR43394:SF2; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR00958; 3a01208; 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..90
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 91..773
FT /note="ATP-dependent permease MDL2, mitochondrial"
FT /id="PRO_0000045331"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 119..413
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 493..733
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 56
FT /note="G -> A (in Ref. 1; AAA20682)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="S -> C (in Ref. 1; AAA20682)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="S -> C (in Ref. 1; AAA20682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 85137 MW; 58B1DF92D60E1E58 CRC64;
MLNGRLPLLR LGICRNMLSR PRLAKLPSIR FRSLVTPSSS QLIPLSRLCL RSPAVGKSLI
LQSFRCNSSK TVPETSLPSA SPISKGSARS AHAKEQSKTD DYKDIIRLFM LAKRDWKLLL
TAILLLTISC SIGMSIPKVI GIVLDTLKTS SGSDFFDLKI PIFSLPLYEF LSFFTVALLI
GCAANFGRFI LLRILSERVV ARLRANVIKK TLHQDAEFFD NHKVGDLISR LGSDAYVVSR
SMTQKVSDGV KALICGVVGV GMMCSLSPQL SILLLFFTPP VLFSASVFGK QIRNTSKDLQ
EATGQLTRVA EEQLSGIKTV QSFVAEGNEL SRYNVAIRDI FQVGKTAAFT NAKFFTTTSL
LGDLSFLTVL AYGSYLVLQS QLSIGDLTAF MLYTEYTGNA VFGLSTFYSE IMQGAGAASR
LFELTDRKPS ISPTVGHKYK PDRGVIEFKD VSFSYPTRPS VQIFKNLNFK IAPGSSVCIV
GPSGRGKSTI ALLLLRYYNP TTGTITIDNQ DISKLNCKSL RRHIGIVQQE PVLMSGTIRD
NITYGLTYTP TKEEIRSVAK QCFCHNFITK FPNTYDTVIG PHGTLLSGGQ KQRIAIARAL
IKKPTILILD EATSALDVES EGAINYTFGQ LMKSKSMTIV SIAHRLSTIR RSENVIVLGH
DGSVVEMGKF KELYANPTSA LSQLLNEKAA PGPSDQQLQI EKVIEKEDLN ESKEHDDQKK
DDNDDNDNNH DNDSNNQSPE TKDNNSDDIE KSVEHLLKDA AKEANPIKIT PQP
