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Database: UniProt
Entry: B3DLE6_XENTR
LinkDB: B3DLE6_XENTR
Original site: B3DLE6_XENTR 
ID   B3DLE6_XENTR            Unreviewed;        71 AA.
AC   B3DLE6;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
GN   Name=atp5me {ECO:0000313|Ensembl:ENSXETP00000104132,
GN   ECO:0000313|RefSeq:NP_001016415.1,
GN   ECO:0000313|Xenbase:XB-GENE-5722303};
GN   Synonyms=atp5i {ECO:0000313|RefSeq:NP_001016415.1,
GN   ECO:0000313|Xenbase:XB-GENE-5722303}, atp5k
GN   {ECO:0000313|EMBL:AAI67416.1, ECO:0000313|RefSeq:NP_001016415.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI67416.1};
RN   [1] {ECO:0000313|RefSeq:NP_001016415.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI67416.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole embryo {ECO:0000313|EMBL:AAI67416.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSXETP00000104132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000104132};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [4] {ECO:0000313|Ensembl:ENSXETP00000104132}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2021) to UniProtKB.
RN   [5] {ECO:0000313|RefSeq:NP_001016415.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00003606, 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; BC167416; AAI67416.1; -; mRNA.
DR   RefSeq; NP_001016415.1; NM_001016415.2.
DR   STRING; 8364.ENSXETP00000005322; -.
DR   PaxDb; 8364-ENSXETP00000056323; -.
DR   Ensembl; ENSXETT00000119609; ENSXETP00000104132; ENSXETG00000036008.
DR   GeneID; 549169; -.
DR   KEGG; xtr:549169; -.
DR   AGR; Xenbase:XB-GENE-5722303; -.
DR   CTD; 521; -.
DR   Xenbase; XB-GENE-5722303; atp5me.
DR   eggNOG; KOG4326; Eukaryota.
DR   HOGENOM; CLU_180903_0_0_1; -.
DR   OMA; IKFARYS; -.
DR   OrthoDB; 5361366at2759; -.
DR   TreeFam; TF314719; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Bgee; ENSXETG00000036008; Expressed in heart and 14 other cell types or tissues.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008143};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
FT   COILED          36..67
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   71 AA;  8255 MW;  500FE72269C2F96A CRC64;
     MVPPVQVSPL IKFTRYSALL VGMIYGMKRY DYLKPIAEEE RKVEAEEKRQ REEAERIAKE
     IAAANEDTIL K
//
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