PPN1_YARLI
ID PPN1_YARLI Reviewed; 747 AA.
AC Q6CEE7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Endopolyphosphatase;
DE EC=3.6.1.10;
GN Name=PPN1; OrderedLocusNames=YALI0B16236g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382128; CAG83218.1; -; Genomic_DNA.
DR RefSeq; XP_500965.1; XM_500965.1.
DR AlphaFoldDB; Q6CEE7; -.
DR SMR; Q6CEE7; -.
DR STRING; 4952.CAG83218; -.
DR EnsemblFungi; CAG83218; CAG83218; YALI0_B16236g.
DR GeneID; 2906836; -.
DR KEGG; yli:YALI0B16236g; -.
DR VEuPathDB; FungiDB:YALI0_B16236g; -.
DR HOGENOM; CLU_013424_1_1_1; -.
DR InParanoid; Q6CEE7; -.
DR OMA; MKAILMG; -.
DR Proteomes; UP000001300; Chromosome B.
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 InterPro; IPR041805; ASMase/PPN1_MPP.
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..747
FT /note="Endopolyphosphatase"
FT /id="PRO_0000058550"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..747
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 570..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..626
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 85087 MW; 9F6C5E25D8D75012 CRC64;
MLPKTLTIWA SLASLAVAQS GQVVFAKNAD GKFVHSTDDL DQGQRKIRGK FLHITDIHPD
PYFHVGAVAE DKCHVDPDHK DSDYPDEDSE LVWFRATGKK KHNHHKGKDH EKMPKAGYYG
HPLSSCDGPI SLMNATFDWI DQNIRDEIDF IIWTGDNVRH DNDNRYPRLE QDIFGYNQIV
SSKFHELFRY NETRDGEGHN GGGDPQHPLV IPIIPSLGNN DVFPHNLYLA GPSFQSRRML
QIWSEFVPEA QQHIFSRGSY YFQEVITGKL AVISLNTLYF YKSNPMSDGC DEKTDPGYKH
LVWLGVVLDE MRQRGMKVWL SGHVPPVEKN YEDSCHLKLA YWLTEYRDII VGSVFGHMNI
DHFVVMDPKK IEKAQSQDLG TPGLGYKSHV TDFLDVAISA SHPVHTFGSI YKRNYIESVR
EDYSEIPGPK KWLDEYASNF AIAHVSPSVI PNYFPSLRVW EYNITGLGEE IGNPPHPPPS
FRAWSDVLEE FERDYAQDVM DEIEVEWFDA NSDVIEAEDN DGDDDEDENE DDPEMLTEEA
IKEGVANINP ETGTLASIFG GLKFWKSSTA VATSSEPESD DYDSDLDAER KKGKKKGKKG
KKGKKGKKGK KKKGKKGKKG KKGKRDKSMP PKFPKDLQPG PAYIPQLFTP IGYTQYYANI
TQFNKEYKKT GASNFEYVVE YTTNDAPYNF EHLTVRNWVE LARVLGKNFR DLDLEAEKSK
SDQLWKVYMD RAFVGTGAEY LEEPDDD
