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Database: UniProt
Entry: Q54PE2_DICDI
LinkDB: Q54PE2_DICDI
Original site: Q54PE2_DICDI 
ID   Q54PE2_DICDI            Unreviewed;       484 AA.
AC   Q54PE2;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN   ORFNames=DDB_G0284617 {ECO:0000313|EMBL:EAL65078.1};
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL65078.1, ECO:0000313|Proteomes:UP000002195};
RN   [1] {ECO:0000313|EMBL:EAL65078.1, ECO:0000313|Proteomes:UP000002195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000313|EMBL:EAL65078.1,
RC   ECO:0000313|Proteomes:UP000002195};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RG   The Dictyostelium discoideum Sequencing Consortium;
RA   Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA   White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA   Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA   Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA   Noegel A.A., Barrell B., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases to synthesize the diphosphate group-containing inositol
CC       pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC       diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC       InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC       of cellular processes, including apoptosis, vesicle trafficking,
CC       cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC       hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC         inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC         ChEBI:CHEBI:456216; EC=2.7.4.24;
CC         Evidence={ECO:0000256|RuleBase:RU365032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC         + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC         + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU365032}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000256|RuleBase:RU365032}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL65078.1}.
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DR   EMBL; AAFI02000070; EAL65078.1; -; Genomic_DNA.
DR   RefSeq; XP_638433.1; XM_633341.1.
DR   AlphaFoldDB; Q54PE2; -.
DR   SMR; Q54PE2; -.
DR   STRING; 44689.Q54PE2; -.
DR   PaxDb; 44689-DDB0233955; -.
DR   GeneID; 8624683; -.
DR   KEGG; ddi:DDB_G0284617; -.
DR   dictyBase; DDB_G0284617; ppip5K.
DR   eggNOG; KOG1057; Eukaryota.
DR   HOGENOM; CLU_564327_0_0_1; -.
DR   InParanoid; Q54PE2; -.
DR   OMA; SIGICAM; -.
DR   PhylomeDB; Q54PE2; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IMP:dictyBase.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IMP:dictyBase.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11950; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR037446; His_Pase_VIP1.
DR   InterPro; IPR040557; VIP1_N.
DR   PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   Pfam; PF08443; RimK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365032};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365032};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT   DOMAIN          4..93
FT                   /note="VIP1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18086"
FT   DOMAIN          243..287
FT                   /note="ATP-grasp fold RimK-type"
FT                   /evidence="ECO:0000259|Pfam:PF08443"
FT   REGION          341..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  55669 MW;  D43FED8C25D46C4C CRC64;
     MAKISLGICC MEEKLKCNVM KYFIKKLKEF KELEIIEFDS NTIFNLPIQE WPIVDSFLSF
     YSNGFPLEKA IRYWKLRRPY LVNDLELQLL LQDRQKVNKI LEDNNIPCPK SLYVLRDPIT
     NNLITPNFNQ SDDYIEVNGN RIYKPFIEKP FNSDDHNNYI YYPKSQGGGC RKLFRKVGNN
     SSDYFNDINT IRDKGSYTYE EFLKIDDFKD VKIYSTKSFS YSELRKSPSV DGFVERTTMG
     KEKRSVTNLS DQEVNISFKI NKAFKQFVCG FDILRVNGIS YVCDVNGWSF VKGDHFKTFY
     DSTSKSLFEK LFNHFKNRNT IITNINTNTI HNCSIGIAEN APQPSSTNTS PEQPTFDFSP
     SSSPTNLYPS SSSPLFNLNL NNLNNLNNLN NNNNSNNNSI GNDQNNSNST VTTPPHFDLI
     SSSAYDKHHQ DIFSRHIRVY NHQNLNLNNN NNNNNKNNNN NNNNIFSTIS SSISVDDSFT
     GSAI
//
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