PI4KA_BOVIN
ID PI4KA_BOVIN Reviewed; 2102 AA.
AC O02811; F1MLV0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphatidylinositol 4-kinase alpha;
DE Short=PI4-kinase alpha;
DE Short=PI4K-alpha;
DE Short=PtdIns-4-kinase alpha;
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:P42356};
GN Name=PI4KA; Synonyms=PIK4CA;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-2102, AND ACTIVITY REGULATION.
RC TISSUE=Brain;
RX PubMed=9218477; DOI=10.1074/jbc.272.29.18358;
RA Balla T., Downing G.J., Jaffe H., Kim S., Zolyomi A., Catt K.J.;
RT "Isolation and molecular cloning of wortmannin-sensitive bovine type III
RT phosphatidylinositol 4-kinases.";
RL J. Biol. Chem. 272:18358-18366(1997).
RN [3]
RP GENE STRUCTURE.
RX PubMed=23229899; DOI=10.1083/jcb.201206095;
RA Nakatsu F., Baskin J.M., Chung J., Tanner L.B., Shui G., Lee S.Y.,
RA Pirruccello M., Hao M., Ingolia N.T., Wenk M.R., De Camilli P.;
RT "PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its impact
RT on plasma membrane identity.";
RL J. Cell Biol. 199:1003-1016(2012).
CC -!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed
CC step in the production of the second messenger inositol-1,4,5,-
CC trisphosphate. {ECO:0000250|UniProtKB:P42356}.
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:0000250|UniProtKB:P42356};
CC -!- ACTIVITY REGULATION: Activated by Triton X-100, insensitive to
CC inhibition by adenosine and inhibited by wortmannin. The PI4K complex
CC acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P)
CC synthesis (By similarity). Interaction with TMEM150A regulates
CC PtdIns(4)P synthesis (By similarity). {ECO:0000250|UniProtKB:P42356,
CC ECO:0000269|PubMed:9218477}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC FAM126 (FAM126A or FAM126B). Interacts with TMEM150A; regulating
CC recruitment to the plasma membrane. Interacts with TTC7A.
CC {ECO:0000250|UniProtKB:P42356}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42356}. Cell
CC membrane {ECO:0000250|UniProtKB:P42356}. Note=Localization to the
CC plasma membrane is mediated by the PI4K complex and association with
CC EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or
CC FAM126B). Localization to the plasma membrane is regulated by TMEM150A.
CC {ECO:0000250|UniProtKB:P42356}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; U88532; AAC48730.1; -; mRNA.
DR EMBL; DAAA02045733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_777002.1; NM_174577.2.
DR AlphaFoldDB; O02811; -.
DR SMR; O02811; -.
DR STRING; 9913.ENSBTAP00000018572; -.
DR ChEMBL; CHEMBL3185; -.
DR PaxDb; O02811; -.
DR PRIDE; O02811; -.
DR GeneID; 282309; -.
DR KEGG; bta:282309; -.
DR CTD; 5297; -.
DR eggNOG; KOG0902; Eukaryota.
DR InParanoid; O02811; -.
DR OMA; QEYRYSE; -.
DR OrthoDB; 1147978at2759; -.
DR TreeFam; TF102041; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 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.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2102
FT /note="Phosphatidylinositol 4-kinase alpha"
FT /id="PRO_0000226047"
FT DOMAIN 1530..1718
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1808..2086
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1820
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1954..1962
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1973..1997
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q3L2"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 1154
