VATL2_SCHPO
ID VATL2_SCHPO Reviewed; 162 AA.
AC Q9URZ8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=V-type proton ATPase subunit c' {ECO:0000250|UniProtKB:P32842};
DE Short=V-ATPase subunit c' {ECO:0000250|UniProtKB:P32842};
DE AltName: Full=Proteolipid protein vma11;
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit 2;
DE Short=V-ATPase 16 kDa proteolipid subunit 2;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit 2;
DE AltName: Full=Vacuolar proton pump c' subunit {ECO:0000250|UniProtKB:P32842};
GN Name=vma11 {ECO:0000312|PomBase:SPAC732.01};
GN ORFNames=SPAC732.01 {ECO:0000312|PomBase:SPAC732.01};
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:P32842}.
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:P32842}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32842};
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; CAB62424.1; -; Genomic_DNA.
DR PIR; T50253; T50253.
DR RefSeq; NP_593600.1; NM_001019031.2.
DR AlphaFoldDB; Q9URZ8; -.
DR SMR; Q9URZ8; -.
DR BioGRID; 278273; 1.
DR STRING; 4896.SPAC732.01.1; -.
DR PaxDb; Q9URZ8; -.
DR EnsemblFungi; SPAC732.01.1; SPAC732.01.1:pep; SPAC732.01.
DR GeneID; 2541780; -.
DR KEGG; spo:SPAC732.01; -.
DR PomBase; SPAC732.01; vma11.
DR VEuPathDB; FungiDB:SPAC732.01; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_1_1; -.
DR InParanoid; Q9URZ8; -.
DR OMA; MSVCPPY; -.
DR PhylomeDB; Q9URZ8; -.
DR PRO; PR:Q9URZ8; -.
DR Proteomes; UP000002485; Chromosome I.
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; ISO:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; IC: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..162
FT /note="V-type proton ATPase subunit c'"
FT /id="PRO_0000071787"
FT TOPO_DOM 1..11
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..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..93
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 140
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P32842"
SQ SEQUENCE 162 AA; 16785 MW; 6A4C532BC986C52B CRC64;
MSSNLCPIYS SFFGFAGVCA SMVFSCLGAG YGTALAGRGI AAVGAFRPEI VMKSLIPVVM
SGIIGVYGLV MSVLIAGDMS PDNDYSLFSG FIHLSAGLAV GLTGVAAGYA IGVVGDRGVQ
SFMRQDRIFV SMVLILIFAE VLGLYGLIVG LILQTKTSNV CY
