ID A0A2V0NVV7_9CHLO Unreviewed; 205 AA.
AC A0A2V0NVV7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=V-type proton ATPase subunit c 1 {ECO:0000313|EMBL:GBF91778.1};
GN ORFNames=Rsub_04082 {ECO:0000313|EMBL:GBF91778.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF91778.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF91778.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF91778.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic cells.
CC {ECO:0000256|RuleBase:RU363060}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex attached to an integral membrane V0 proton pore
CC complex. {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF91778.1}.
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DR EMBL; BDRX01000026; GBF91778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0NVV7; -.
DR STRING; 307507.A0A2V0NVV7; -.
DR InParanoid; A0A2V0NVV7; -.
DR Proteomes; UP000247498; 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:UP000247498};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..205
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015968087"
FT TRANSMEM 46..70
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 131..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 171..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 53..111
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; 21252 MW; E4F97F731C99CFED CRC64;
MALGSAGFWL LAPFTVSAFS FAVSVGSPDR FIDWPYLWLL FRNISPFFYA VVGVALCVGT
SILGAAWGIF ITGSSLVGAA VRVPRITSKN LISIIFCEAV AIYGVIVAII LQTKLEAVTA
EQGLFTRSNM AAGYAIFAAG LTCGLSNLVC GMCVGIVGSS CALSDAQNST LFVKILVVEI
FGSALGLFGV IVGIIMAGNA GFAKV
//
