ID Q2F630_BOMMO Unreviewed; 205 AA.
AC Q2F630;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000256|ARBA:ARBA00029494};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000256|ARBA:ARBA00031057};
GN Name=692859 {ECO:0000313|EnsemblMetazoa:NP_001040169.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:ABD36187.1};
RN [1] {ECO:0000313|EMBL:ABD36187.1}
RP NUCLEOTIDE SEQUENCE.
RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA Lin T.B., Chen J.E.;
RT "Blast silkworm EST database for functional genes.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001040169.1}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001040169.1};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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. V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment.
CC {ECO:0000256|RuleBase:RU363060}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits. {ECO:0000256|RuleBase:RU363060}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000256|ARBA:ARBA00007296, ECO:0000256|RuleBase:RU363060}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363060}.
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DR EMBL; DQ311242; ABD36187.1; -; mRNA.
DR RefSeq; NP_001040169.1; NM_001046704.1.
DR RefSeq; XP_012550712.1; XM_012695258.1.
DR AlphaFoldDB; Q2F630; -.
DR SMR; Q2F630; -.
DR STRING; 7091.Q2F630; -.
DR PaxDb; 7091-BGIBMGA000231-TA; -.
DR EnsemblMetazoa; NM_001046704.1; NP_001040169.1; LOC692859.
DR EnsemblMetazoa; XM_012695258.3; XP_012550712.1; LOC692859.
DR GeneID; 692859; -.
DR KEGG; bmor:692859; -.
DR eggNOG; KOG0233; Eukaryota.
DR HOGENOM; CLU_085752_0_1_1; -.
DR InParanoid; Q2F630; -.
DR OMA; GWFLENT; -.
DR OrthoDB; 1112183at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10263:SF18; V-TYPE PROTON ATPASE 21 KDA PROTEOLIPID SUBUNIT C; 1.
DR PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
PE 2: Evidence at transcript level;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU363060};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW Reference proteome {ECO:0000313|Proteomes:UP000005204};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363060};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363060};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363060}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 89..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 133..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 169..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 50..109
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 137..196
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 205 AA; 21554 MW; C9FD3988CF6D2E26 CRC64;
MRYFLSYLFV LLVGLAIPIF SLYYVLNGKG EQISLGWFLE NTSPYMWGTL GIAFSVALSV
VGAAMGIHTT GVSIVGGGVK APRIKTKNLI SVIFCEAVAI YGLITAIVLS GMLEKYSEPF
TSVSVKQQNW MAGYVMFGAG LAVGLVNLFC GIAVGIVGSG AALADAANAA LFVKILIVEI
FGSAIGLFGL IVGIYMTSKV KMGNQ
//
