ID V5IFE7_IXORI Unreviewed; 93 AA.
AC V5IFE7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB75901.1};
RN [1] {ECO:0000313|EMBL:JAB75901.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB75901.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
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; GANP01008567; JAB75901.1; -; mRNA.
DR AlphaFoldDB; V5IFE7; -.
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}.
FT REGION 53..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 93 AA; 10943 MW; A9AC15F8CA7283E3 CRC64;
MVELAPPVAV SPFIRACRWG ALTAGVFYGA YHFRRLSRKE TKLREYEAQQ MELMREKREE
EKKEEKQEEG NRLDPGLKDN RTPRIPRTLA SHL
//
