ID A0A3Q0H859_ALLSI Unreviewed; 1355 AA.
AC A0A3Q0H859;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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_025068254.1,
GN ECO:0000313|RefSeq:XP_025068256.1, ECO:0000313|RefSeq:XP_025068257.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025068254.1};
RN [1] {ECO:0000313|RefSeq:XP_025068254.1, ECO:0000313|RefSeq:XP_025068256.1}
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_025068254.1; XM_025212469.1.
DR RefSeq; XP_025068256.1; XM_025212471.1.
DR RefSeq; XP_025068257.1; XM_025212472.1.
DR STRING; 38654.A0A3Q0H859; -.
DR KEGG; asn:102386038; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000189705; 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:UP000189705};
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 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 150601 MW; 16B92BF5E3C6A0B4 CRC64;
MSSLTTPTEG EGSAPRFFVG SRDDETDCLG PDMNPDEIDF FEDEEEEESP PERQIVVGIC
AMTKKSKSKP MTQILERLCK FEYITVVVMG EDVILNEPVE NWPLCDCLIS FHSKGFPLDK
AVAYAKLCKP FLINDLDMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPD KPNECNLVEG
EDHVEVNGIM FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNIIMRE
LAPQFHIPWS IPTEAEDIPI VPTTSGTMME LRCVIAVIRH GDRTPKQKMK MEVKHPRFFE
LFEKYDGYKT GKLKLKRPEQ LQEVLDIARL LVVELGTQND SEMEERKSKL EQLKSVLEMY
GHFSGINRKV QLTYLSHGHP KASSEDEEAR KEAAPSLLLV LKWGGELTPA GRVQAEELGR
AFRCMYPGGQ GDYAGFPGCG LLRLHSTYRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHEIMQ KDTMFGDEDY EKLAPTGSVS
LTNSMAFIQN PVEVCNQVFA LIENLTTQIQ KRLEDPKSAD LQLYHSETLE LMLQRWSKLE
RDFRMKNGRY DISKIPDIYD CIKYDVQHNS TLQLEGTAEL FKLSKALADV IIPQEYGISK
EEKLEIAIGF CLPLVKKIQL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
VHSLLSIFRY GGLLDESKDQ QWKRAMDYLS AVSELNYMTQ IVIMLYEDNN KDPSSEERFH
VELHFSPGVK GCEEDGNVPT GFGFRPASAE NEEKKPDQGS MEDLSKVKNI TETDRAQLRS
PLPSEMVSVQ RRSPLIRNRK TGSMEVLSES SSKSGGYRLF STYSRQASEM KQSGLGSQCT
GLFSTTVLGG SSSAPNLQDY ARSHGKKFAT SLTYKDELLS MPAVKRFSVS FAKHPTNGFE
GCSMVPTIYP LETLHNSLSL RQVNAFLTAL CRSCSVSHAR SSSALFDSMM GTPAPGDPFL
SQRILSVSAL PLRPRSDKPP WYSSGPSSTV SSAGPSSPAS VENYARFSFT EKPSISPQRS
EERLSGQAPA PGEERLSGQA PAPGEERLSG QAPAPGAGEA PXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXPGAEQAPE QVEGAVAWGE AEPAGEVLEP AEAGLPAPEE
TLASCDEEES EGDSTGPGPP AEDTASQPPP QDVHN
//
