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Database: UniProt
Entry: B3RPL7_TRIAD
LinkDB: B3RPL7_TRIAD
Original site: B3RPL7_TRIAD 
ID   B3RPL7_TRIAD            Unreviewed;       836 AA.
AC   B3RPL7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=TRIADDRAFT_63669 {ECO:0000313|EMBL:EDV28211.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV28211.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28211.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B.,
RA   Dellaporta S.L., Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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; DS985242; EDV28211.1; -; Genomic_DNA.
DR   RefSeq; XP_002110045.1; XM_002110009.1.
DR   STRING; 10228.TriadP63669; -.
DR   EnsemblMetazoa; TriadT63669; TriadP63669; TriadG63669.
DR   GeneID; 6750707; -.
DR   KEGG; tad:TRIADDRAFT_63669; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; B3RPL7; -.
DR   KO; K02154; -.
DR   OMA; LGTQNFG; -.
DR   OrthoDB; EOG091G01BI; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009022};
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:UP000009022};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    407    431       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    543    563       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    578    598       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    636    655       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       94    121       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   836 AA;  95308 MW;  B30900E5B29D67C4 CRC64;
     MGSLFRSEAM TLCQLFLQSE AAYACVSELG ELGLVQFRDL NPDVNIFQRK FVNEVRRCEE
     MERKLRFVYK EIERASIPMV DTGDIPDAPP PREMIDLEST FEQLENEMKE INSNQEALNK
     NFLELTELKF ILRKTQTFFD EVENNQITAD QPNNDDQQAL LAEEGKTIQA AKRLSFVTGV
     IQRESLPGFE RLLWRACRGN VFLRTAEIET PLEDPRTGDS IIKCVFIIFF QGEQLRLRIK
     KICEGFKATL YPCPENAAER REMAIGVMTR IEDLQVVLNQ TKEHRNTVLG AAAKNINPWI
     IKVKKIKGIY HALNMFNLDV THKCLIAECW CAVDDLDRIH QALKRGSEKS GSTVPSILNR
     METKESPPTY NITNKFTNGF QNIVDAYGVA DYQEVNPAPF AIVTFPFLFG VMFGDSGHGT
     LMFLFGLYLV LKEKSIAKIK GGEMVDTVFG GRYIILLMGI CAIYTGTIYN DWFSRSLNIF
     GSQWYFSNVT LSDEFVRTHS DIQLNPKTAF HNQTPYPVGL DPIWQLAVNK LTFTNSFKMK
     MSVILGIFQM SFGVVLSLLN HLYFKRTVNI YCEFIPEVIF LGCIFGYMIG LIFFKWLAFT
     CYSEFQPSIL LAMIDMFLNF GATIPKDSLL YAGQGVLQPI LVALAVVAVP WMLLVKPLYL
     RREHQKAMAA KGSTVRYDTT SETAPIVKSE EPPEGVEHNE QKEEPEEEEE FDFGEIFVHQ
     AIHTIEYCLG CISNTASYLR LWALSLAHAE LSEVLWVMVL KIGFSTNGYA GFVVTWFMFG
     GWAALTIAIL LIMEGLSAFL HALRLHWVEF QNKFYDGQGM PFQPFSFVRI MKAEEE
//
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