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Database: UniProt
Entry: A0A084W069_ANOSI
LinkDB: A0A084W069_ANOSI
Original site: A0A084W069_ANOSI 
ID   A0A084W069_ANOSI        Unreviewed;       237 AA.
AC   A0A084W069;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN   ORFNames=ZHAS_00011553 {ECO:0000313|EMBL:KFB43613.1};
OS   Anopheles sinensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=74873 {ECO:0000313|EnsemblMetazoa:ASIC011553-PA, ECO:0000313|Proteomes:UP000030765};
RN   [1] {ECO:0000313|EMBL:KFB43613.1, ECO:0000313|Proteomes:UP000030765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA   Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA   Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA   Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT   "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT   of mosquito competence for malaria parasites.";
RL   BMC Genomics 15:42-42(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASIC011553-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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 and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements. {ECO:0000256|RuleBase:RU368017}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(0) has three main
CC       subunits: a, b and c. {ECO:0000256|RuleBase:RU368017}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU368017}.
CC       Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000256|ARBA:ARBA00007479, ECO:0000256|RuleBase:RU368017}.
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DR   EMBL; ATLV01019092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE525262; KFB43613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084W069; -.
DR   STRING; 74873.A0A084W069; -.
DR   EnsemblMetazoa; ASIC011553-RA; ASIC011553-PA; ASIC011553.
DR   VEuPathDB; VectorBase:ASIC011553; -.
DR   VEuPathDB; VectorBase:ASIS010950; -.
DR   OMA; KHMVDWI; -.
DR   OrthoDB; 2939076at2759; -.
DR   Proteomes; UP000030765; 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:UniProtKB-UniRule.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.5.2210; -; 1.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
DR   SUPFAM; SSF161060; ATP synthase B chain-like; 1.
PE   3: Inferred from homology;
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368017};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU368017};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU368017};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368017};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU368017};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU368017};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
FT   COILED          122..149
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   237 AA;  27124 MW;  968349D818338E3A CRC64;
     MLSRAVLLSA AKKPAALVLA RGASSQPAER PKRPEHGGKV RLGFLPEEWF TFFYNKTGVT
     GPYVFGAGLL TYLCSKEIYI MEHEYYNGLS LAIMVVFAVK KFGPSMASYL DKEVDKIENE
     WKESRENSIQ QLSQAIEDEK KEQWRAEGQT MLMQAKKENV ALQLEAAYRE RAMNAYREVK
     KRLDYQVERQ NVDRRISQKH MVDWIVNNVV KSITPDQEKE NLNKCIADLG ALAARSK
//
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