ID   A0A1R2ASC5_9CILI        Unreviewed;       793 AA.
AC   A0A1R2ASC5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=SteCoe_35412 {ECO:0000313|EMBL:OMJ67431.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ67431.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ67431.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ67431.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a
CC       multimeric enzyme that catalyzes the translocation of protons across
CC       the membranes. Required for assembly and activity of the V-ATPase.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ67431.1}.
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DR   EMBL; MPUH01001500; OMJ67431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2ASC5; -.
DR   OrthoDB; 180022at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 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   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM        398..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        442..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        510..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        541..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        616..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          50..77
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   793 AA;  91386 MW;  F80058EF374C1888 CRC64;
     MGFLRSEEMG YYSIVIPNDQ AWEVLNQLGK LSAVQFVDQN SDQAVFNRRY ASYIRRCEEA
     ERRLRFLAQE QERFKVQVMF PKDSNLVLDM IDGDLRINKI PAQTHFETLE NDLQNYEDSM
     ILQLKNFEQL TTGMEFLKEK KVVLSKAREA FNIEGQLGGS LFSRIAGIIE NEDINRFKRM
     VFRITRGNAL SVFSDIKDNE EDAKKKIVHQ KSVFFIMYQG DQSGNISTRL GRICDTIGIR
     RYALPNDAGS LDEEWKHNED EIVANADILE KTKQAIINLL RKLATPKGES PCSLIEEIRL
     FVLKEKSIYH SLNMFSLKGN MFYGSCWCPK SDEQRILHAL SAGFLKEIEG GFPHNQKPPT
     YFRLNDFTQP FQNIVDTYGI PAYQEANPAF FSAVTFPFLF GIMFGDVGHG LVLTIFATYL
     CWAEKSIVQS GGLFKPAVPV RYLLLMMGLC ATYCGFIYND FLGIPFNFFG SRWDDKDIYY
     DQYIQSSTYP FGFDPVWYRS KNELIFFNSF KMKLSVVFGV IQMICGNFFK GANAIHFKSK
     INFFFEFIPQ LVFMCGIFGY MIIMVFIKWC TSWNYNFGDT APNLITVLMN MFLKLGKLDD
     SKDRTLWGDK EGQEQLQLIL LLVSVLCVPI MLFPKPIILN HMYKKQQHGG KEAGYEEFDE
     ENHGEKDHSF GELFIHQMIE TIEYVLGAVS NTASYLRLWA LSLAHAQLSS VFFEKALVST
     IEMGNPVAVV IGFFLFANIS VGVLMCMDSL ECFLHALRLH WVEFMNKFYK GDGIKFQPFS
     FDLVIKVYES KKQ
//