PI42A_CHICK
ID PI42A_CHICK Reviewed; 405 AA.
AC Q5F356;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha {ECO:0000305};
DE EC=2.7.1.149 {ECO:0000250|UniProtKB:P48426};
DE AltName: Full=1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha;
DE AltName: Full=Diphosphoinositide kinase 2-alpha;
DE AltName: Full=Phosphatidylinositol 5-phosphate 4-kinase type II alpha;
DE Short=PI(5)P 4-kinase type II alpha;
DE Short=PIP4KII-alpha;
DE AltName: Full=PtdIns(5)P-4-kinase isoform 2-alpha;
GN Name=PIP4K2A; Synonyms=PIP5K2A; ORFNames=RCJMB04_33l24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-
CC phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring,
CC to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both
CC ATP- and GTP-dependent kinase activities.
CC {ECO:0000250|UniProtKB:P48426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423,
CC ChEBI:CHEBI:84968, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:83423, ChEBI:CHEBI:84968;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965;
CC Evidence={ECO:0000250|UniProtKB:P48426};
CC -!- ACTIVITY REGULATION: In rod outer segments, activated by light.
CC {ECO:0000250|UniProtKB:Q9R0I8}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P48426}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O70172}.
CC Nucleus {ECO:0000250|UniProtKB:P48426}. Lysosome
CC {ECO:0000250|UniProtKB:O70172}. Cytoplasm
CC {ECO:0000250|UniProtKB:P48426}.
CC -!- PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light
CC and increases kinase activity. {ECO:0000250|UniProtKB:Q9R0I8}.
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DR EMBL; AJ851794; CAH65428.1; -; mRNA.
DR RefSeq; NP_001026142.1; NM_001030971.1.
DR AlphaFoldDB; Q5F356; -.
DR SMR; Q5F356; -.
DR STRING; 9031.ENSGALP00000042061; -.
DR PaxDb; Q5F356; -.
DR GeneID; 420504; -.
DR KEGG; gga:420504; -.
DR CTD; 5305; -.
DR VEuPathDB; HostDB:geneid_420504; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_7_0_1; -.
DR InParanoid; Q5F356; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; Q5F356; -.
DR PRO; PR:Q5F356; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0016309; F:1-phosphatidylinositol-5-phosphate 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:1902635; P:1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0090119; P:vesicle-mediated cholesterol transport; ISS:UniProtKB.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Lysosome;
KW Membrane; Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="Phosphatidylinositol 5-phosphate 4-kinase type-2
FT alpha"
FT /id="PRO_0000185469"
FT DOMAIN 32..404
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 287..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 46092 MW; 14331C226B3C6DB2 CRC64;
MAAPGTVASV MASKTKTKKK HFVVQKVKLF RASDPLLSVL MWGVNHSINE LSHVQIPVML
MPDDFKAYSK IKVDNHLFNK ENMPSHFKFK EYCPMVFRNL RERFGIDDQD FQNSLTRSAP
LANDSQARSG ARFHTSYDKR YIIKTITSED VAEMHNILKK YHQFIVECHG NTLLPQFLGM
YRLTVDGVEI YMIVTRNVFS HRLSVYRKYD LKGSTVAREA SDKEKAKELP TFKDNDFIND
GQKIHIDENN KRMFLEKLKK DVEFLAQLKL MDYSLLVGIH DVERAEQEEV ECEENDGEDE
GESDGTHPIG TPPDSPGNTL NSSLPLAPGE FDPAIDVYGI KSHESAPRKE VYFMAIIDIL
THYDAKKKAA HAAKTVKHGA GAEISTVNPE QYSKRFLDFI ANILT
