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Database: UniProt
Entry: A9SRI3_PHYPA
LinkDB: A9SRI3_PHYPA
Original site: A9SRI3_PHYPA 
ID   A9SRI3_PHYPA            Unreviewed;       820 AA.
AC   A9SRI3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   05-JUL-2017, entry version 38.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=PHYPADRAFT_214893 {ECO:0000313|EMBL:EDQ66245.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:EDQ66245.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y.,
RA   Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T.,
RA   Kuroki Y., Toyoda A., Suzuki Y., Hashimoto S.-I., Yamaguchi K.,
RA   Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N.,
RA   Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H.,
RA   Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K.,
RA   Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A.,
RA   Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T.,
RA   Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H.,
RA   Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J.,
RA   Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(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; DS544996; EDQ66245.1; -; Genomic_DNA.
DR   RefSeq; XP_001768891.1; XM_001768839.1.
DR   UniGene; Ppa.831; -.
DR   STRING; 3218.PP1S107_75V6.1; -.
DR   GeneID; 5932091; -.
DR   KEGG; ppp:PHYPADRAFT_214893; -.
DR   InParanoid; A9SRI3; -.
DR   KO; K02154; -.
DR   Proteomes; UP000006727; Partially assembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000325; C:plant-type vacuole; 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:UP000006727};
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:UP000006727};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    417    441       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    462    479       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    548    566       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    578    601       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    636    655       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    757    777       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       86    120       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   820 AA;  93326 MW;  331AF7FA88B299CA CRC64;
     MVAMDLFRSE EMTLVQLIIP AESAHDTVTY LAELGLLQFK DLNPERSPFQ RTYANQVKRC
     GEMSRKIRYF QDQITKSGRT AAYRPLRDKD IGVDELEAKL TDLEAELLEI NANTDKLQRT
     HSELTEFQLV LHKAGAFFSS VRNAANTVQQ RADIENGSSI GEAIDRPLLQ EQEMQTEPSK
     QARLGFITGV IPKIKAASFE RILFRATRGN MFLKQASIED AVVDPATGEK IEKTVFVIFF
     SGERAKTKIS KICDAFGANC YPFPEESSRQ GHMKTEVDNR LLDLQHTLDA GINHRDNVLN
     SIGNNLDQWT VMVRREKAVY HTLNMLSIDV TRKCLVAEGW CPVSAKPKIQ DALQRAAFVS
     NSQVNTIFQV LHTKESPPSY FETNKFTNAF QEIVEAYGVG RYQEANPGCF TIITFPFLFA
     VMFGDWGHGI CLLLGALYLV LNEKKLGSKK LGDIMEMAYG GRYVILLMAI FSIYTGFIYN
     EFFSVPFGFF GGSAYRCPDS QYSIESCPMA TTSGMEKWSY EPYAFGVDPI WHGSRSELPF
     TNSLKMKMSI LLGIAQMNLG ILLSYFNARY FRSALDVWYQ FIPQLLFLNA LFGYLSFLIV
     LKWCQGSKPD LYHVMIYMFL SPTEDLGENQ LFMGQTFVQI VLLLVALVAV PWMLFPKPLI
     LRKRHVQKMQ GRAYGMLRES DTESTDLEID GEHDEEEFEF GEVLVHQMIH TIEFVLGAVS
     NTASYLRLWA LSLAHAQLSA VFYDRVLMFA WGYTNPIIRL IGLIVFASVT FGVLLLMETL
     SAFLHALRLH WVEFQNKFYL GDGYKFQPFS FRTLSEEDDL
//
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