VATO_SCHPO
ID VATO_SCHPO Reviewed; 199 AA.
AC O14046;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Probable V-type proton ATPase 20 kDa proteolipid subunit;
DE Short=V-ATPase 20 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump 20 kDa proteolipid subunit;
GN Name=vma16; ORFNames=SPAC2C4.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (By similarity). {ECO:0000250|UniProtKB:P23968}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1) (By similarity). The decameric c-ring forms the proton-conducting
CC pore, and is composed of eight proteolipid subunits c, one subunit c'
CC and one subunit c'' (By similarity). {ECO:0000250|UniProtKB:P23968}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P23968};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16373.1; -; Genomic_DNA.
DR PIR; T38524; T38524.
DR RefSeq; NP_594516.1; NM_001019945.2.
DR AlphaFoldDB; O14046; -.
DR SMR; O14046; -.
DR STRING; 4896.SPAC2C4.13.1; -.
DR PaxDb; O14046; -.
DR EnsemblFungi; SPAC2C4.13.1; SPAC2C4.13.1:pep; SPAC2C4.13.
DR GeneID; 2541999; -.
DR KEGG; spo:SPAC2C4.13; -.
DR PomBase; SPAC2C4.13; vma16.
DR VEuPathDB; FungiDB:SPAC2C4.13; -.
DR eggNOG; KOG0233; Eukaryota.
DR HOGENOM; CLU_085752_0_1_1; -.
DR InParanoid; O14046; -.
DR OMA; PYAWAST; -.
DR PhylomeDB; O14046; -.
DR Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SPO-77387; Insulin receptor recycling.
DR Reactome; R-SPO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:O14046; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IC:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISO:PomBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR GO; GO:0007035; P:vacuolar acidification; ISO:PomBase.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..199
FT /note="Probable V-type proton ATPase 20 kDa proteolipid
FT subunit"
FT /id="PRO_0000071779"
FT TOPO_DOM 1..3
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..86
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..170
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 94
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P23968"
SQ SEQUENCE 199 AA; 20886 MW; 3403B3AA5266124A CRC64;
MSLFSTSLWT TTVMSIIVGL YMLFHNSGES FDFGSFLLDT SPYTWGLLGI ASCVAFGIIG
AAWGIFICGT SILGGAVKAP RIKTKNLISI IFCEVVAIYS LIIAIVFSAK INDINPAGFY
TKSHYYTGFA LFWGGITVGL CNLICGVCVG ITGSSAALAD AQDASLFVKV LVVEIFGSVL
GLFGLIVGLL IGGKASDFS
