ID A0A3B1IZ09_ASTMX Unreviewed; 1356 AA.
AC A0A3B1IZ09;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|Ensembl:ENSAMXP00000035307.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000035307.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000035307.1}
RP IDENTIFICATION.
RG Ensembl;
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_007255377.1; XM_007255315.2.
DR Ensembl; ENSAMXT00000045128.1; ENSAMXP00000035307.1; ENSAMXG00000011364.2.
DR GeneTree; ENSGT00390000009048; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000011364; Expressed in pharyngeal gill and 14 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:UP000018467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 60..149
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 914..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 152330 MW; 02F4C05BCBEA2907 CRC64;
MSETEDVDHP RFFVGADDAE GEELLDPGRV LGYDCLYENV EEEDEDADEE EYDSPPERQI
VVGICAMAKK SKSKPMKEIL ERLCLFKYIT VVTFEEEVIL SEPVENWPLC DCLISFHSKG
FPLDKAVAYE KLRNPFVIND LDLQYFIQDR REVYRILKAE GIQLPRYAVL NRDPARPQEC
NLVEGEDHVE VNGEIFQKPF VEKPVSAEDH NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP
ESNVRKTGSY IYEEFMPTDG TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV
ILNAREKLIA WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN
IVMRELAPQF QIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP KQKMKMEVRH
QRFFDLFGKY EGYKSGKLKL KKPKQLQEVL DTARQLLVEL GQNNDTEIEE SKAKLEQLKT
VLEMYGHFSG INRKVQLTYL PHGCPKTSSE EEDVRRDDPS LLLVLKWGGE LTPAGRVQAE
ELGRAFRCMY PGGQGDYAGF PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL
EGELTPILVQ MVKSANMNGL LDSDSDSLNS CQQKVKARLH DILQKDRDFA SEDYEKLAPT
TSTSLVKSMQ MIKNPVKTCD KVYSLIQNLT LQIRQRMEDP KSADIQLYHS ETLELMLRRW
SKLEKDFKMK NGRYNISKIP DIYDCIKYDV QHNSSLKLDN TMEIYRLSKA LADIVIPQEY
GISQAEKLDI AKGYCTPLIR KIRSDLQRTQ DDDTVNKLHP VYSRGVMSPE RHVRTRLYFT
SESHVHSLLS ILRYGALCDE TKDEQWKRAM DYLKVVSELN YMTQIVIMLY EDPNKDPSSE
ERFHVELHFS PGAKGCEEDK NLPSGFGYRP ASRENEGSKK KSQNDSDEET SSSLKRDEPD
RALVMFRPMV SDPIYIHRKS PLPRSKKIGS VEEESPLSVS SPESIGTWIH YTCGVGTGRR
RRRSGDQITS SPVSPKSLAF TSSIFGSWQQ VLSENNSHTR PGRLHTEQKL TTGMGFELYS
MVPSICPLET LHNSLSLKQV DDFLASIAKS HESLLDISGC SPAVQGKKAP LNTYTPAKVL
PCPFTQSLAK KSPEKTSPVR GGSPSRASRP VQTNLPQTNL PLQGASGDMR SQLNSTEQTT
GSKAATQPKT TEPQQATAIS TSASPLPACN KGQLQSASQE TQERQPSSTR SIPSFTITTH
HNVTAAVTKE HQISSLENHC HITSQQAKTQ EGQSGAKSVV DTPKDKSTKQ TSQKERCDGT
VQPCCATTVT TKEQELSAAV QKEQNAVGDF TKLGKP
//
