ID A0A2K5MZI9_CERAT Unreviewed; 1129 AA.
AC A0A2K5MZI9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=PPIP5K2 {ECO:0000313|Ensembl:ENSCATP00000030629.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030629.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000030629.1}
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; A0A2K5MZI9; -.
DR Ensembl; ENSCATT00000054892.1; ENSCATP00000030629.1; ENSCATG00000038434.1.
DR GeneTree; ENSGT00390000009048; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000038434; Expressed in colon and 12 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:SF10; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 2; 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:UP000233060};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 49..138
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 903..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 128334 MW; A5F2B0C07FA4A348 CRC64;
SNKIKMSEAP RFFVGPEDTE INPGNYRHFF HHADEDDEEE DDSPPERQIV VGICSMAKKS
KSKPMKEILE RISLFKYITV VVFEEEVILN EPVENWPLCD CLISFHSKGF PLDKAVAYAK
LRNPFVINDL NMQYLIQDRR EVYSILQAEG ILLPRYAILN RDPNNPKECN LIEGEDHVEV
NGEVFQKPFV EKPVSAEDHN VYIYYPTSAG GGSQRLFRKI GSRSSVYSPE SNVRKTGSYI
YEEFMPTDGT DVKVYTVGPD YAHAEARKSP ALDGKVERDS EGKEVRYPVI LNAREKLIAW
KVCLAFKQTV CGFDLLRANG QSYVCDVNGF SFVKNSMKYY DDCAKILGNI VMRELAPQFH
IPWSIPLEAE DIPIVPTTSG TMMELRCVIA VIRHGDRTPK QKMKMEVRHQ KFFDLFEKCD
GYKSGKLKLK KPKQLQEVLD IARQLLMELG QNNDSEIEEN KPKLEQLKTV LEMYGHFSGI
NRKVQLTYLP HGCPKTSSEE EDSRREEPSL LLVLKWGGEL TPAGRVQAEE LGRAFRCMYP
GGQGDYAGFP GCGLLRLHST YRHDLKIYAS DEGRVQMTAA AFAKGLLALE GELTPILVQM
VKSANMNGLL DSDSDSLSSC QQRVKARLHE ILQKDRDFTA EDYEKLTPSG SISLIKSMHL
IKNPVKTCDK VYSLIQSLTS QIRHRMEDPK SSDIQLYHSE TLELMLRRWS KLEKDFKTKN
GRYDISKIPD IYDCIKYDVQ HNGSLKLENT MELYRLSKAL ADIVIPQEYG ITKAEKLEIA
KGYCTPLVRK IRSDLQRTQD DDTVNKLHPV YSRGVLSPER HVRTRLYFTS ESHVHSLLSI
LRYGALCNES KDEQWKRAMD YLNVVNELNY MTQIVIMLYE DPNKDLSSEE RFHVELHFSP
GAKGCEEDKN LPSGYGYRPA SRENEGRRPF KTDNDDEPHT SKRDEVDRAV ILFKPMVSEP
IHIHRKSPLP RSRKMATNDV VSENANYLRT PRTLVEQKQN PTVGFELYSM VPSICPLETL
HNALSLKQVD EFLASIASPS SDVPRKTPEI SSTALRSSPI MRKKVSLNTY TPAKILPTPP
ATLKSTKASS KPAASGPSSA VVPNTSSRKK SITSKTETHE HKKNTGKKK
//
