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Database: UniProt
Entry: S7PQL8_MYOBR
LinkDB: S7PQL8_MYOBR
Original site: S7PQL8_MYOBR 
ID   S7PQL8_MYOBR            Unreviewed;       584 AA.
AC   S7PQL8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 9.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=D623_10020726 {ECO:0000313|EMBL:EPQ13163.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ13163.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D.,
RA   Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N.,
RA   Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A.,
RA   Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; KE163676; EPQ13163.1; -; Genomic_DNA.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   PANTHER; PTHR11629; PTHR11629; 2.
DR   Pfam; PF01496; V_ATPase_I; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000052978};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    182    210       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    230    250       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    329    350       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    356    380       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    515    540       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   584 AA;  67053 MW;  C19A19A240288DF6 CRC64;
     MKKNMFIIFY QGEQLRQKIR KICEGFRATI YPCPEPAAER KEMLAGINTR LEDLVTVITQ
     TESHRQSLLQ EAAANWHSWV VKVQKMKAIY HILNMCNIDV TQQCIIAEIW FPVADTGRIK
     KALEQGMELS GSSMAPILTA VQSKTAPPTF NRTNKFTAGF QNIVDAYGVG NYREMNPAPY
     TIITFPFLFA VMFGDCGHGT VMLLAALWMV RNERRFLAQK TDNEIWNTFF QGRYLILLMG
     IFSIYTGFIY NDCFSKAFNI FGSSWSVRPM FRNGTWNMET METNPLLQLN PAIPGVYSGN
     PYPFGIDPIW NLASNKLTFL NSYKMKMSVI LGIVQMTFGV ILSLFNHIYF RKTLNILLQF
     IPEMIFMLCL FGYLVFMIIF KWCYYDVHVS QKAPSILIHF INMFMFNYND PSNAPLYKHQ
     LQASMIQEHT AEDIEGDNSS PPRRADAHRA QEDYEEEFNF GDIFVHQAIH TIEYCLGCIS
     NTASYLRLWA LSLAHAELSE VLWTMVMNIG LRLRGWGGLI GVFIIFAVFA VLTVAILLIM
     EGLSAFLHAL RLHWVEFQNK FYVGAGYKFS PFSFKNILDG TVEE
//
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