ID A0A1V4KIM6_PATFA Unreviewed; 504 AA.
AC A0A1V4KIM6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN Name=PI4K2A {ECO:0000313|EMBL:OPJ84330.1};
GN ORFNames=AV530_015777 {ECO:0000313|EMBL:OPJ84330.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ84330.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ84330.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ84330.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ84330.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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|ARBA:ARBA00001686,
CC ECO:0000256|RuleBase:RU367084};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell
CC projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}.
CC Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00037864}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037864}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Membrane
CC {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367084}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome
CC {ECO:0000256|ARBA:ARBA00034102}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
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:OPJ84330.1}.
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DR EMBL; LSYS01003057; OPJ84330.1; -; Genomic_DNA.
DR STRING; 372326.A0A1V4KIM6; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
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:SF7; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-ALPHA; 1.
DR PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367084};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367084};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367084}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 149..478
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 56645 MW; D158E34411A45030 CRC64;
MATPGLGVAG AERPTGRGGA VTRTEVAGTG GAAGPGGRDG RDXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXEFAE VVRRAELASE RGIFPERISQ GSSGSYFVKD PQGAQAAAAA
AAQRERNDFP EDPEFAEVVR RAELASERGI FPERISQGSS GSYFVKDPQG KIIGVFKPKN
EEPYGQLNPK WTKWLQKLCC PCCFGRDCLV LNQGYLSEAG ASLVDQKLEL NIVPRTKVVY
LASETFNYSA IDRVKSRGKR LALEKVPKVG QRFNRIGLPP KVGSFQLFVE GYKDADYWLR
RFEAEPLPEN TNRQLLLQFE RLVVLDYIIR NTDRGNDNWL IKYDCPLDSA GVRDSDWVVV
KEPIIKLAAI DNGLAFPLKH PDSWRAYPFY WAWLPQAKIP FSQEIKDLIL PKISDPNFVK
DLEEDLYELF KKDPGFDRGQ FHKQIAVMRG QILNLTQALK DGKSPLHLVQ MPPVIVETAR
SHQRTTSESY TQSFQSRKPF FSWW
//
