ID W6UBP4_ECHGR Unreviewed; 997 AA.
AC W6UBP4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
GN ORFNames=EGR_06619 {ECO:0000313|EMBL:EUB58530.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB58530.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB58530.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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|ARBA:ARBA00036767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000256|ARBA:ARBA00036767};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004308}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037860}.
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:EUB58530.1}.
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DR EMBL; APAU02000060; EUB58530.1; -; Genomic_DNA.
DR AlphaFoldDB; W6UBP4; -.
DR STRING; 6210.W6UBP4; -.
DR EnsemblMetazoa; XM_024495868.1; XP_024349726.1; GeneID_36342334.
DR OMA; DEQITRC; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EUB58530.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 711..982
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 336..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 110419 MW; 0D175ECA71BBD793 CRC64;
MQADMRRVGL GAPGALFVRS AAFPFYELDS RHISSWGLHA FFAAFTFLFA LNWCIANCLL
VIAIFAIFVI GCALVLFTSV IYYFFCHHHH FSFEAAEMDE QNTEVHLPKL PLSPSMIGRA
CPGQAALANS TSNTNSLILS SSPPFSSLMR FINSSVFSVH HAVHYLNEGS ASKDWDYLAK
RLFEYRTEDV DFYLPQLVVL FLQCDGPTRS LLPYLFQRVK TSLRFATEMA WLVDAHNISS
HSTPNSPFKP LKSYPIDFIP AVTTTTSSST IEVAKEVEEE SGSSGSLNGS LNCLEMEDNE
PSIVKQTQTS TAVEKGDQLM KHKRAASDLT CLANGSEAQS RDQAEASNDS CGTAFGSEAG
NHADVDDDLE SPEAFDGSKP TRSEAWIEMH SRFYDPAASR SDTHLHLRRP RLLRATTFTP
ASFSTDLLGL PEGQNQQPGR LQDALTDFLD AGSATAAMTV GGTSKQSLRS DKLIGLCQGE
WDFMNALLSI SHRLAPFASK EQRTSHLQAE LGKLNFGLPA RVWLPVEATE HIVLRIPPSA
AVCLNSAEKV PYLVYMEILV CNDVMTTRLP QRPGTATGFT HCNNPSCHSY DINSPQLTPA
SSKTCLTSAR AFAAPDVISL FSTDSGESLG ACVSSMTATP AVVAAGASNE DPTTTTSTSR
SKHQQRDKNE PTVCYVNAKD IRRRLEQNAA CQPQRTFKLD PEDPSAAVLK EPWELKARRI
QEASPWGHLP GWQLAAVIVK VGDDLRQEQL AYQLLSYLKK IWADYHLNLW LRPLNIVITS
PDSGLVEVVK DTVSFHQIRR HARLSLRDYI IREHGQPNSE GFLSAQRNFV QSCAAYCLVG
YLLQVKDRHN GNILIDKEGH VVHIDYGFML SASPGRNICF ESSPFKLTAE QVELMGGVGG
DMFNYYKSLI VQGLLAARKH MDELLLLVKI THNGYPHLPC FVSRGGARTL EALRQRFMLG
STDEQITRCV EYLICQSLNS LTTRLYDNYQ YYANGIQ
//
