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Database: UniProt
Entry: Q4U8W2_THEAN
LinkDB: Q4U8W2_THEAN
Original site: Q4U8W2_THEAN 
ID   Q4U8W2_THEAN            Unreviewed;       936 AA.
AC   Q4U8W2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=TA10280 {ECO:0000313|EMBL:CAI76741.1};
OS   Theileria annulata.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76741.1, ECO:0000313|Proteomes:UP000001950};
RN   [1] {ECO:0000313|EMBL:CAI76741.1, ECO:0000313|Proteomes:UP000001950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M.,
RA   Coulson R.M.R., Cronin A., de Villiers E.P., Fraser A., Fosker N.,
RA   Gardner M., Goble A., Griffiths-Jones S., Harris D.E., Katzer F.,
RA   Larke N., Lord A., Maser P., McKellar S., Mooney P., Morton F.,
RA   Nene V., O'Neil S., Price C., Quail M.A., Rabbinowitsch E.,
RA   Rawlings N.D., Rutter S., Saunders D., Seeger K., Shah T., Squares R.,
RA   Squares S., Tivey A., Walker A.R., Woodward J., Dobbelaere D.A.E.,
RA   Langsley G., Rajandream M.A., McKeever D., Shiels B., Tait A.,
RA   Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata
RT   compared with T. parva.";
RL   Science 309:131-133(2005).
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; CR940353; CAI76741.1; -; Genomic_DNA.
DR   RefSeq; XP_953366.1; XM_948273.1.
DR   STRING; 353154.XP_953366.1; -.
DR   EnsemblProtists; CAI76741; CAI76741; TA10280.
DR   GeneID; 3862621; -.
DR   KEGG; tan:TA10280; -.
DR   EuPathDB; PiroplasmaDB:TA10280; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q4U8W2; -.
DR   KO; K02154; -.
DR   Proteomes; UP000001950; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar 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   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001950};
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:UP000001950};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    467    492       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    513    530       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    599    621       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    628    651       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    696    720       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    864    887       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   936 AA;  107991 MW;  DB2A16FF235DBE3B CRC64;
     MGIFRSETMV HGTLVIPHER ARSCIDLLSR HTNIQYIDMN ERRMDRPYKK YVQRIDHMER
     MIRVLYEEIA KLPNSKIVRH NIDNFLEHDN MYRLDQVEES LVKLYDQFQM FKENDSLLRL
     ERDEALSEYY VLLVASKQLS LITPDRSFSD IPNTISLPVT NLDESSDSRE HLLNDNTQSD
     TEMINLSPYD LSSRTSSSIS FTNIAGLISS QEKEAFSRAI FRAMRGNVFT LLHDTTDLRA
     MVLSKGLVDQ EELDADNDKT VFVIYCQSSN NNATYNKIKK LCTGFQAKLF NWCKTQSELA
     PRLKTLEDVI KDKKRALEAY KEYFRSEIAC LLEVIRPGGN SVIEEWFLFC KKEKYLYYIL
     NHFEGSDITL RADCWFPADE EEKIREHLLA EKASGSVSAL LLVDIQAPFV SVHPLHPGSH
     ENLSHIPPTY NKTNKISKSF QNVVDTYGIS RYKEVNPAPF TVMTFPFLFG LMFGDIAHGF
     CVILFALFLI LYYRKLKRKF SGDIANMILE GRYMILLMGI MATYAGFIYN DFLSLPNSFF
     GTGWVSNGTP PEGGSESDGT YVETLVKSAK NFPVVFGLDS AWIGAVNEQS VLHSFKMKFS
     VIFGFFQMTL GIVLKGFNAI YFSSVLDFFF EFVPQLAMMC SFVGYMNFLI FHKWLTPVDS
     GYAKPSIITT LIDMCMMKTL EPHEIMYEGQ QTVQRVLMII LILSVPMMLI PKPLILYFTI
     KKQGRTRTNN NSTRDYEMVY CGPEEEDLEA IARENVPNYP HRRSSLDLGV DKFKKVDAKN
     KDNQFSVTIQ KDENEAVPSE PHHAPKLSEL FIHQFIETIE FTLGTISNTA SYLRLWALSL
     SHQQLSLVLF KQLILNCLDS STSLFVMIFG LFIRSIFFSV FTFFIMLCMD SLECYLHALR
     LQWVEFQNKF FKADGRFFRP FNIKLLLDDP TIMEPK
//
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