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Database: UniProt
Entry: A0A061FK99_THECC
LinkDB: A0A061FK99_THECC
Original site: A0A061FK99_THECC 
ID   A0A061FK99_THECC        Unreviewed;       137 AA.
AC   A0A061FK99;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
DE   Flags: Fragment;
GN   ORFNames=TCM_034162 {ECO:0000313|EMBL:EOY14929.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14929.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY14929.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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|ARBA:ARBA00002481, 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}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004128,
CC       ECO:0000256|RuleBase:RU363060}.
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; CM001886; EOY14929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061FK99; -.
DR   EnsemblPlants; EOY14929; EOY14929; TCM_034162.
DR   Gramene; EOY14929; EOY14929; TCM_034162.
DR   HOGENOM; CLU_085752_2_0_1; -.
DR   OMA; VACISTK; -.
DR   Proteomes; UP000026915; Chromosome 8.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd18175; ATP-synt_Vo_c_ATP6C_rpt1; 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; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   PANTHER; PTHR10263:SF60; V-TYPE PROTON ATPASE SUBUNIT C2; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU363060};
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:UP000026915};
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};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|RuleBase:RU363060}.
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        83..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          44..103
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOY14929.1"
FT   NON_TER         137
FT                   /evidence="ECO:0000313|EMBL:EOY14929.1"
SQ   SEQUENCE   137 AA;  14188 MW;  434AA5F5293ABCCD CRC64;
     VLSKYNLKKK LLHLQEQQIR SITIFGKMSS TFSGDETAPF FGFLGAAAAL VFSCMGAAYG
     TAKSGVGVAS MGVMRPELVM KSIVPVVMAG VLGIYGLIIA VIISTGINPK AKSYYLFDGY
     AHLSSGLACG LAGLSAG
//
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