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Database: UniProt
Entry: VPP1_PONAB
LinkDB: VPP1_PONAB
Original site: VPP1_PONAB 
ID   VPP1_PONAB              Reviewed;         837 AA.
AC   Q5R422;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   10-MAY-2017, entry version 62.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 1;
DE            Short=V-ATPase 116 kDa isoform a1;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN   Name=ATP6V0A1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for assembly and activity of the vacuolar
CC       ATPase. Potential role in differential targeting and regulation of
CC       the enzyme for a specific organelle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
CC       least thirteen different subunits. It has a membrane peripheral V1
CC       sector for ATP hydrolysis and an integral V0 for proton
CC       translocation. The V1 sector comprises subunits A-H, whereas V0
CC       includes subunits a, d, c, c', and c''. Interacts with SPAAR.
CC       {ECO:0000250|UniProtKB:Q93050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Melanosome
CC       {ECO:0000250}. Note=Coated vesicle. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; CR861438; CAH93494.1; -; mRNA.
DR   ProteinModelPortal; Q5R422; -.
DR   STRING; 9601.ENSPPYP00000009433; -.
DR   PRIDE; Q5R422; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOVERGEN; HBG014606; -.
DR   InParanoid; Q5R422; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasmic vesicle; Hydrogen ion transport;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    837       V-type proton ATPase 116 kDa subunit a
FT                                isoform 1.
FT                                /FTId=PRO_0000119213.
FT   TOPO_DOM      1    388       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    389    407       Helical. {ECO:0000255}.
FT   TOPO_DOM    408    409       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    410    426       Helical. {ECO:0000255}.
FT   TOPO_DOM    427    441       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    442    471       Helical. {ECO:0000255}.
FT   TOPO_DOM    472    534       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    535    554       Helical. {ECO:0000255}.
FT   TOPO_DOM    555    572       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    573    593       Helical. {ECO:0000255}.
FT   TOPO_DOM    594    638       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    639    658       Helical. {ECO:0000255}.
FT   TOPO_DOM    659    724       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    725    749       Helical. {ECO:0000255}.
FT   TOPO_DOM    750    770       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    771    809       Helical. {ECO:0000255}.
FT   TOPO_DOM    810    837       Cytoplasmic. {ECO:0000255}.
FT   MOD_RES     250    250       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Z1G4}.
FT   MOD_RES     360    360       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q93050}.
FT   MOD_RES     364    364       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q9Z1G4}.
SQ   SEQUENCE   837 AA;  96269 MW;  C817922275566D50 CRC64;
     MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
     MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
     NFLELTELKF ILRKTQQFFD EMADPDLLGE SSSLLEPSEM GRGTPLRLGF VAGVINRERI
     PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
     RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQMEDHRQ RVLQAAAKNI RVWFIKVRKM
     KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
     PPTYNKTNKF TYGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
     VWMVLRESRI LSQKNENEMF STVFSGRYII LLMGVFSMYT GLIYNDCFSK SLNIFGSSWS
     VRPMFTYNWT EETLRGNPVL QLNPALPGVF GGPYPFGIDP IWNIATNKLT FLNSFKMKMS
     VILGIIHMLF GVSLSLFNHI YFKKPLNIYF GFIPEIIFMT SLFGYLVILI FYKWTAYDAH
     TSENAPSLLI HFINMFLFSY PESGYSMLYS GQKGIQCFLV VVALLCVPWM LLFKPLVLRR
     QYLRRKHLGT LNFGGIRVGN GPTEEDAEII QHDQLSTHSE DADEPTEDEV FDFGATMVHQ
     AIHTIEYCLG CISNTASYLR LWALSLAHAQ LSEVLWTMVI HIGLSVKSLA GGLVLFFFFT
     AFATLTVAIL LIMEGLSAFL HALRLHWVEF QNKFYSGTGF KFLPFSFEHI REGKFGE
//
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