VPP1_SCHPO
ID VPP1_SCHPO Reviewed; 831 AA.
AC O13742;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=V-type proton ATPase subunit a;
DE Short=V-ATPase a subunit;
DE AltName: Full=Vacuolar ATPase 91 kDa subunit;
DE AltName: Full=Vacuolar proton pump a subunit;
DE AltName: Full=Vacuolar proton translocating ATPase subunit a;
GN Name=vph1; ORFNames=SPAC16E8.07c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Subunit of the V0 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 {ECO:0000250|UniProtKB:P32563}.
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:P32563}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32563};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11035.2; -; Genomic_DNA.
DR PIR; T37787; T37787.
DR RefSeq; NP_594219.2; NM_001019642.2.
DR AlphaFoldDB; O13742; -.
DR SMR; O13742; -.
DR BioGRID; 278776; 1.
DR STRING; 4896.SPAC16E8.07c.1; -.
DR MaxQB; O13742; -.
DR PaxDb; O13742; -.
DR EnsemblFungi; SPAC16E8.07c.1; SPAC16E8.07c.1:pep; SPAC16E8.07c.
DR GeneID; 2542310; -.
DR KEGG; spo:SPAC16E8.07c; -.
DR PomBase; SPAC16E8.07c; vph1.
DR VEuPathDB; FungiDB:SPAC16E8.07c; -.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_2_1; -.
DR InParanoid; O13742; -.
DR OMA; FSYDRAR; -.
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:O13742; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR GO; GO:0007035; P:vacuolar acidification; ISO:PomBase.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..831
FT /note="V-type proton ATPase subunit a"
FT /id="PRO_0000119223"
FT TOPO_DOM 1..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..439
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..548
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..650
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..769
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 831 AA; 94159 MW; 9114BFA35428C6FA CRC64;
MSPSLFRSEE VSLVQLYLPT ESARPIMSAL GELSTIHFKD LNPDVVAFQR SFVREIRRLT
DTERLLRYLH SEIDLNGIHV PDHNLPPSYE SVLESSTIED IIERITRLEA RVRQLVESSQ
LLEARYLQQL EFANVLTKAD AFFSKSGNTV DPLRNNYETS SIFSGEDDTT APLIENALEL
GTTGTFDSEE TSPQMNTTLD FVSGIIPTVK FQFLERILWR TLRGNLFIHQ VRADDSLIHG
AEKNEEKTIF LVIAHGTQIL LRIRKISESL GATLFPVEED APGRTSQIQQ ANVSISDLNA
VLENTRSALY TELTFIAEHI SAWEAVLHKD KTVFQVMNLF NYDQNHKCLI AEGWCPTANL
PMVQKTLRNI SDLTDSQAPT ILNVVHTSEQ PPTYFRVNKF TEGFQSIIDS YGIATYREVN
HGIVAIVTFP FLFAIMFGDL GHGAIMASVA LMFVLYEKTL GAKKDLDEIV GMVFYGRYIV
LLMGLFSMYV GFVYNDLFSK PMSIFSSRWV WPVKSEEAIA RAVQVGTYPI GIDPTWHSAD
NNLLFMNSYK MKLSIILGVI HMTFCLFLSL SNYRFFKRKL DIYAVFVPSL IFLEAIFGYL
VITIVYKWCI DWKAKDLQPP SLLNMLILMF LSPGTLEDQL YPGQKYLQVG LVIAALICVP
WLLIVKPFVL WRRHSNEENK YQSLNSDLPN VDEADALMAV DSQEKQAEPF ELGEVVIHQV
IHTIEFCLGC VSHTASYLRL WALSLAHNQL SSVLWNMTLA NGFRMTGIVG SIFVVILFGF
WFIATCVVLV AMEGTSAMLH SLRLHWVEGM SKHFEGEGYA FTPFTFKVTA E
