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MDL1_YEAST
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   03-AUG-2022, entry version 182.
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; 134.
DR   STRING; 4932.YLR188W; -.
DR   TCDB; 3.A.1.212.1; the atp-binding cassette (abc) superfamily.
DR   MaxQB; P33310; -.
DR   PaxDb; P33310; -.
DR   PRIDE; P33310; -.
DR   EnsemblFungi; YLR188W_mRNA; YLR188W; YLR188W.
DR   GeneID; 850885; -.
DR   KEGG; sce:YLR188W; -.
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; FNTLQMG; -.
DR   BioCyc; YEAST:G3O-32311-MON; -.
DR   PRO; PR:P33310; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P33310; 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; 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   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; 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; PTHR24221; PTHR24221; 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   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
 
 
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