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Database: UniProt
Entry: A0A0B2VLM0_TOXCA
LinkDB: A0A0B2VLM0_TOXCA
Original site: A0A0B2VLM0_TOXCA 
ID   A0A0B2VLM0_TOXCA        Unreviewed;       446 AA.
AC   A0A0B2VLM0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN   Name=PI4K2B {ECO:0000313|EMBL:KHN81930.1};
GN   ORFNames=Tcan_04866 {ECO:0000313|EMBL:KHN81930.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN81930.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN81930.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN81930.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN81930.1}.
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DR   EMBL; JPKZ01001440; KHN81930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VLM0; -.
DR   STRING; 6265.A0A0B2VLM0; -.
DR   OMA; GSTAEMN; -.
DR   Proteomes; UP000031036; 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   Gene3D; 1.10.1070.20; -; 1.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF5; 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:KHN81930.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Transferase {ECO:0000256|RuleBase:RU367084}.
FT   DOMAIN          125..424
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  51375 MW;  A56A573470BB4248 CRC64;
     MEEEAENENS RKRGGIDGDQ NERMGDKSGI KVITKSLQTE FDDKGAESAQ QQTSCSSRTG
     RDSNAESEDI KSWSSSLPST SRQSDTSWAR RIHEYVASTK LGTTNVEDED FNENLRRCAD
     AMNAGVRPLR IPSGSSGSYF IRDVNEETIA VFKPKNEEPF APLNPKWPKF FQRILCFCCF
     GRACLIPNNG YLSETGASLV DEKLELHIVP KTRVVKLASP AFFYSRTCWK TKVPKLKAGS
     YQLFVHGYVS ANSIVPEWSK EGRPCPLTHK EAERFKMLFQ KMCVLDYVIR NTDRHMDNWL
     IKYEKNKVME IAAIDNGLAF PVKHPETTSR LRPFPFGWAH LSWAKMSWDE DLRAHLLRLL
     TPQFVQELCD DIKTLFKYDT EVNRFLKYNQ LRVMRGQLWN LRMALLAREP PAEMVKRPLL
     LVSRKYHRRP PTNDWNKSFN VKLADA
//
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