ID C4WUH3_ACYPI Unreviewed; 273 AA.
AC C4WUH3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN Name=ACYPI000258 {ECO:0000313|EMBL:BAH71543.1};
GN Synonyms=100158834 {ECO:0000313|EnsemblMetazoa:NP_001155377.1};
OS Acyrthosiphon pisum (Pea aphid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH71543.1};
RN [1] {ECO:0000313|EMBL:BAH71543.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LSR1 {ECO:0000313|EMBL:BAH71543.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:BAH71543.1};
RA Shigenobu S., Nakabachi A., Richards S.;
RT "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA Weinstock G., Gibbs R.A.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001155377.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) 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; AK341065; BAH71543.1; -; mRNA.
DR RefSeq; NP_001155377.1; NM_001161905.2.
DR AlphaFoldDB; C4WUH3; -.
DR STRING; 7029.C4WUH3; -.
DR EnsemblMetazoa; NM_001161905.2; NP_001155377.1; LOC100158834.
DR GeneID; 100158834; -.
DR KEGG; api:100158834; -.
DR eggNOG; KOG3976; Eukaryota.
DR HOGENOM; CLU_087186_0_0_1; -.
DR InParanoid; C4WUH3; -.
DR OMA; KHMVDWI; -.
DR Proteomes; UP000007819; 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 2: Evidence at transcript level;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368017};
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:UP000007819};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 273 AA; 31284 MW; 8B20060943EE371D CRC64;
MLSRLALRSE LFRVAPLCAN VVRTTQTKPA VTSTNESIIV PGFPKPNGLP QPNPFDGPER
DLVNFPRMVR LEEPAKTRYL FVPEEWFEVF YKKTGVTGPY VLAAGITTYV LSKEIWVVEH
EFPYVLATIG LFYVGWKKFG ASLAGFLDKE IDEYEASCNA SRKGEIDGLT ESIENQKKEV
WRTEAQKHVI QAKRENVAIQ LEAIYRERAL QAYNQVKRRL DYQLDLANLT RTVQQRHMVN
WIIENVLKSL TNEQEKQSFK KCMVDLQALA AKA
//
