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Database: UniProt
Entry: A0A455BQF6_PHYMC
LinkDB: A0A455BQF6_PHYMC
Original site: A0A455BQF6_PHYMC 
ID   A0A455BQF6_PHYMC        Unreviewed;      1475 AA.
AC   A0A455BQF6;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-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_028351199.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028351199.1};
RN   [1] {ECO:0000313|RefSeq:XP_028351199.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028351199.1};
RG   RefSeq;
RL   Submitted (SEP-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_028351199.1; XM_028495398.2.
DR   Proteomes; UP000248484; Chromosome 11.
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: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:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365032};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
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          912..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1441..1475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1133..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1475 AA;  163516 MW;  436E3D39F02B3669 CRC64;
     MWSLPASEGE 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 MVYTVGPDYA HAEARKSPAL DGKVERDSEG KEIRYPVMLT
     AMEKLVARKV CVAFKQTVCG FDLLRANGHS FVCDVNGFSF VKNSMKYYDD CAKILGNTIM
     RELAPQFQIP WSIPTEAEDI PIVPTTSGTM MELRCVIAII RHGDRTPKQK MKMEVTHPRF
     FSLFEKHGGY KTGKLKLKRP EQLQEVLDIT RLLLAELEKE PGGEIEEKTG KLEQLKSVLE
     MYGHFSGINR KVQLTYYPHG VKASNEGQDP QGEALAPSLL LVLKWGGELT PAGRVQAEEL
     GRAFRCMYPG GQGDYAGFPG CGLLRLHSTF RHDLKIYASD EGRVQMTAAA FAKGLLALEG
     ELTPILVQMV KSANMNGLLD SDGDSLSSCQ HRVKARLHHI LQQDAPFGPE DYDQLAPTGS
     TSLLNSMAII QNPVKVCDQV FALIENLTYQ IQERMQDPKS VDLQLYHSET LELMLQRWSK
     LERDFRQKSG RYDISKIPDI YDCVKYDVQH NGSLGLQGTA ELLRLSKALA DVVIPQEYGI
     SREEKLEIAV GFCLPLLRKI LLDLQRTHED ESVNKLHPLY SRGVLSPGRH VRTRLYFTSE
     SHVHSLLSVF RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER
     FHVELHFSPG VKGVEEEGSA PTGCGFRPAS SENEEMKTDQ GSMEDLCPGK ASDEPDRALQ
     TSPQPSEGPG LPKRSPLIRN RKAGSMEVLS ETSSSRPGGY RLFSSSRPPT EMKQSGLGSQ
     CTGLFSTTVL GGSSSAPNLQ DYARSQGKKL PPASLKHRDE LLFVPAVKRF SVSFAKHPTN
     GFEGCSMVPT IYPLETLHNA LSLRQVSEFL SRVCQRHTDA QAQASAALFD SMHSNQTSDS
     PFSPPRTLHS PTLQLRQRSE KPPWYSSGPS STVSSAGPSS PTAVDGNCHF GFSHHPSLNS
     HVTEEHQGLG LLQETIGNGA QELPIEGEQE PFDRNQSPQE PPVETSQPCQ KVAEEVSQPC
     QNIPEEVSQP CQEVPDISQP CKENHDDVNQ TCQEVPQISQ PCQNASQLYQ KVSEEACELC
     QENSEEVNQP HQGVPVEAGR LVHGFPVGVG GLAQEILVEV GKPAQGIPEE LSQPCQKFSG
     DIGRLGQEAS AIILLSQDIP EVDKPSQEFP GEGDLHVQEV PEEVNQQQSY VVPELIDQLS
     GEDVPQVQYP SSNANPQSQS LTRDQNSPLP PATCD
//
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