ID   PPN1_SCHPO              Reviewed;         577 AA.
AC   Q9C1W8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Endopolyphosphatase;
DE            EC=3.6.1.10;
GN   Name=ppn1; ORFNames=SPBC713.07c;
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).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP)
CC       chains of many hundreds of phosphate residues into shorter lengths.
CC       {ECO:0000250|UniProtKB:Q04119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate;
CC         Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:Q04119};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04119}.
CC   -!- PTM: Processing by proteases in the vacuole may be required for
CC       activation. {ECO:0000250|UniProtKB:Q04119}.
CC   -!- SIMILARITY: Belongs to the endopolyphosphatase PPN1 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAC22608.1; -; Genomic_DNA.
DR   RefSeq; NP_595346.1; NM_001021254.2.
DR   AlphaFoldDB; Q9C1W8; -.
DR   SMR; Q9C1W8; -.
DR   BioGRID; 277655; 73.
DR   STRING; 4896.SPBC713.07c.1; -.
DR   MaxQB; Q9C1W8; -.
DR   PaxDb; Q9C1W8; -.
DR   EnsemblFungi; SPBC713.07c.1; SPBC713.07c.1:pep; SPBC713.07c.
DR   GeneID; 2541140; -.
DR   KEGG; spo:SPBC713.07c; -.
DR   PomBase; SPBC713.07c; -.
DR   VEuPathDB; FungiDB:SPBC713.07c; -.
DR   eggNOG; KOG3770; Eukaryota.
DR   HOGENOM; CLU_013424_2_0_1; -.
DR   InParanoid; Q9C1W8; -.
DR   OMA; MKAILMG; -.
DR   PhylomeDB; Q9C1W8; -.
DR   PRO; PR:Q9C1W8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000298; F:endopolyphosphatase activity; ISO:PomBase.
DR   GO; GO:0004309; F:exopolyphosphatase activity; ISO:PomBase.
DR   GO; GO:0006112; P:energy reserve metabolic process; IC:PomBase.
DR   GO; GO:0006798; P:polyphosphate catabolic process; ISO:PomBase.
DR   CDD; cd00842; MPP_ASMase; 1.
DR   InterPro; IPR041805; ASMase/PPN1_MPP.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR012358; EndopolyPtase_N1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..577
FT                   /note="Endopolyphosphatase"
FT                   /id="PRO_0000058549"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..577
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          430..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..456
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   577 AA;  66026 MW;  D5EC6913A6E89647 CRC64;
     MRPSVITVAV LFVQSTWASF AFGNPMSMRN KAHTNDLVNS KGKPLVGRFL HITDMHPDIY
     YEKGSTVDHY CHSYDHNSDD TPLGKSKVGY LSPGPGYECD SSPALIDKTL EWLKEHQDDV
     LGGIDFILWT GDNSRHDNDN HFPRTQSEIL ASNEDLVNKM IEAFPDVPIV SAIGNNDIYP
     HNIMEAGPSS MTRQLAGAWD ALIPYEERHT FEKGSYYLCD VIPDKLAAIS INTLYLSNKN
     AAVDGCPDDN LDEPGSLFMR WFKIQLEAYR LKGMKVWLLG HIPPTRGQWY EDCYTSFTDL
     LYEFRDIIVG QLYGHMNINH FVFLEFDKLP VDTESYGIKS AQPKYVKSLI DAQYAELPTF
     PENLTEEFLN GTVGNYSLAT VGGSIIPEMF PTFRVYEYNI SDIANQLDDR EELTEITSFN
     WETLEEQSQS DYEIDKKKKK KKKNNKKKKK NKRKNIKPGP LGPAYVPSLF TPISFKQYFL
     NTSNYMDATK DTEISYELLY TSKDSPYNMP DLTVPEYMRL AKRIATCDKP EDPHQFKLQS
     GDQNTFRISK KKKPSICPIA YTYLWHAYIG SISDFED