VATC_SCHPO
ID VATC_SCHPO Reviewed; 394 AA.
AC Q9HDW6;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=V-type proton ATPase subunit C;
DE Short=V-ATPase subunit C;
DE AltName: Full=Vacuolar proton pump subunit C;
GN Name=vma5 {ECO:0000312|PomBase:SPAPB2B4.05};
GN ORFNames=SPAPB2B4.05 {ECO:0000312|PomBase:SPAPB2B4.05};
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (By similarity). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments (By similarity).
CC Subunit C is necessary for the assembly of the catalytic sector of the
CC enzyme and is likely to have a specific function in its catalytic
CC activity (By similarity). Reversibly leaves the enzyme after glucose
CC depletion, causing the catalytic subcomplex V1 to detach from the V0
CC section (By similarity). {ECO:0000250|UniProtKB:P31412}.
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). {ECO:0000250|UniProtKB:P31412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole
CC membrane {ECO:0000250|UniProtKB:P31412}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P31412}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {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; CU329670; CAC21471.1; -; Genomic_DNA.
DR RefSeq; NP_593891.1; NM_001019321.2.
DR AlphaFoldDB; Q9HDW6; -.
DR SMR; Q9HDW6; -.
DR BioGRID; 279889; 1.
DR STRING; 4896.SPAPB2B4.05.1; -.
DR iPTMnet; Q9HDW6; -.
DR MaxQB; Q9HDW6; -.
DR PaxDb; Q9HDW6; -.
DR PRIDE; Q9HDW6; -.
DR EnsemblFungi; SPAPB2B4.05.1; SPAPB2B4.05.1:pep; SPAPB2B4.05.
DR GeneID; 2543469; -.
DR KEGG; spo:SPAPB2B4.05; -.
DR PomBase; SPAPB2B4.05; vma5.
DR VEuPathDB; FungiDB:SPAPB2B4.05; -.
DR eggNOG; KOG2909; Eukaryota.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; Q9HDW6; -.
DR OMA; GEYWLIS; -.
DR PhylomeDB; Q9HDW6; -.
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:Q9HDW6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISO:PomBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR GO; GO:0007035; P:vacuolar acidification; ISO:PomBase.
DR CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..394
FT /note="V-type proton ATPase subunit C"
FT /id="PRO_0000209357"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 394 AA; 44361 MW; FCEC100946D6E773 CRC64;
MSKSDFWILS VPSRGGSNAD LCDDIERLLV SGSTSLISTV APFDVPPFKV ESLDVLISQS
EQLTKQDAQC ASAISKISDI IKNTVSSSSG DLKDYFMVQD KSPLEYVSSF AWNSSRFHMN
KTISEISDRI TSEIISFEND IRTRQTSFQQ ASSAFQNMQK KQSGNLSQKS LANIVHEEDV
VHGSDYLTNV FIAVPLNLEK QFLNSYETLT DLVIPRSAKK LDQDSEFVLY TVVVFKKTAD
SFITKAREAK YTIREFTFEQ GLRETEQSEF DDAAVKEKRM LSSLLRYASI AFSESFQGWI
HLKCLCVYVE SILRYGLPPD FSSVIFQPMA KSEVKIKNIL LSKYAYLAQN PVGNNKVKNV
DSSAGLDESM ADLNLDEEYL PFVLFTVPSK VFNY