PI5L1_BOVIN
ID PI5L1_BOVIN Reviewed; 396 AA.
AC Q17QS4; Q58DG8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase-like protein 1;
DE Short=PI(4)P 5-kinase-like protein 1;
DE Short=PtdIns(4)P-5-kinase-like protein 1;
DE EC=2.7.1.68;
GN Name=PIP5KL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a scaffold to localize and regulate type I PI(4)P
CC 5-kinases to specific compartments within the cell, where they generate
CC PI(4,5)P2 for actin nucleation, signaling and scaffold protein
CC recruitment and conversion to PI(3,4,5)P3. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC -!- SUBUNIT: Heterodimerizes with other type I phosphatidylinositol 4-
CC phosphate 5-kinase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Localized to large
CC cytoplasmic vesicular structures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q17QS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q17QS4-2; Sequence=VSP_024902, VSP_024903;
CC -!- CAUTION: It is unsure if the enzyme has intrinsic kinase activity.
CC {ECO:0000305}.
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DR EMBL; BT021629; AAX46476.1; -; mRNA.
DR EMBL; BC118210; AAI18211.1; -; mRNA.
DR RefSeq; NP_001069315.2; NM_001075847.2. [Q17QS4-1]
DR AlphaFoldDB; Q17QS4; -.
DR SMR; Q17QS4; -.
DR STRING; 9913.ENSBTAP00000040826; -.
DR PaxDb; Q17QS4; -.
DR Ensembl; ENSBTAT00000076319; ENSBTAP00000066069; ENSBTAG00000003387. [Q17QS4-1]
DR GeneID; 523736; -.
DR KEGG; bta:523736; -.
DR CTD; 138429; -.
DR VEuPathDB; HostDB:ENSBTAG00000003387; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000158633; -.
DR InParanoid; Q17QS4; -.
DR OMA; PRHELHG; -.
DR OrthoDB; 1562683at2759; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003387; Expressed in esophagus and 33 other tissues.
DR ExpressionAtlas; Q17QS4; baseline.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; 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; 2.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Lipid metabolism;
KW Membrane; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Phosphatidylinositol 4-phosphate 5-kinase-like
FT protein 1"
FT /id="PRO_0000285757"
FT DOMAIN 38..395
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_024902"
FT VAR_SEQ 225..257
FT /note="CEVSRWVEPAPEGSVLVLVLKDLNFQGKTINLG -> MSPALPGQVRVEPAA
FT PCPAPDEHSGWGTDAPAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_024903"
SQ SEQUENCE 396 AA; 44778 MW; 218E24E583B1EF78 CRC64;
MAAPSPGPRE ILAPSPEAGR RAAASSSGHR GLLWRLRDKQ CRLGLFEIGP GHELHQVMCL
MQAGLWAATQ VSMDHPPTGL PTEEDFSEVL TQVHEGFELG TLAGPVFARL RRSLGLAEED
YQAALGPSRP YLQFLSTSKS KASFFLSHDQ RFFLKTLRSR EVQALLAHLP RYVHHLQRHP
HSLLARVLGV HSLRVARGKK KYFIVMQSVF YPAGRISERY DIKGCEVSRW VEPAPEGSVL
VLVLKDLNFQ GKTINLGPQR SWFLRQMELD TAFLRELNVL DYSLLMAFQR LHEDERGPGS
SLIFRTARSI RGAQSAEESG AQNRRLLPDA PNALHIVDGP EHRYFLGLVD LTTVYGLRKR
LEQLWKTLRY PGRTFSTVSP ACYARRLCQW VEAHTE
