PPN1_CRYNJ
ID PPN1_CRYNJ Reviewed; 678 AA.
AC Q5KH67;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Endopolyphosphatase;
DE EC=3.6.1.10;
GN Name=PPN1; OrderedLocusNames=CNE01080;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017345; AAW43547.1; -; Genomic_DNA.
DR RefSeq; XP_570854.1; XM_570854.1.
DR AlphaFoldDB; Q5KH67; -.
DR SMR; Q5KH67; -.
DR STRING; 5207.AAW43547; -.
DR PaxDb; Q5KH67; -.
DR PRIDE; Q5KH67; -.
DR EnsemblFungi; AAW43547; AAW43547; CNE01080.
DR VEuPathDB; FungiDB:CNE01080; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_2_0_1; -.
DR InParanoid; Q5KH67; -.
DR OMA; LRFQDTI; -.
DR OrthoDB; 1116351at2759; -.
DR Proteomes; UP000002149; Chromosome 5.
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 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..678
FT /note="Endopolyphosphatase"
FT /id="PRO_0000058545"
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..678
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 70..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 678 AA; 77209 MW; 8B3C696309AC617D CRC64;
MRSPLLASLF ALALSIASSE AAISSTEQVP LSGSVPQLDH SELQNVRINK KRPLKGRFLH
ITDIHPDPHY KTGSTFDSGC HRKPKKDGKS EGKKATENER GNEDLDDKEF DTLIKNEDLA
GKWGTAVSDC DCPMSLVNIT FDWLKEEWAN EVDFVVWTGD NARHDIDRRI PRTPKEIFDS
NRMIVDRMLD AFGRDMPIVP SIGNNDIYPH NVLAAGPSRI TEEFLLIWKH FIPSEAAHVF
ERGAYFSVEV IPDRLAVISL NTLFWYDANT LVDGCRDHSN DPGALEMDWL EVQLNNFRQR
GMQVWLTGHV PPHMNHYYDN CYLRYGDLAL RYQDTIVGHL FGHMNVDHFF FIDVDELEAT
SELTSTSSNT TLSDLPLLHG PRLPRPGPGK YTAMGRSGAR KLEEELRKDF GQMPGPGILK
LKDYAVMNVA PSVIPTYYPG IRIFSYNISD EEDSFDQGHS YQGADELLDD EDEGDELEEL
ELPSDNGFFG GLDERENEDI EILKGSGGHR HDVPKGDCSL PSNEDKPHCT FKRKPRHYSK
RSPSRTNRAL SPLGYTQFYL PSMMKQKKRP KWEVEYTTYK VKTLVPSSPE NTTQPLPVPL
HLLPRYDPSI FSKPKNKTEE KEVAKKTAKF YKAVKAVTPY RMKDLTIGSW VKLARMLVLE
KKRWKKFAEL MLVSTETD
