VATL1_SCHPO
ID VATL1_SCHPO Reviewed; 161 AA.
AC P50515;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=V-type proton ATPase subunit c {ECO:0000250|UniProtKB:P25515};
DE Short=V-ATPase subunit c {ECO:0000250|UniProtKB:P25515};
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump c subunit {ECO:0000250|UniProtKB:P25515};
GN Name=vma3 {ECO:0000312|PomBase:SPAC1B3.14};
GN ORFNames=SPAC1B3.14 {ECO:0000312|PomBase:SPAC1B3.14};
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 [GENOMIC DNA].
RX PubMed=1839480; DOI=10.1002/yea.320070911;
RA Toyama R., Goldstein D.J., Schlegel R., Dhar R.;
RT "A genomic sequence of the Schizosaccharomyces pombe 16 kDa vacuolar H(+)-
RT ATPase.";
RL Yeast 7:989-991(1991).
RN [2]
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:P25515}.
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:P25515}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P25515};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59947; CAA42572.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11240.1; -; Genomic_DNA.
DR PIR; S32970; S32970.
DR RefSeq; NP_594799.1; NM_001020227.2.
DR AlphaFoldDB; P50515; -.
DR SMR; P50515; -.
DR BioGRID; 278932; 2.
DR STRING; 4896.SPAC1B3.14.1; -.
DR MaxQB; P50515; -.
DR PaxDb; P50515; -.
DR EnsemblFungi; SPAC1B3.14.1; SPAC1B3.14.1:pep; SPAC1B3.14.
DR GeneID; 2542471; -.
DR KEGG; spo:SPAC1B3.14; -.
DR PomBase; SPAC1B3.14; vma3.
DR VEuPathDB; FungiDB:SPAC1B3.14; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P50515; -.
DR OMA; NFIQLGA; -.
DR PhylomeDB; P50515; -.
DR Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
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:P50515; -.
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; TAS:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; 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; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..161
FT /note="V-type proton ATPase subunit c"
FT /id="PRO_0000071761"
FT TOPO_DOM 1..9
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..91
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..161
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 138
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P25515"
SQ SEQUENCE 161 AA; 16326 MW; DE752DFDC8C8E639 CRC64;
MSTDLCPVYA PFFGVMGCTA AIVFASFGAA YGTAKAGVGI SAMGVLRPDL IVKNTIPVVM
AGIIAIYGLV VSVLISGNLK QILSLYSGFI QLGAGLSVGL AGLAAGFAIG IVGDAGVRGT
AQQPRLFVAM ILILIFAEVL GLYGLIVALL LNTRATDNVT C
