ID A0A3Q1AP60_AMPOC Unreviewed; 1124 AA.
AC A0A3Q1AP60;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN Name=PPIP5K1 {ECO:0000313|Ensembl:ENSAOCP00000003137.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000003137.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000003137.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC group-containing inositol pyrophosphates diphosphoinositol
CC pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC respectively called InsP7 and InsP8, regulate a variety of cellular
CC processes, including apoptosis, vesicle trafficking, cytoskeletal
CC dynamics, exocytosis, insulin signaling and neutrophil activation.
CC Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to
CC produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1,
CC produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when
CC cells are exposed to hyperosmotic stress.
CC {ECO:0000256|ARBA:ARBA00037056}.
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|ARBA:ARBA00034629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000256|ARBA:ARBA00034629};
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: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514,
CC ECO:0000256|RuleBase:RU365032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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DR AlphaFoldDB; A0A3Q1AP60; -.
DR STRING; 80972.ENSAOCP00000003137; -.
DR Ensembl; ENSAOCT00000010310.1; ENSAOCP00000003137.1; ENSAOCG00000000304.1.
DR GeneTree; ENSGT00390000009048; -.
DR OMA; AWPRCDA; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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 PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF11; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 1; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|RuleBase:RU365032}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transferase {ECO:0000256|RuleBase:RU365032};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 912..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 844..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 126243 MW; 96A98508C5493D55 CRC64;
MGYLSAMSAL YKVQQSLSVY VSLFIVFACS LQMSDLLNNF SACVCKPGFP LDKAVSYAKL
RNPLHINDLN MQYYIQDRRE VYRILQEEGI DLPRYAVLNR DPDKPEECNL VEGEDHVEVN
GEIFQKPFVE KPVCAEDHNV YIYYPTSAGG GSQRLFRKIG SRSSVYSPES SVRKTGSYIY
EEFMPTDGTD VKVYTVGPDY AHAEARKSPA LDGKVERDSE GKEVRYPVML SAMEKLVARK
VCLAFKQTVC GFDLLRANGH SYVCDVNGFS FVKNSMKYYD DCAKILGNIV MRELAPQFQI
PWSIPTEAED IPIVPTTSGT MMELRCVIAV IRHGDRTPKQ KMKMEVRNPM FFDLFEKYGG
YKTGKLKLKK PKQLQEVLDI TRQLLADLGQ HNDCEIEEKK SKLEQLKTVL EMYGHFSGIN
RKVQLTYLPH GQPKTSSEEE DTRKEGPSLL LVLKWGGELT PAGRVQAEEL GRAFRCMYPG
GQGDYAGFPG CGLLRLHSTY RHDLKIYASD EGRVQMTAAA FAKGLLALEG ELTPILVQMV
KSANMNGLLD NDSDSLSSCQ HRVKARLHEI LQKDREFTDE DYDRLAPTCS ASLVNSMKIV
ENPVATCDQV YALIQSLTSQ IRKRMEDPKS ADLQLYHSET LELMLQRWSK LERDFRMKNG
RYDISKIPDI YDCVKYDVIH NATLGLEDTL ELFRLSRALA DIVIPQEYGI NKVEKLDIAY
AYCLPLVRKI QLDLQRTHED ESVNKLHPLY SRGVMSPGRH VRTRLYFTSE SHVHSLLSIF
RYGGLLDEEK DQQWKRAMDY LSAVSELNYM TQIVIMLYED NNKDLTSEER FHVELHFSPG
VKGVEEEENA PTGFGFRPAS AENGQKQPDP GSLEDLSRDE TDRAVPLSEP ITIQRRSPLI
RNHKTGSMEA EALNYASVTV LFLTAHLVII IVSSIKILSN RKSRSQCAGL FSTTVLGGSS
SAPNLQDYAR AHRKKFSTGS LSYKDELLSM PAVKRFSVSF AKHPTNGFEG CSMVPSIYPL
ETLHNSLSLK QVNEFLTGVC QSAVDPHTRT TRGLTLLFSS KCFFLSYTSS VGLSCVPADS
SGPSSTVSSA GPSSPTTADT SPRFSFSDKI SLTPQGSEET HSSQ
//
