ID A0A182PQQ1_9DIPT Unreviewed; 1285 AA.
AC A0A182PQQ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI009282-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI009282-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI009282-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR STRING; 199890.A0A182PQQ1; -.
DR EnsemblMetazoa; AEPI009282-RA; AEPI009282-PA; AEPI009282.
DR VEuPathDB; VectorBase:AEPI009282; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0033179; C: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 PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 834..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1077..1096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1213..1238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 485..562
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 144377 MW; DAC7CFD68A401937 CRC64;
MSARSHRGLY RRKQPSTDER SKSFDQSALS DYDDEEGSDT LTELSRESLT SSQGRSSIGS
IPWAEDAIKQ NQTEWERIDR MFYGEEDLPS DAKLRDEILE WTSVFPFLRV TGKPIAIVES
VHAKGNDPFY EETFLVDPPL PSRTRSSRSG REGAGKQLAR DVECLLTSCD LDKCLCISSG
QTLRSSNQQQ QQQQPAPVQT KAGRRSGTDR GAPELLDRVE NRLIKVKPLN SLLVPQVPVV
SVGSYGLLIS NYHHCVGPGV GYQALSGGSR NCSAQSVTRL CHNADTSSYG VGGRSRNGNL
QRKLAPLPHR PPQQQQHHSH QKSAKTIDSA ILSASATHNR IPPLTKNYKF LVQNSYVAPT
LLAEIEQRHH SKLNVVKSAT TRYMASSPTN HLFALPALTG IDGLVRHNPV TGDAALQRSP
GKNPRVFRSE ESGTMGSLFR SEEMSLCQLF LQSEAAYACV SELGELGLVQ FRDLNPDVNA
FQRKFVNEVR RCDEMERKLR YLEKEIKKDG IPMLDTGESP EAPQPREMID LEATFEKLEN
ELREVNQNAE ALKRNYLELT ELKHILRKTQ VFFDEQEGGM HTTESMTRAL ITDESRTGKA
MGPVQLGFVA GVILRERLPA FERMLWRACR GNVFLRQAMI EDPLEDPSNG DKVYKSVFII
FFQGDQLKTR VKKICEGFRA TLYPCPEAPT DRREMAMGVM TRIEDLHTVL GQTQDHRHRV
LVAAAKNLKN WFVKVRKIKA IYHTLNLFNL DVTQKCLIAE CWVPLLDFET IQIALRRGTE
RSGSSVPPIL NRMETFEDPP TYNRTNKFTH AFQALINAYG VASYREMNPA PYTIITFPFL
FAVMFGDLGH GTIMALFGLW MVLKEKPLAA KKSDNEIWNI FFGGRYIIFL MGVFSMYTGF
VYNDIFSKSL NVFGSAWSIN YNTSTVMTNK ALQLDPAGKD YAQTPYPIGL DPVWQVAPLN
KIIFQNAYKM KISIIFGVIH MLFGVFVGLF NHRYFKNKMA IYCEFIPQVI FLVFLFFYMT
LLMFIKWVKY SASSESVSHS AGCAPSILIT FINMVLFKAP DENTGDCSPF MFAGQQGLQK
FLVVVALLCV PWMLLAKPIL IMRGRKEAAH QPIAPYNNEN GDADGLNQHN NAVGTQGGQP
PAQQQSGGGG HGHDNEEMSE IFIHQGIHTI EYVLGSVSHT ASYLRLWALS LAHAQLAEVL
WNMVLQNGLK QDGWIGGIAL WAVFAFWAVL TVGILVLMEG LSAFLHTLRL HWVEFQSKFY
AGLGYAFQPF SFEVILESSS SSSEE
//
