ID A0A452C560_BALAS Unreviewed; 1394 AA.
AC A0A452C560;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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|RefSeq:XP_028018096.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028018096.1};
RN [1] {ECO:0000313|RefSeq:XP_028018096.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028018096.1};
RG RefSeq;
RL Submitted (JAN-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 RefSeq; XP_028018096.1; XM_028162295.1.
DR Proteomes; UP000261681; 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 InterPro; IPR040557; VIP1_N.
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 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 55..144
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 902..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 154807 MW; 5C1740CF92859A42 CRC64;
MWSLPTSEGE SATAHFFLGA GDEGLGTRGI GMRTEESDSE LLEDEEDEVP PEPQIIVGIC
AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFS
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY
GHFSGINRKV QLTYYPHGVK ASNEGQDPQG EALAPSLLLV LKWGGELTPA GRVQAEELGR
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS
LLNSMAIIQN PVKVCDQVFA LIENLTHQIQ ERMQDPKSVD LQLYHSETLE LMLQRWSKLE
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
EEKLEIAVGF CLALLRKILL DLQRTHEDEY SRGVLSPGRH VRTRLYFTSE SHVHSLLSVF
RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER FHVELHFSPG
VKGVEEEGSA PTGCGFRPAS SENEEMKTDQ GSMEDLCPGK ASDEPDRALQ TSPQPSEGPG
LPKRSPLIRN RKAGSMEVLS ETSSSRPGGY RLFSSSRPPA EMKQSGLGSQ CTGLFSTTVL
GGSSSAPNLQ DYARSQGKKL PPASLKHRDG FEGCSMVPTI YPLETLHNAL SLRQVSEFLS
RVCQRHTDAQ AQASAALFDS MHSNQTSDSP FSPPRTLHSP TLQLRQRSEK PPWYSSGPSS
TVSSAGPSSP TAVDGNCHFG FSDHPSLNSH VTEEHQGLGL LQESIGNGAQ ELPIEREQEP
FERNQSPQEP PVETSQPCQK VAEEVSQPCQ DIPEEVSQPC QEVPDISQPC KEKHDDVNQT
CQEVPQISQP CQNASQLYQK VSEEACELCQ ENSEEVNQPR QGVPVEVGRL VHGFPVGVGG
LAQEILMEVG KPAQEIPEEL SQPCQEFSGD IGRLAQEASA IILLSQDIPE VDKPSQEFPG
EGDLYVQEVP EEVN
//
