ID A0A3B4AIH3_9GOBI Unreviewed; 849 AA.
AC A0A3B4AIH3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000016409.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000016409.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3B4AIH3; -.
DR STRING; 409849.ENSPMGP00000016409; -.
DR Ensembl; ENSPMGT00000017518.1; ENSPMGP00000016409.1; ENSPMGG00000013473.1.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000261520; Unplaced.
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:SF22; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 2; 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 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 409..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 454..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 548..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 578..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 644..667
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 779..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 94..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 849 AA; 97710 MW; A4D61D56609BA6C2 CRC64;
MNSLLRSEEM CLAQLFLQSG SAYDCISELG ELGLVEFRDL NPSVNAFQRK HVNEIKKCEE
MERILSYLLR EIKKADISLP EGDVNPAAPL PKHVIAIMEQ LQRLEVELGE VTRNKEKLQK
NLLELTEYTH MLRITRNFVQ KSSERESLQV QYEEFPFLEK ETMMDYSSMQ RLGAKLGFIS
GLIHRVKIEA FERMLWRVCK GYTILSYAEL DEYLDDPDTG EPTKSVVFLI SYWGEQIGQK
VKKICDCYHC HLYPYPSNNE ERNDVVEGLK TRIQDLHIVL HRTEEYLKQV LIRASESVYT
WVLQIKKMKA IYYVLNQCSF DVTNKCLIAE VWCPVNDLPA LRRALEEGSR KSGATVPSFV
NRIPTSDTPP SLIRTNKFTS GFQNIVDAYG VCSYREVNPA PFTIITFPFL FAVMFGDLGH
GIIMALFAFW MVFYENDRKL KNTRNEIWNT FFEGRYIILM MGLFSVYTGF IYNDCFSKSL
NIFGSKWNVS AMIEAKIWKR EDILGNRALT LDPNVTGVFT GPYPFGIDPI WNLATNRLTF
LNSYKMKMSV ILGIIHMSFG VILSTFNHLH FRKSYNLYLV LLPELLFLLC LFGYLVFMIL
YKWLAFSAKD SRHAPSILIH FINMFLMQGD ATQPLYAGQN GLQIFLLLIA VLSVPVLLMG
KPLYLYWLSK GHHRIGAYRG YERVRHDSDE ELYLLRAHDM EEGSSHSEVS MSGEHQSEEF
NFADEFLHQA IHTIEYCLGC ISNTASYLRL WALSLAHAQL SEVLWAMVMR VGLKMDTSLG
VLFLVPVFGL FAVLTVSILL VMEGLSAFLH ALRLHWVEFQ NKFYSGSGVK FVPFSFSLMP
SSFDNDGLL
//