ID A0A1J1I242_9DIPT Unreviewed; 227 AA.
AC A0A1J1I242;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=CLUMA_CG007361 {ECO:0000313|EMBL:CRK93834.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK93834.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK93834.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CVRI01000038; CRK93834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1I242; -.
DR STRING; 568069.A0A1J1I242; -.
DR OrthoDB; 1112183at2759; -.
DR Proteomes; UP000183832; 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 3: Inferred from homology;
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:UP000183832};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 88..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 133..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 173..194
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 139..195
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 227 AA; 23645 MW; 0584F927DA94D61A CRC64;
MRYALGYTLT GTLTTLSSLW ILYHVLTGQG ERVSVGWFLE ETSPYMWACL GIAFAVSLSV
VGAAIGIHTT GVSIVGGGVK APRIKTKNLI SVIFCEAVAI YGLITAIVLS GMLDPYTQKG
MASSDTIRGN NFMAGHVMFG AGLSVGLVNL FCGIAVGIVG SGAALADAAN SALFVKILIV
EIFGSAIGLF GLIVGKGSNN LIGLSRLESS VQFIRPGFEP RLGHEVE
//
