ID A0A182R3Y8_ANOFN Unreviewed; 576 AA.
AC A0A182R3Y8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase {ECO:0000256|ARBA:ARBA00014846, ECO:0000256|RuleBase:RU364126};
DE EC=2.7.1.158 {ECO:0000256|ARBA:ARBA00012023, ECO:0000256|RuleBase:RU364126};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN000879-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN000879-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN000879-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). {ECO:0000256|RuleBase:RU364126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000256|RuleBase:RU364126};
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2. {ECO:0000256|RuleBase:RU364126}.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family.
CC {ECO:0000256|ARBA:ARBA00007229}.
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DR AlphaFoldDB; A0A182R3Y8; -.
DR STRING; 62324.A0A182R3Y8; -.
DR EnsemblMetazoa; AFUN000879-RA; AFUN000879-PA; AFUN000879.
DR VEuPathDB; VectorBase:AFUN000879; -.
DR VEuPathDB; VectorBase:AFUN2_007490; -.
DR OrthoDB; 8233at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.200.110; Inositol-pentakisphosphate 2-kinase, N-lobe; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; INOSITOL POLYPHOSPHATE KINASE 1; 1.
DR PANTHER; PTHR14456:SF2; INOSITOL-PENTAKISPHOSPHATE 2-KINASE; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364126};
KW Kinase {ECO:0000256|RuleBase:RU364126};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364126};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
FT REGION 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 67103 MW; 66E9D5450933CBB1 CRC64;
MGKINASHSN YCYDSVLMRS DDKYLRSCSK VDPIDEPYDD DDDDDEDEDD ERPNETLKVP
DRIKWRAEKL DNVRSIASGS SDDEQETRTI RHDILERIDE NRLVYRAEGN ANIVLSVSDN
KHVLRMRKSN VENREGKGDT NVDLRRFVKY SEVIASQFSA CYVPAPKLAH LNTYNLQMFN
ERLRCFRPAM RLGKEIRALD GILYPDVAFL PKWLYPARVR DFSQDPKISS TPPTHYQTYC
VEIKPKQGWL AYEFCDNIPL PELTNGGDLR KCRYCLHQYL KLQKKSIAKI SKYCPLDLYS
GKPVRVLQAV KGLIGAPQNN FKILKNGKVV YDDKREKSMF NRILREMFPR DGRTKDERST
IFINLIKEIL LKDFTTNDEH CDRKLLNIKK ERKKKDKNQL HERACSSANQ QFLPKSCALR
QILDVQLLVK SSISTIDPSL LAKSRTDPYR YIDDMYEKFI NYKEDAVYDV RNSTTWPKEP
FSTEYLSEEE KYQLGATALD CSIMITFRRL YGDRAEENSL NETARNHIVS IEGMKFLVNV
TITDLDPKSH KHYAKYVEQL AASAVAYREF TSKLRR
//
