ID   PPN1_NEUCR              Reviewed;         731 AA.
AC   Q9P3S1; Q7RUX7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Endopolyphosphatase;
DE            EC=3.6.1.10;
GN   Name=epp-1; Synonyms=ppn1; ORFNames=B24P7.140, NCU02996;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB97279.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA36146.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL389890; CAB97279.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002236; EAA36146.3; ALT_INIT; Genomic_DNA.
DR   PIR; T50959; T50959.
DR   RefSeq; XP_965382.3; XM_960289.3.
DR   AlphaFoldDB; Q9P3S1; -.
DR   SMR; Q9P3S1; -.
DR   STRING; 5141.EFNCRP00000002488; -.
DR   EnsemblFungi; EAA36146; EAA36146; NCU02996.
DR   GeneID; 3881532; -.
DR   KEGG; ncr:NCU02996; -.
DR   HOGENOM; CLU_013424_1_1_1; -.
DR   InParanoid; Q9P3S1; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR012358; EndopolyPtase_N1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
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..731
FT                   /note="Endopolyphosphatase"
FT                   /id="PRO_0000058548"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..731
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          375..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..684
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..706
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        540
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   731 AA;  83680 MW;  EACD3915CBA37CC5 CRC64;
     MSLSRCILGL ACLWHGVIAS PLGAVPSNIP IATDLQTAAE TVAQPIANSA RKLHGKFLHI
     TDLHPDQFYK PHSSTDEADA CHRGKGPAGV YGAEVSDCDS PFALINATFD WIAANVKDDI
     DFVIWTGDTA RHDSDEGVPR NADQVLGTNR WIADKMAELF SDSTGRHLEI PIVPTLGNND
     ILPHNILLPG PNSWLQHYTH IWRRFVPEAQ RHSFQFGGWF YVEVIPNRLA IFSLNTLYFF
     DRNAGTDGCA SPSEPGYKQM EWLRIQLHIM RERGMKAILM GHVPPARTDS KKLWDENCWQ
     KYSLWLRQYR DVVVSGVFGH MNIDHFFIHD ERDINVGQLA GLADNSIDIR EAMDDELSVT
     GAADYLRELR QNWAKLQPPP TDSKNSGQLK KGKKGRKGKK KKPDVWGERY SLSLVSPSIV
     PNYYPALRIV EYNISGLEDT PVWRDAAKDA MSIELEQNDR QKHLDLKRQH PSHMEDDDEI
     DAQKKKGKKH KGGDSKPKKP DFLIPHPPAK SSPPGPAYSP QPLTLTGYTQ YFANLTHINN
     ITTEASSALL DHDEEEETWV DWLLRWRKGR HGNRKPIHPK PDPREFQFEV EYSTFNDKLY
     KLRDLTVKNY VELAYRISKQ PKKGKAKSID VSYESAAEEE EEEEEEEEED LFEEVEETDE
     EEEQEDDDLS DGEEVDDDSD EDELETETFK KHDKKKHKKK KGKKRQNKVW MHFLTHAFVS
     TVEKEDLKKF T