UniProt: E0VSG9

Database: UniProt
Entry: E0VSG9_PEDHC

LinkDB:  E0VSG9_PEDHC 
Original site:  E0VSG9_PEDHC

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (4)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (1)   
All databases (15)   

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ID   E0VSG9_PEDHC            Unreviewed;       464 AA.
AC   E0VSG9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN   Name=8234442 {ECO:0000313|EnsemblMetazoa:PHUM418320-PA};
GN   ORFNames=Phum_PHUM418320 {ECO:0000313|EMBL:EEB16325.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB16325.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB16325.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB16325.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB16325.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM418320-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM418320-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000256|RuleBase:RU367084};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367084};
CC       Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00008941,
CC       ECO:0000256|RuleBase:RU367084}.
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DR   EMBL; AAZO01005129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235751; EEB16325.1; -; Genomic_DNA.
DR   RefSeq; XP_002429063.1; XM_002429018.1.
DR   AlphaFoldDB; E0VSG9; -.
DR   STRING; 121224.E0VSG9; -.
DR   EnsemblMetazoa; PHUM418320-RA; PHUM418320-PA; PHUM418320.
DR   GeneID; 8234442; -.
DR   KEGG; phu:Phum_PHUM418320; -.
DR   CTD; 8234442; -.
DR   VEuPathDB; VectorBase:PHUM418320; -.
DR   eggNOG; KOG2381; Eukaryota.
DR   HOGENOM; CLU_032516_1_1_1; -.
DR   InParanoid; E0VSG9; -.
DR   OMA; DPVFTWC; -.
DR   OrthoDB; 1332545at2759; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF1; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2; 1.
DR   PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU367084};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|RuleBase:RU367084, ECO:0000313|EMBL:EEB16325.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Transferase {ECO:0000256|RuleBase:RU367084}.
FT   DOMAIN          127..464
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   464 AA;  52440 MW;  12D9BEE8AB61022D CRC64;
     MTVEKPNIKN NNELHKAVSA GSLSLCSVGS DAVDLLPDVG FNIVGSSNEG TIDSTGTNRE
     NEPLLSRDDI QPLNHISVFS RGIFTLPVVT IVDGSLLNEI NIKNPIYSDD PQFAKLIQDT
     ETAIENGIFP ERISQGSSGS YFCKNPEGRI IGVFKPKNEE PYGHLNPKWT KWMHKLCCPC
     CFGRSCLIPN QGYLSEAGAY LVDSRFQLNV VPKTKIVKLV SETFHYSRLD RQKSKTKTAI
     SNQFPKVGRR FHRLGLKPKV GSFQTFVDGY KDAEYWLKRF ESEPPPPVVQ TEFQIQFERL
     VALDYIIRNT DRGNDNWLIK YCSGDGKPSI NANGSEMTEV TEWPGNESPK IKIAAIDNGL
     AFPFKHPDSW RAYPYYWAWL PQAKIPFSSD IRQHLLPLVS DQSFIDDVVD DLKVLFEMDK
     GFDSHLFERQ MSVMRGQILN LKQALMDGKS PVQLVQMHSV TLER
//

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