ID   Q6Z0Z9_ORYSJ            Unreviewed;       167 AA.
AC   Q6Z0Z9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN   OrderedLocusNames=Os02g0550100 {ECO:0000313|EMBL:BAS79155.1};
GN   ORFNames=OSNPB_020550100 {ECO:0000313|EMBL:BAS79155.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS79155.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAS79155.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(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|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}.
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DR   EMBL; AP014958; BAS79155.1; -; Genomic_DNA.
DR   RefSeq; XP_015622696.1; XM_015767210.1.
DR   AlphaFoldDB; Q6Z0Z9; -.
DR   SMR; Q6Z0Z9; -.
DR   STRING; 39947.Q6Z0Z9; -.
DR   PaxDb; 39947-Q6Z0Z9; -.
DR   EnsemblPlants; Os02t0550100-01; Os02t0550100-01; Os02g0550100.
DR   GeneID; 4329623; -.
DR   Gramene; Os02t0550100-01; Os02t0550100-01; Os02g0550100.
DR   KEGG; osa:4329623; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   HOGENOM; CLU_085752_1_0_1; -.
DR   InParanoid; Q6Z0Z9; -.
DR   OMA; CAMGVLR; -.
DR   OrthoDB; 5482523at2759; -.
DR   Proteomes; UP000059680; Chromosome 2.
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   CDD; cd18176; ATP-synt_Vo_c_ATP6C_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; 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:SF80; 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   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:UP000059680};
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        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        132..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          19..78
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          99..157
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   167 AA;  16735 MW;  9FA05FF1A5258A68 CRC64;
     MAGASTFSGD ETAPFFGFLG AAAALVFSCM GAAYGTAKSG VGVASMGVMR PELVMKSIVP
     VVMAGVLGIY GLIIAVIIST GINPKAKPYF LFDGYAHLSS GLACGLAGLA AGMAIGIVGD
     AGVRANAQQP KLFVGMILIL IFAEALALYG LIVGIILSSR AGQSRAD
//