ID A0A1U8BNP1_MESAU Unreviewed; 1559 AA.
AC A0A1U8BNP1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-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=Ppip5k1 {ECO:0000313|RefSeq:XP_012967790.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012967790.1};
RN [1] {ECO:0000313|RefSeq:XP_012967790.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_012967790.1; XM_013112336.1.
DR GeneID; 101838924; -.
DR CTD; 9677; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000189706; 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; 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:UP000189706};
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 916..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 173722 MW; C9127BFB788F218E CRC64;
MWSLPANEDE STTAHFFLGA GDEGLGTCEI GMRMEESDSE LLEDEEDEVP PEPQIIVGIC
AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA CPEECNLIEG
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE VRYPVMLTAM
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFA
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG VEIEEKTGKL EQLKSVLEMY
GHFSGINRKV QLTYYPHGVK ASNEGQDLPR ETLTPSLLLV LKWGGELTPD GRVQAEELGR
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS
LLNSMSVIQN PVKVCDQVFS LIENLTHQIR ERMQDPSSVD LQLYHSETLE LMLQRWSKLE
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LHLSKALADV VIPQEYGISR
EEKMEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
VHSLLSVFRY GGLLDETQDA QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH
VELHFSPGVK GIEEGSAPAG CGFRPASSEN EEMKPDQGSI ENLCSGKASD EPDRALQTSP
QPIEGTGLPR RSPLIRNRKA GSMEVMNMQC TGNLDLIPLR GRRRRRSGDL PRLSPAIGLQ
PRAVSTTHLA SCTQVLSETS SSRPGGYRLF SSSRPPTEMK QSGLGSQCTG LFSTTVLGGS
SSAPNLQDYA RSHGKKLPPA SLKHRDELLD DQHPVVRLLR TFSSDCPRGW PVSLDATLAH
HLHQCSYHLR LFRNWLRSGQ DDPECLYGFE GCSMVPTIYP LETLHNALSL RQVSEFLTKV
CQRHTDAHAQ ASAALFDSMH SNQASDSPFS PPRALHSPPL QLRHRSEKPP WYSSGPSSTV
SSAGPSSPTT VDGNSHFGFS DQSSVDTHVT EENQGLGLLQ ETPGDGTQEF PIERQQELIE
SNQSPQEPSV EISPLGQGVA EVSQTCQEVP DTTQTCHDIL EEVGQHNQEV PDISQLFLKN
LDTATNTCQP CQKASQLSRE VYQLCQDNPE ENNQLCQEVP VELGRMAHGF PVNIDSMVQE
TFIEIGRPTQ EIPEGMGPPF QEFSVEVGML AQEVPAIIEL SQGILEADDP SQELTEETGL
QAQEVSEEID QDSRVVPEVV DELPSDDIPQ GQCLSSDVNT ESQSLAHGQH FSLPPAMYN
//
