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YLH47_YEAST
ID   YLH47_YEAST             Reviewed;         454 AA.
AC   Q06493; D6W4C3; P89103;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=LETM1 domain-containing protein YLH47, mitochondrial;
DE   AltName: Full=LETM1 homolog;
DE   Flags: Precursor;
GN   Name=YLH47; Synonyms=MRS7; OrderedLocusNames=YPR125W;
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 44774 / DBY747;
RX   PubMed=8252639; DOI=10.1007/bf00336780;
RA   Waldherr M., Ragnini A., Jank B., Teply R., Wiesenberger G., Schweyen R.J.;
RT   "A multitude of suppressors of group II intron-splicing defects in yeast.";
RL   Curr. Genet. 24:301-306(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 44774 / DBY747;
RA   Teply R.;
RT   "Isolation and characterisation of suppressors of mrs2-1 mutation in
RT   saccharomyces cerevisiae.";
RL   Thesis (1996), Vienna Biocenter, Austria.
RN   [3]
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   [4]
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   [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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15138253; DOI=10.1074/jbc.m403607200;
RA   Nowikovsky K., Froschauer E.M., Zsurka G., Samaj J., Reipert S.,
RA   Kolisek M., Wiesenberger G., Schweyen R.J.;
RT   "The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+
RT   homeostasis with a potential role in the Wolf-Hirschhorn syndrome.";
RL   J. Biol. Chem. 279:30307-30315(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE MITOCHONDRIAL RIBOSOMES.
RX   PubMed=16476776; DOI=10.1083/jcb.200505060;
RA   Frazier A.E., Taylor R.D., Mick D.U., Warscheid B., Stoepel N., Meyer H.E.,
RA   Ryan M.T., Guiard B., Rehling P.;
RT   "Mdm38 interacts with ribosomes and is a component of the mitochondrial
RT   protein export machinery.";
RL   J. Cell Biol. 172:553-564(2006).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
CC   -!- FUNCTION: Involved in mitochondrial potassium homeostasis through the
CC       mitochondrial K(+)/H(+) exchange regulation. {ECO:0000250,
CC       ECO:0000269|PubMed:15138253}.
CC   -!- SUBUNIT: Associates with the mitochondrial ribosomes.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15138253,
CC       ECO:0000269|PubMed:16476776, ECO:0000269|PubMed:16823961}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:16476776,
CC       ECO:0000269|PubMed:16823961}.
CC   -!- MISCELLANEOUS: Present with 11300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U48418; AAB70096.1; -; Genomic_DNA.
DR   EMBL; U40828; AAB68065.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11539.1; -; Genomic_DNA.
DR   PIR; S69017; S69017.
DR   RefSeq; NP_015450.1; NM_001184222.1.
DR   AlphaFoldDB; Q06493; -.
DR   SMR; Q06493; -.
DR   BioGRID; 36293; 101.
DR   DIP; DIP-5345N; -.
DR   IntAct; Q06493; 5.
DR   MINT; Q06493; -.
DR   STRING; 4932.YPR125W; -.
DR   TCDB; 2.A.97.1.4; the mitochondrial inner membrane k(+)/h(+) and ca(2+)/h(+) exchanger (letm1) family.
DR   MaxQB; Q06493; -.
DR   PaxDb; Q06493; -.
DR   PRIDE; Q06493; -.
DR   EnsemblFungi; YPR125W_mRNA; YPR125W; YPR125W.
DR   GeneID; 856243; -.
DR   KEGG; sce:YPR125W; -.
DR   SGD; S000006329; YLH47.
DR   VEuPathDB; FungiDB:YPR125W; -.
DR   eggNOG; KOG1043; Eukaryota.
DR   GeneTree; ENSGT00950000183167; -.
DR   HOGENOM; CLU_008958_5_0_1; -.
DR   InParanoid; Q06493; -.
DR   OMA; LSNAFMY; -.
DR   BioCyc; YEAST:G3O-34263-MON; -.
DR   PRO; PR:Q06493; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06493; 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:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; IGI:SGD.
DR   GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
DR   GO; GO:1902600; P:proton transmembrane transport; IGI:SGD.
DR   InterPro; IPR011685; LETM1-like.
DR   InterPro; IPR044202; LETM1/MDM38-like.
DR   InterPro; IPR033122; LETM1_RBD.
DR   PANTHER; PTHR14009; PTHR14009; 1.
DR   Pfam; PF07766; LETM1; 1.
DR   PROSITE; PS51758; LETM1_RBD; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..454
FT                   /note="LETM1 domain-containing protein YLH47,
FT                   mitochondrial"
FT                   /id="PRO_0000244478"
FT   TOPO_DOM        46..136
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..454
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          177..371
FT                   /note="Letm1 RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          376..423
FT                   /evidence="ECO:0000255"
FT   CONFLICT        265
FT                   /note="G -> R (in Ref. 1 and 2; AAB70096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="P -> L (in Ref. 1 and 2; AAB70096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="T -> S (in Ref. 1 and 2; AAB70096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  52174 MW;  351907A14B39841A CRC64;
     MLKYRSLPIK RAIHHPAPGI TPISPRIMVS RLRVIPSFNL KFNRWNSSVP ESSKKELKTT
     DGNQESASKV SPVKEKEKVP FKVKMQKALR HYWDGSKLLG LEIKISSKLL MKSAAGYPLT
     RRENLQLKRT TQDIVRLVPF AAFLIIPFAE LLLPFALKLF PNLLPSTYES SKKRENKLEN
     LRNTRKLMSE IIKNNKSHFK PNNISEEQKA LFNRFYTHVR ATGVPESRQQ LIEVARLFTD
     DTVLDNVTRP YLIALAKYMN LQPFGTDVML RYRIRYKMLE LKKDDLSIYY EDAEQLSLSE
     LKTACASRGI RSVDVEPSVL YSNLRLWLNM RLKDKIPSTL LIMATAYNYG NVQSKESLYD
     ALCDVLIGIP DELYHEVKVN VVKEDEASAK QKLKQLREQE EIMKEEEQQE ENAIVSVKDE
     LSLDDQDKNI DAAAPDVKPH DTKPIGEAAA IKEK
 
 
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