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Database: UniProt
Entry: G1Q6M8_MYOLU
LinkDB: G1Q6M8_MYOLU
Original site: G1Q6M8_MYOLU 
ID   G1Q6M8_MYOLU            Unreviewed;       499 AA.
AC   G1Q6M8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   20-DEC-2017, entry version 28.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=LOC102435006 {ECO:0000313|Ensembl:ENSMLUP00000019361};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019361, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000019361, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000019361}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU361189}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSMLUP00000019361}.
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DR   EMBL; AAPE02058120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000019361; -.
DR   Ensembl; ENSMLUT00000025711; ENSMLUP00000019361; ENSMLUG00000023194.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   InParanoid; G1Q6M8; -.
DR   OMA; CPVSDLP; -.
DR   OrthoDB; EOG091G01BI; -.
DR   TreeFam; TF300346; -.
DR   Proteomes; UP000001074; 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; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001074};
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:UP000001074};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    409    432       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    453    472       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       58     78       {ECO:0000256|SAM:Coils}.
FT   COILED       93    127       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   499 AA;  57774 MW;  2551397C53ADD7C5 CRC64;
     MASVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NVDVNSFQRK FVNEVRRCES
     MERILRFLED EIKNEIEVQW LEKSPPTPLP REMISLETVL EKLEGELQEA NQNHQALKKS
     FLELTELKYL LKKTQDFFEN GQDRSVSQNS WFEQIWDLDT SGLLELRAMP AYMAGKLGFT
     AGVINRERMA SFERLLWRVC RGNIYLKFSE MDTVLEDPVT DLKMTWDMFI IFYQGEQLRQ
     KIRKICEGFR ATIYPCPEPA AERKEMLAGI NTRLEDLVTV ITQTESHRQS LLQEAAANWH
     SWVVKVQKMK AIYHILNMCN IDVTQQCIIA EIWFPVADTR IKKALEQGME LSGSSMAPIL
     TAVQSKTAPP TFNRTNKFTA GFQNIVDAYG VGNYREINPA PYTIITFPFL FAVMFGDCGH
     GTVMLLAALW MVRNERRFLA QKTDNEIWNT FFQGRYLILL MGIFSIYTGF IYNDCFSKAF
     NIFGSSWSVR PMFRNGTWK
//
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