VATL_AEDAE
ID VATL_AEDAE Reviewed; 157 AA.
AC O16110; Q17PR4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE AltName: Full=V-ATPase subunit c {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN ORFNames=AAEL000291;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9397516;
RX DOI=10.1002/(sici)1520-6327(1998)37:1<80::aid-arch10>3.0.co;2-6;
RA Gill S.S., Chu P.B., Smethurst P., Pietrantonio P.V., Ross L.S.;
RT "Isolation of the V-ATPase A and c subunit cDNAs from mosquito midgut and
RT Malpighian tubules.";
RL Arch. Insect Biochem. Physiol. 37:80-90(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). {ECO:0000250|UniProtKB:P23380,
CC ECO:0000250|UniProtKB:P27449}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC {ECO:0000250|UniProtKB:P27449}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AF008924; AAB71660.1; -; mRNA.
DR EMBL; CH477190; EAT48687.1; -; Genomic_DNA.
DR RefSeq; XP_001654757.1; XM_001654707.1.
DR AlphaFoldDB; O16110; -.
DR SMR; O16110; -.
DR STRING; 7159.AAEL000291-PA; -.
DR GeneID; 5573732; -.
DR KEGG; aag:5573732; -.
DR VEuPathDB; VectorBase:AAEL000291; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; O16110; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; O16110; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..157
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071749"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..94
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..157
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 141
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
FT CONFLICT 7
FT /note="N -> K (in Ref. 1; AAB71660)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="F -> I (in Ref. 1; AAB71660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 16045 MW; BD332E56C3F82629 CRC64;
MALPEENPVY GPFFGVMGAA AAIIFSALGA AYGTAKSGTG IAAMSVMRPE LIMKSIIPVV
MAGIIAIYGL VVAVLIAGSL DTPTKYSLYK GFIHLGAGLA VGFSGLAAGF AIGIVGDAGV
RGTAQQPRLF VGMILILIFA EVLGLYGLIV AIYLYTK
