ID   R4IPV5_PSECR            Unreviewed;        55 AA.
AC   R4IPV5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   10-MAY-2017, entry version 19.
DE   RecName: Full=ATP synthase protein 8 {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400266};
GN   Name=ATP8 {ECO:0000313|EMBL:AFV57260.1};
OS   Pseudobagrus crassilabris (Bagrid catfish) (Leiocassis crassilabris).
OG   Mitochondrion {ECO:0000313|EMBL:AFV57260.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Bagridae; Pseudobagrus.
OX   NCBI_TaxID=175786 {ECO:0000313|EMBL:AFV57260.1};
RN   [1] {ECO:0000313|EMBL:AFV57260.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23311344;
RA   Liang H.W., Li Z., Zou G.W.;
RT   "Complete mitochondrial DNA genome of Leiocassis
RT   crassilabris(Siluriformes: Bagridae).";
RL   Mitochondrial DNA 24:222-224(2013).
RN   [2] {ECO:0000313|EMBL:AGM51227.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24512421; DOI=10.3109/19401736.2013.792067;
RA   Zhou L., Xie Z., Zhang Y.;
RT   "The complete mitochondrial genome of Leiocassis crassilabris
RT   (Teleostei, Siluriformes: Bagridae).";
RL   Mitochondrial DNA 25:183-184(2014).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation.
CC       {ECO:0000256|SAAS:SAAS00585567}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel.
CC       {ECO:0000256|SAAS:SAAS00585553}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400291};
CC       Single-pass membrane protein {ECO:0000256|RuleBase:RU003661,
CC       ECO:0000256|SAAS:SAAS00400291}.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family.
CC       {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00585545}.
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DR   EMBL; JX867257; AFV57260.1; -; Genomic_DNA.
DR   EMBL; KC768227; AGM51227.1; -; Genomic_DNA.
DR   RefSeq; YP_008080853.1; NC_021394.1.
DR   RefSeq; YP_008080853.1; NC_021394.1.
DR   RefSeq; YP_008080853.1; NC_021394.1.
DR   GeneID; 15822349; -.
DR   CTD; 4509; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR001421; ATP8_metazoa.
DR   Pfam; PF00895; ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|SAAS:SAAS00119314};
KW   CF(0) {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00119302};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU003661,
KW   ECO:0000256|SAAS:SAAS00478108};
KW   Ion transport {ECO:0000256|RuleBase:RU003661,
KW   ECO:0000256|SAAS:SAAS00119304};
KW   Membrane {ECO:0000256|SAAS:SAAS00119303, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003661,
KW   ECO:0000256|SAAS:SAAS00119301, ECO:0000313|EMBL:AFV57260.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003661,
KW   ECO:0000256|SAAS:SAAS00119312, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00119308,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003661,
KW   ECO:0000256|SAAS:SAAS00478149}.
FT   TRANSMEM      6     24       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   55 AA;  6437 MW;  02DE5AE073F14FEA CRC64;
     MPQLNPAPWF AILVFSWLIF LTVIPNKVLN HTFTNEVTAL SAETLKSDTW NWPWH
//