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Database: UniProt
Entry: A0A0C7N2Z0_9SACH
LinkDB: A0A0C7N2Z0_9SACH
Original site: A0A0C7N2Z0_9SACH 
ID   A0A0C7N2Z0_9SACH        Unreviewed;        92 AA.
AC   A0A0C7N2Z0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
GN   ORFNames=LALA0_S05e04126g {ECO:0000313|EMBL:CEP62370.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62370.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP62370.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62370.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; LN736364; CEP62370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N2Z0; -.
DR   STRING; 1245769.A0A0C7N2Z0; -.
DR   HOGENOM; CLU_159435_1_0_1; -.
DR   OrthoDB; 2043243at2759; -.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
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   Pfam; PF05680; ATP-synt_E; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..92
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002195480"
SQ   SEQUENCE   92 AA;  10123 MW;  6A151480FD5DEF27 CRC64;
     MSALNVFRYS AVLLGVAVGL QTDLSLKSQA SKQQEEKAYA EKLQLIEQAK AEYAKLHAPK
     SETKTSNQKV DLEDPNLDYA KVILGAVESL KQ
//
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