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Database: UniProt
Entry: A7TP94_VANPO
LinkDB: A7TP94_VANPO
Original site: A7TP94_VANPO 
ID   A7TP94_VANPO            Unreviewed;       872 AA.
AC   A7TP94;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   20-DEC-2017, entry version 43.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=Kpol_1019p1 {ECO:0000313|EMBL:EDO15881.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15881.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480440; EDO15881.1; -; Genomic_DNA.
DR   RefSeq; XP_001643739.1; XM_001643689.1.
DR   STRING; 436907.XP_001643739.1; -.
DR   EnsemblFungi; EDO15881; EDO15881; Kpol_1019p1.
DR   GeneID; 5544001; -.
DR   KEGG; vpo:Kpol_1019p1; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   InParanoid; A7TP94; -.
DR   KO; K02154; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   PhylomeDB; A7TP94; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IEA:EnsemblFungi.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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:UP000000267};
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:UP000000267};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    460    483       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    504    522       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    582    602       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    614    634       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    675    694       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    778    798       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    810    833       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      130    150       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   872 AA;  100197 MW;  7427D0808A9B8D93 CRC64;
     MFQEEAIFRS ADMAYIQLYI PLEISREIVS MLGNLGNVMF RDLNSNLTAF QRGYVSHLQR
     YNDIERLLNY LGEVSVKHSE AVWKYTLHVD EQGNDIETPH ISQIIAELDV NSQDAINDVM
     DDIISFESRV KQLDDSLVQL KIKLNDLIEQ RYVFFECGRF LEANTGLAGR LSRDNMDAND
     FRLNSDDLSD NLSEAFSFDD DTVANTDLEE GLLRNDLARD EEIEVFDQVG FNNNFMIVGS
     IKRSKVELLN RIVWRLLRGN LFFQNFSIDE TLLENGEKVE KDCFIIFTHG ETLLKKVKRV
     VESLEGHIYP MEDRSHDRIQ ELNTQINDVQ QIVYATEQTL HTELLVVNDQ LPKWTALVKR
     EKYIYATLNL FKDQSQGLLA EGWVPASEMM LVSNSLKEHG EQIGSEYTPV INVIQTNKTP
     PTYHRTNKFT GAFQSIVDAY GIASYKEINP GLATIVTFPF MFAIMFGDAG HGFILLLIAL
     FLIMNEKKFE AMQREEIFDM AFTGRYMICL MGFFSIYTGL MYNDVFSKSM TLFKSGWEWP
     SSFKKGESIE ATKVGVYPFG LDFAWHGTDN NLIFTNSYKM KLSILMGFIH MSYSYLFSYV
     NFKYKNSKVD IIGNFLPGLI FMQSIFGYLS WAILYKWTRD WIKEGKPAPN LLNMLINMFL
     APGTVSEQLY KGQSFIQMVL LIAALVCVPW LLLYKPLMLR KQHNQAQLQG YQNINEQRVN
     ESLLDSQSNA GDEVIITEEF NKEDQHEFNF GDIVIHQVIH TIEFCLNCIS HTASYLRLWA
     LSLAHAQLST VLWDMTIANS FSSANSGSPF AVAKVVFLFG MWFVLTVCIL VLMEGTSAML
     HSLRLHWVEA MSKFFEGDGY AYEPFSFKKL SD
//
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