ID A0A1S3MDK5_SALSA Unreviewed; 1438 AA.
AC A0A1S3MDK5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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|RefSeq:XP_014001016.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014001016.1};
RN [1] {ECO:0000313|RefSeq:XP_014001016.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014001016.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014001016.1; XM_014145541.1.
DR GeneID; 106571936; -.
DR CTD; 23262; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR Bgee; ENSSSAG00000073972; Expressed in head kidney and 15 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:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 64..153
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 918..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 160307 MW; 32AF28BC2F4C97B9 CRC64;
MSKGGDAPDG GEHPRFFVGC DDNEGEELLD PGRVMGYDCL YENVEEEEED EDDEMYDSPP
ERQIVVGICA MSKKSKSKPM KEILERLCLF KYITVVTIEE EVILNEPVDN WPLCDCLISF
HSKGFPLDKA VAYEKLRNPF VINDLDLQYY IQDRREVYRI LKNQGILLPR YAVLNRDPAR
PEECNLVEGE DHVEVNGEVF QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS
VYSPESNVRK TGSYIYEEFM PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV
RYPVILNARE KLIAWKVCLA FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK
ILGNIIMREL APQFSIPWSI PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM
EVRHQRFFDL FEKCGGYKNK KLKLKKPKQL QEVLDIARQL LVEIGQNNDS EIEESKAKLE
QLKTVLEMYG HFSGINRKVQ MTYLPHGCPK TSSEEEDVRR DDPSLLLVLK WGGELTPAGR
VQAEELGRAF RCMYPGGQGD YAGFPGCGLL RLHSTYRHDL KIYASDEGRV QMTAAAFAKG
LLALEGELTP ILVQMVKSAN MNGLLDSDSD SLSSCQQRVK ARLHEILQRD RDFTAEDYEK
LAPTTSSSLI KSMQMIKNPV KTCDKVYALI QSLTLQIRQR MEDPKSADIQ LYHSETLDLM
LRRWAKLEKD FRMKNGRYNI SKIPDIYDCI KYDVQHNSSL NLSNTMEIYR LSKALADIVI
PQEYGIAQPE KLDIAKGYCT PLIRKIRSDL QRTQDDDTVN KLHPVYSRGV MSPERHVRTR
LYFTSESHVH SLLSILRYGA FCDETKDDQW KRAMEYLKVV SELNYMTQIV IMLYEDPNKD
PSSEERFHVE LHFSPGAKGC EDDKNLPSGF GYRPASRENE GSKKKSKEDN DEESANAKRD
EPDRAALMMF RPLVSDPIYI NRKCPLPRSK KIGSVESPLQ PDFIKTAAGK EESPLSVSSP
DSIGTWLHYT CGVGTGRRRR RSGDQITSSP VSPKSLAFTS SIFGSWQQVL SENNAHAQRP
GRLYSEHKLT PGVGSHCAGL FSTMVLGASS SAPNLQDYAR AHRKKLTSSG FLDEATRGSA
VKRFSISFAR HPTNGFELYS MVPSICPLET LHNSLSLKQI DDFLASIAAS HESLLDISAS
SPAAKKTPLN TYTPAKILPC PFTQGKKNVD KAATGISSSP TKDPRSGPAD PSPNAAAGDK
ASQPSPSQPT TESKAALQSS SEDLEPPAGL SATQNPATQH ASKDKLEPST PDKCVKQTLQ
HDAQSCKVPP QTQSGDVSPQ SPAQGAPSGK VPSKNPTQDN LTCKMSPHSP SKKIQTFPQD
APSGKVTTQA PSLDPTEKGS KTSPHDKVHQ GLNSKGTLGE GAMSFTTSKE REAKLDSK
//
