PPN1_ASHGO
ID PPN1_ASHGO Reviewed; 594 AA.
AC Q756F2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Endopolyphosphatase;
DE EC=3.6.1.10;
GN Name=PPN1; OrderedLocusNames=AER313C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 24; 49 AND 63-64.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52993.2; -; Genomic_DNA.
DR RefSeq; NP_985169.2; NM_210523.2.
DR AlphaFoldDB; Q756F2; -.
DR SMR; Q756F2; -.
DR STRING; 33169.AAS52993; -.
DR EnsemblFungi; AAS52993; AAS52993; AGOS_AER313C.
DR GeneID; 4621382; -.
DR KEGG; ago:AGOS_AER313C; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_1_1; -.
DR InParanoid; Q756F2; -.
DR OMA; MKAILMG; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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 CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 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..594
FT /note="Endopolyphosphatase"
FT /id="PRO_0000058543"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..594
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 67588 MW; 4C98C4B8F95D96B0 CRC64;
MAAEEGRRLQ MKNGEGVGRS GRPRWALWIA ALMAGALWWT VHSDAVALMS KACGKDAATT
PRAARALRGR FLHITDIHPD PLYVEGSSIA GACHGDPARD ASDRAGRFGD AMGGCDAPMD
LMNYTLAWVA THLRDEIDFV VWTGDNARHD NDRRQPRTAE QILHMNAQVA DQFYELFQQQ
RDGDTMQGVP VVPSLGNNDV FPHNMFSLGP TLMTRQLQRI WAKFIPEEQR QAFEHDTSFF
VEVIPDRLAV ISFNTLYFFK SNPLVDNCND KAQPGHALLL WLGSVLEEMR ARNMKVWLSG
HVPPIPKNFE GSCYNKLAWW TYEYRDVIIG GLYGHMNVDH FYPADGKAAK KSIKRRGKAR
TKERNTQEQP LDILDDSVDN LFSGRGAMPL RKEKYMRRLF KDVYCPIAKR LEDKGKQEQS
YERYSMVHVA ASVIPTFNPG FRVWEYNLTG IDNAVAPAPW TRLVRRAQQI LSPLRKKKHG
PDRTLPPKKP KHLAAGPGHI PQALTPIRFT QYYADLAEIN KDYARELEAG RSHDEAAAAA
FRYKIEYTSE DEPYPMESLL VRDYVKLASK LTEDRTAWKT YVRRAFVSSG YRDN
