ID A0A3P9NHD8_POERE Unreviewed; 1116 AA.
AC A0A3P9NHD8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:ENSPREP00000009005.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009005.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009005.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009005.1};
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; A0A3P9NHD8; -.
DR STRING; 8081.ENSPREP00000009005; -.
DR Ensembl; ENSPRET00000009114.1; ENSPREP00000009005.1; ENSPREG00000006124.1.
DR GeneTree; ENSGT00390000009048; -.
DR OMA; AQIWACS; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006124; Expressed in caudal fin and 1 other cell type or tissue.
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 Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 65..154
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
SQ SEQUENCE 1116 AA; 126968 MW; CF0FE1C6B350CD8C CRC64;
MSEPCNGPRP VEERGRIRRD VPRFVIGCEE DEQDMGQMEA GMKNEMLHQD DMEVYENESP
SERQIVVGIC AMMKKSKSKP MTQILERLCK FDYIDVVIFP EEVILEEPVE KWPLCDCLIS
FHSKGFPLDK AVEYAKLRNP MLINDLNMQY FIQDRREVYR ILQEEGIDLP RYGVLNRDPD
DPEECNLVEG EDHVEVNGEV FPKPFVEKPV CAEDHNVYIY YPTSAGGGSQ RLFRKIGSRS
SVYSPESNVR KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE
IRYPVMLTAM EKLVARKVCL AFKQTVCGFD LLRANGHSYV CDVNGFSFVK NSMKYYDDCA
KVLGNMVMRE LAPQLHIPWS IPMEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK
MEVRHPLFFE LFKKYGGYKT GKLKLKKPKQ LQEVLDIARL LLVELGQHND CEIEEKKSKL
EQLKTVLEMY GHFSGINRKV QLTYLRNGQP KASSEEEDCK KDGPSLLLVL KWGGELTPAG
RVQAEELGRA FRCMYPGGQG DFAGFPGCGL LRLHSTYRHD LKIYASDEGR VQMTAAAFAK
GLLALEGELT PILVQMVKSA NMNGLLDSDS DSLTDCQQKV KARLHEIMQK DQDFTQDDFQ
KLAPTGSPSL VNSMKVIENP VKTCDKVYAL IQSLTSQIRK RLEDPKSADL QLYHSETLEL
MLQRWSKLER DFRMKNGRYD ISKIPDIYDC IKYDSQHNAS VGLEDTLELF RLSRALADIV
IPQEYGINKA EKLDIAQAYC VPLMKKIYLD LQRTHEDEAV NKLHPLYSRG VMSPGRHVRT
RLYFTSESHV HSLLSMFRYG GLLDEVKDQQ WKQAMDYLSA VTELNYMTQI VIMLYEDNNK
DPSSEERFHV ELHFSPGVKG CEDEENVPMG FGFRPASSEG SLEDLSQDQT DDALPVTELI
NLQRRSPMIR NRKTGSMEVE ESLPLSSIHN ALLRFEGCSM VPSIYPLETL HNSLSLKQVE
EFLSKVCESS GEAQAKAMKG GSYGSSTLTD VDVWRKFTSS SASLSDQRTS APLSRLCEGR
VRVFSQKQLC SQPCSRTHSD FDTDWSRCSL NRPSVW
//
