ID A0A671XPH9_SPAAU Unreviewed; 1129 AA. AC A0A671XPH9; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 14-DEC-2022, entry version 8. DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032}; DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032}; OS Sparus aurata (Gilthead sea bream). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Spariformes; Sparidae; Sparus. OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010053088.1, ECO:0000313|Proteomes:UP000472265}; RN [1] {ECO:0000313|Ensembl:ENSSAUP00010053088.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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-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|ARBA:ARBA00033672}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; CC Evidence={ECO:0000256|ARBA:ARBA00033672}; 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|ARBA:ARBA00033696}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; CC Evidence={ECO:0000256|ARBA:ARBA00033696}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU365032}. CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1 CC subfamily. {ECO:0000256|ARBA:ARBA00005609, CC ECO:0000256|RuleBase:RU365032}. 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 AlphaFoldDB; A0A671XPH9; -. DR Ensembl; ENSSAUT00010055804.1; ENSSAUP00010053088.1; ENSSAUG00010019615.1. DR GeneTree; ENSGT00390000009048; -. DR Proteomes; UP000472265; Unplaced. 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; IEA:UniProtKB-EC. 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:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07061; HP_HAP_like; 1. DR Gene3D; 3.40.50.1240; -; 1. DR InterPro; IPR033379; Acid_Pase_AS. DR InterPro; IPR000560; His_Pase_clade-2. DR InterPro; IPR037446; His_Pase_VIP1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR040557; VIP1_N. DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1. DR Pfam; PF00328; His_Phos_2; 1. DR Pfam; PF18086; PPIP5K2_N; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU365032}; KW Reference proteome {ECO:0000313|Proteomes:UP000472265}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}. FT DOMAIN 31..120 FT /note="PPIP5K2_N" FT /evidence="ECO:0000259|Pfam:PF18086" SQ SEQUENCE 1129 AA; 127667 MW; ABBCB1D5BF0F067F CRC64; YPLLIVLSNG DKNHEQSDEL KVCSSPPERQ IVVGICAMMK KSKSKPMTQI LERLCKFDYI NVVIFPEEVI LEEPVEKWPL CDCLISFHSK GFPLDKAVEY AKLRNPLLIN DLNMQYYIQD RREVYRILRE EGIDLPRYAV LNRDPDNPEE CNLVEGEDHV EVNGEVFPKP FVEKPVCAED HNVYIYYPTS AGGGSQRLFR KIGSRSSVYS PESSVRKTGS YIYEEFMPTD GTDVKVYTVG PDYAHAEARK SPALDGKVER DSEGKEIRYP VMLTSMEKLV ARKVCLAFKQ TVCGFDLLRA NGHSFVCDVN GFSFVKNSMK YYDDCAKVLG NMVMRELAPQ FHIPWSIPME AEDIPIVPTT SGTMMELRCV IAIIRHGDRT PKQKMKMEVR HPLFFELFDK YGGYKSGKLK LKKPKQLQEV LDIARLLLVE LGQHTDCEIE EKKSKLEQLK TVLEMYGHFS GINRKVQLTY LRNGQPKASS EEEDSKKDGP SLLLVLKWGG ELTPAGRVQA EELGRAFRCM YPGGQGDYAG FPGCGLLRLH STYRHDLKIY ASDEGRVQMT AAAFAKGLLA LEGELTPILV QMVKSANMNG LLDSDSDSLT DCQQKVKARL HEIMQKDQEL TQDDYQKLAP TGSPSLVNSM KVIENPVKTC DKVYGLIQSL TSQIRKRLED PKSADLQLYH SETLELMLQR WSKLERDFRT KNGRYDISKI PDIYDCIKYD SQHNASLGLE DTLELFRLSR ALADIVIPQE YGISKAEKLD IAQAYCVPLM KKIQLDLQRT HEDEAVNKLH PLYSRGVMSP GRHVRTRLYF TSESHVHSLL SIFRYGGLLD EEKDWQWKQA MDYLSAVSEL NYMTQIVIML YEDNDKPSSE ERFHVELHFS PGVKGCEDEE NVPLGYGFRP ASSEPNQGSL EDLSQDQVDQ ALPVSEPINI QRRSPMIRNR KTGSMEVPDL SVSGADVMLC SLCSGLFSAS ALGVSCSAPN LRDYVRTHHH HHRKPPLSPG SLPIGLFSMP AVKRFSVSFA RHPTNGFEGC SMVPSIYPLE TLHNSLSLKQ VDEFLNNVCE SSSEAHAKTM KGRPADESAP YVNKKHWAAI KATRTFLPSP NIILHYHQEH HSYLDDLSSA GVEPAQQSS //