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42356"
FT CONFLICT 49..50
FT /note="SL -> CV (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="F -> L (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="I -> L (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="F -> L (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="Y -> H (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 478..479
FT /note="HL -> QV (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="V -> E (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="K -> E (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="F -> L (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 967..968
FT /note="HA -> T (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="A -> S (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="G -> A (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
FT CONFLICT 1628
FT /note="Y -> S (in Ref. 2; AAC48730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2102 AA; 235149 MW; F9A5F0E9B7FD2F2E CRC64;
MAAAAARGGG GGGGGGSFGS GAGGGASRGF YFNTVLSLAR SLAVQRPASL EKVQKLLCMC
PVDFHGIFQL DERRRDAVIA LGIFLIESDL QHKDSVVPYL LRLLKGLPKV YWVEESTARK
GRGTLPVAES FSFCLVTLLS DVAYRDPSLR GEILEALLQV LHVLLGMCQA LEIQEKEYLC
KHAVPCLLGI VRAFGRHSSS EDSILSRLFP RAPAHSPRVP EELEGVRRRS FNDFRSILPS
SLLTVCQEGS LKRKASSASS VAQVSPERGA PPPSPPGGSA FHCLEASYSP NGSTSESDYY
FSAVSSSFSV SPLFNGVTYK EFSIPLEMLR ELLNLVKKIV EEPVLKSLDA VVTGVIEASP
SADLCYGAFS DPLYVAVLRM LRDTLYYMRD LPTSFVKEVH DFVLEQFNSS QGELQKILHD
ADRAHSELSP LKLRCQASAA CVDLMVWAVK DEQGAENLCV KLSEKLQSKT SSKVIIAHLP
LLICCLQGLG RLCERFPVVV HSVTPSLRDF LVVPSPVLVK LYKCHSQYHT VAGNDIKISV
TNEHAESTLN VASGKKSQPS MYEQLRDIAI DNVCRCLKAG LTVDPVIVEA FLASLSNRLY
ISQESDKDAH LIPDHTIRAL GHIAVALRDT PKVMEPILQI LQQKFCQPPS PLDVLIIDQL
GCLVITGNQY IYQEVWNLFQ QISVKASSVV YSATKDYKDH GYRHCSLAVI NALANIAANI
QDEHLVDELL MNLLELFVQL GLEGKRASER ASEKGPALKA SSSAGNLGVL IPVIAVLTRR
LPPIKEPKPR LQKLFRDFWL YSVLMGFAVE GSGLWPEEWY EGVCEIATKS PLLTFPSKEP
LRSVLQYNSA MKNDTVTPAE LSELRSTIVN LLDPAPEVSA LIGKLDFAMS TYLLSVYRLE
YMRVLRSSDP ARFQVMFCYF EDKAIQKDKS GMMQCVIAVA DKVFDAFLNM MAEKAKTKEN
EEELERHAQF LLVSFNHVHK RIRRVADKYL SGLVDKFPHL LWSGTVLKTM LDILQTLSLS
LSADIHKDQP YYDIPDVPYR ITVPDTYEAR ESIVKDFAAR CGMILQEAMK WAPTVTKSHL
QEYLSKHQNW VSGLSQHTGL AMATESVLHY AGYNKQSTSL GATQLTERPA CVKKDYSNFM
ASLNLRNRYA GEVYGMIRFS DATGHTSDLN KMMVQELKAA LGAGDAQQYT QAMFKLTAML
ISSRDCDPQL LHHLCWGPLQ MFNEHGMETA LACWEWLLAG KNGVEVPFMR EMAGAWQMTV
EQKFGLFSAE MKEADPLAAS EASQPKPCAP EVTPHYIWID FLVQRFEIAK YCSSDQVEIF
CSLLQRSLSL SIGGTAGSMN RHVAAIGPRF KLLTLGLSLL HADVLPNATI RNVLREKIYS
TAFDYFSCPP RFPTQGEKRL REDISVMIKF WTAMFSDKKY LTASQLVPPD NQDTRSNLDI
AVGSRQQATQ GWINTYPLSS GMSTISKKSG MSKKTNRGSQ LHKYYMKRRT LLLSLLATEI
ERLITWYNPL SAPELELDQA GESSVANWRS KYISLSEKQW KDNVNLAWSI SPHLAVQLPA
RFKNTEAIGN EVTRLVRLDP GAVSDVPEAI KFLVTWHTID ADAPELSHVL CWAPADPPTG
LSYFSSMYPP HPLTAQYGVK VLRSFPPDAI LFYIPQIVQA LRYDKMGYVR EYILWAASQS
QLLAHQFIWN MKTNIYVDEE GHQKDPDIGD LLEQLVEEIT GSLSGPAKDF YQREFDFFNK
ITNVSAIIKP YPKGDERKKA CLSALSEVKV QPGCYLPSNP EAIVLDIDYK SGTPMQSAAK
APYLAKFKVK RCGVSELEKE GLRCRSDPEE EGSMQEADGQ KISWQAAIFK VGDDCRQDML
ALQIIDLFKN IFQLVGLDLF VFPYRVVATA PGCGVIECIP DCTSRDQLGR QTDFGMYDYF
TRQYGDESTL AFQQARYNFI RSMAAYSLLL FLLQIKDRHN GNIMLDKKGH LIHIDFGFMF
ESSPGGNLGW EPDIKLTDEM VMIMGGKMEA TPFKWFMEMC VRGYLAVRPY MDAVVSLVTL
MLDTGLPCFR GQTIKLLKHR FSPNMTEREA ANFILKVIQN CFLSNRSRTY DMIQYYQNDI
PY
