GenomeNet

Database: UniProt
Entry: Q201X8_ACYPI
LinkDB: Q201X8_ACYPI
Original site: Q201X8_ACYPI 
ID   Q201X8_ACYPI            Unreviewed;       122 AA.
AC   Q201X8;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=V-type proton ATPase subunit F {ECO:0000256|PIRNR:PIRNR015945};
GN   Name=ACYPI000082 {ECO:0000313|EMBL:BAH71421.1};
GN   Synonyms=100145840 {ECO:0000313|EnsemblMetazoa:NP_001119690.1};
OS   Acyrthosiphon pisum (Pea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX   NCBI_TaxID=7029 {ECO:0000313|EMBL:ABD72676.1};
RN   [1] {ECO:0000313|EMBL:ABD72676.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WHAP0081 {ECO:0000313|EMBL:ABD72676.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:ABD72676.1};
RA   Hunter W.B., Stern D.L., Hunnicutt L.E.;
RT   "Expressed genes of the pea aphid, Acyrthosiphon pisum.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH71421.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LSR1 {ECO:0000313|EMBL:BAH71421.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAH71421.1};
RA   Shigenobu S., Nakabachi A., Richards S.;
RT   "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000007819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA   Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA   Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA   Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA   Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA   Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA   Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA   Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA   Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA   Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA   Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA   Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA   James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA   Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA   Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA   Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA   Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA   Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA   Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA   Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA   Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA   Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA   Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA   Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA   Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA   Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA   Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA   Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA   Weinstock G., Gibbs R.A.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblMetazoa:NP_001119690.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment.
CC       {ECO:0000256|ARBA:ARBA00029379}.
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments. {ECO:0000256|PIRNR:PIRNR015945}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2.
CC       {ECO:0000256|ARBA:ARBA00029469}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family.
CC       {ECO:0000256|ARBA:ARBA00010148, ECO:0000256|PIRNR:PIRNR015945}.
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DR   EMBL; DQ413208; ABD72676.1; -; mRNA.
DR   EMBL; AK340910; BAH71421.1; -; mRNA.
DR   RefSeq; NP_001119690.1; NM_001126218.2.
DR   AlphaFoldDB; Q201X8; -.
DR   STRING; 7029.Q201X8; -.
DR   EnsemblMetazoa; NM_001126218.2; NP_001119690.1; GeneID_100145840.
DR   GeneID; 100145840; -.
DR   KEGG; api:100145840; -.
DR   CTD; 100145840; -.
DR   eggNOG; KOG3432; Eukaryota.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; Q201X8; -.
DR   OMA; INQNYAE; -.
DR   OrthoDB; 275186at2759; -.
DR   Proteomes; UP000007819; Unassembled WGS sequence.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 3.40.50.10580; ATPase, V1 complex, subunit F; 1.
DR   InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR   InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR   InterPro; IPR036906; ATPase_V1_fsu_sf.
DR   NCBIfam; TIGR01101; V_ATP_synt_F; 1.
DR   PANTHER; PTHR13861:SF2; V-TYPE PROTON ATPASE SUBUNIT F; 1.
DR   PANTHER; PTHR13861; VACUOLAR ATP SYNTHASE SUBUNIT F; 1.
DR   Pfam; PF01990; ATP-synt_F; 1.
DR   PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR   SUPFAM; SSF159468; AtpF-like; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|PIRNR:PIRNR015945};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|PIRNR:PIRNR015945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007819};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR015945}.
SQ   SEQUENCE   122 AA;  13550 MW;  0EF0D8D72EDE4F7A CRC64;
     MAMHSAVKGK LLAVIGDEDT CVGFLLGGVG EINKHRHSNF MVVDKNTAII DIEECFKGFV
     KRDDIDIILI NQNVAEMIRH VIEGHTQPIP AVLEIPSKDH PYDASKDSIL RRAKGMFNPE
     DV
//
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