ID C9W1E1_RHISA Unreviewed; 85 AA.
AC C9W1E1;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
OS Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Rhipicephalus.
OX NCBI_TaxID=34632 {ECO:0000313|EMBL:ACX53888.1};
RN [1] {ECO:0000313|EMBL:ACX53888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:ACX53888.1};
RX PubMed=20650005; DOI=10.1186/1471-2164-11-450;
RA Anatriello E., Ribeiro J.M., de Miranda-Santos I.K., Brandao L.G.,
RA Anderson J.M., Valenzuela J.G., Maruyama S.R., Silva J.S., Ferreira B.R.;
RT "An insight into the sialotranscriptome of the brown dog tick,
RT Rhipicephalus sanguineus.";
RL BMC Genomics 11:450-450(2010).
RN [2] {ECO:0000313|EMBL:ACX53888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:ACX53888.1};
RX PubMed=24029695; DOI=10.1016/j.ttbdis.2013.05.001;
RA Oliveira C.J., Anatriello E., de Miranda-Santos I.K., Francischetti I.M.,
RA Sa-Nunes A., Ferreira B.R., Ribeiro J.M.;
RT "Proteome of Rhipicephalus sanguineus tick saliva induced by the
RT secretagogues pilocarpine and dopamine.";
RL Ticks Tick Borne Dis. 4:469-477(2013).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane.
CC {ECO:0000256|RuleBase:RU367005}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel.
CC {ECO:0000256|RuleBase:RU367005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU367005}.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family.
CC {ECO:0000256|ARBA:ARBA00007333, ECO:0000256|RuleBase:RU367005}.
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DR EMBL; EZ406089; ACX53888.1; -; mRNA.
DR EMBL; EZ406131; ACX53928.1; -; mRNA.
DR AlphaFoldDB; C9W1E1; -.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; ATP SYNTHASE E CHAIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12427:SF1; ATP SYNTHASE SUBUNIT E, MITOCHONDRIAL; 1.
DR Pfam; PF05680; ATP-synt_E; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU367005};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU367005};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU367005};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU367005}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367005};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU367005};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
SQ SEQUENCE 85 AA; 9768 MW; 4A70D8623A356C3D CRC64;
MVELAPPVSV SPFIRACRWG FLTAGIFYGA FNYRRLSRKE ASIREYEAKQ MEMLKGKREA
EKQMKAREEM ITLAKDVGVP VPPNF
//
