ID A0A3P8QZI4_ASTCA Unreviewed; 1145 AA.
AC A0A3P8QZI4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:ENSACLP00000035075.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000035075.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000035075.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000035075.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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-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: 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}.
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DR AlphaFoldDB; A0A3P8QZI4; -.
DR Ensembl; ENSACLT00000035901.1; ENSACLP00000035075.1; ENSACLG00000023567.1.
DR GeneTree; ENSGT00390000009048; -.
DR Proteomes; UP000265100; Chromosome 7.
DR Bgee; ENSACLG00000023567; Expressed in zone of skin and 7 other cell types or tissues.
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; 3.40.50.11950; -; 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 InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF13; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 1..83
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 866..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 128988 MW; 1F494F6C555316DA CRC64;
MTKKSKSKPM TQILERLCKF DYIDVVIFPE EVILEEPVEK WPLCDCLISF HSKGFPLDKA
VEYAKLRNPL LINDLNMQYF IQDRREVYRI LQEEGIDLPR YAVLNRDPDN PEECNLVEGE
DQVEVNGEVF HKPFVEKPVC AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESSVRK
TGSYIYEEFM PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEI RYPVMLTAME
KLVARKVCLA FKQTVCGFDL LRANGHSFVC DVNGFSFVKN SMKYYDDCAK VLGNMVMREL
APQLHIPWSI PMEAEDIPIV PTTSGTMMEL RCVIAIIRHG DRTPKQKMKM EVRHPLFFEL
FEKYGGYKTG KLKLKKPKQL QEVLDIARLL LVELGQHTDC EIEEKKSKLE QLKTVLEMES
SLNDNQYGHF SGINRKVQLT YLRNGKPKAS SEEEDSKKDG PSLLLVLKWG GELTPAGRVQ
AEELGRAFRC MYPGGQGDYA GFPGCGLLRL HSTYRHDLKI YASDEGRVQM TAAAFAKGLL
ALEGELTPIL VQMVKSANMN GLLDSDSDSL TDCQQKVKAR LHEIMQKDQD FTEQDYQKLA
PTGSPSLVNS MKVIENPVKT CDKVYALIQS LTSQIRKRLE DPKSADLQLY HSETLELMLQ
RWSKLERDFR MKNGRYDISK IPDIYDCIKY DLQHNASLDL EDTRELFRLS RALADIVIPQ
EYGINRAEKL DIAQAYCVPL MKKIQLDLQR THEDEAVNKL HPLYSRGVMS PGRHVRTRLY
FTSESHVHSL LSIFRYGGLL NEEKDQQWKQ AMDYLSAVTE LNYMTQIVIM LYEDNNKDPS
SEERFHVELH FSPGVKGCED EETIPLGFGF RPASSENEDK KPNQGSLEDL SQDEPDQALQ
VSDPINIQRR SPMIRNRKTG SMEVLSETSP THSAKGCTSH RLFISCSRQS PEIKPASGLG
SLCSGLFSAS ALGVSCSAPN LRDYVRTHHR HHHPKPPLSP GSLPCKSGMF ELLSMPAVKR
FSVSYARHPT NGFEGCSMVP SIYPLETLHN SLSLKQVDEF LNSVCESNSE VQAKTMKALS
GLFASQSQIS LYSPQQPLSS SGSEASLRPP GQPLWHGSIP SSAVSSAGPS SPITESSGLN
FSFSE
//
