VOA1_SCHPO
ID VOA1_SCHPO Reviewed; 311 AA.
AC Q9Y7R6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Protein big1;
DE Flags: Precursor;
GN Name=big1; Synonyms=voa1; ORFNames=SPCC306.06c;
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).
CC -!- FUNCTION: Accessory subunit of the V0 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments (By
CC similarity). {ECO:0000250|UniProtKB:P53262}.
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:P53262}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372}. Vacuole membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the BIG1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAB41654.1; -; Genomic_DNA.
DR PIR; T41284; T41284.
DR RefSeq; NP_587814.1; NM_001022807.2.
DR AlphaFoldDB; Q9Y7R6; -.
DR STRING; 4896.SPCC306.06c.1; -.
DR MaxQB; Q9Y7R6; -.
DR PaxDb; Q9Y7R6; -.
DR EnsemblFungi; SPCC306.06c.1; SPCC306.06c.1:pep; SPCC306.06c.
DR GeneID; 2539326; -.
DR KEGG; spo:SPCC306.06c; -.
DR PomBase; SPCC306.06c; big1.
DR VEuPathDB; FungiDB:SPCC306.06c; -.
DR eggNOG; ENOG502S6TD; Eukaryota.
DR HOGENOM; CLU_980576_0_0_1; -.
DR InParanoid; Q9Y7R6; -.
DR OMA; QISYHAF; -.
DR PhylomeDB; Q9Y7R6; -.
DR PRO; PR:Q9Y7R6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0070070; P:proton-transporting V-type ATPase complex assembly; ISO:PomBase.
DR InterPro; IPR037654; Big1.
DR PANTHER; PTHR28285; PTHR28285; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Vacuole.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..311
FT /note="Protein big1"
FT /id="PRO_0000343134"
FT TOPO_DOM 18..267
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 311 AA; 34636 MW; 3DB6FF8CF11478C5 CRC64;
MFSWSILFIV CFSLVSAFKD TSPIFLFSTN SKLPKSSDDS SISTCPMMFF DAAIEALSTC
NTATLIIHQP GLEVNDFQLG AFKHLKRVSL QSPYSLLLPY SKESLDSQEL VHSAKQNCDV
EVVYLGGSFN AFPPLQNDRI TVVYMNELSN ESYHRSAQLM ELDEMFYNLQ STLEQDAQWN
VIIASSPLNN SDFEGFKVDA NEEEANAEFV IQTLGGLNSG KSALQHGQLA SLPDQNEGSQ
TTLAMHQTRK HPVTDNGATG LFTEYQFFTP GLYMGYLALA VLVPTLFISC RLLSSIQISY
HAFDSPRRKQ L
