PI4K_DICDI
ID PI4K_DICDI Reviewed; 1180 AA.
AC P54677; Q54IV1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phosphatidylinositol 4-kinase;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
DE AltName: Full=PI4K-alpha;
GN Name=pikD; Synonyms=pik4; ORFNames=DDB_G0288485;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-1180.
RC STRAIN=AX3;
RX PubMed=7565716; DOI=10.1128/mcb.15.10.5645;
RA Zhou K., Takegawa K., Emr S.D., Firtel R.A.;
RT "A phosphatidylinositol (PI) kinase gene family in Dictyostelium
RT discoideum: biological roles of putative mammalian p110 and yeast Vps34p PI
RT 3-kinase homologs during growth and development.";
RL Mol. Cell. Biol. 15:5645-5656(1995).
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.
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;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000112; EAL63191.2; -; Genomic_DNA.
DR EMBL; U23479; AAA85725.1; -; Genomic_DNA.
DR PIR; T18275; T18275.
DR RefSeq; XP_636702.2; XM_631610.2.
DR AlphaFoldDB; P54677; -.
DR SMR; P54677; -.
DR STRING; 44689.DDB0191346; -.
DR PaxDb; P54677; -.
DR PRIDE; P54677; -.
DR EnsemblProtists; EAL63191; EAL63191; DDB_G0288485.
DR GeneID; 8626659; -.
DR KEGG; ddi:DDB_G0288485; -.
DR dictyBase; DDB_G0288485; pikD.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_273161_0_0_1; -.
DR InParanoid; P54677; -.
DR OMA; CEMSVIT; -.
DR PRO; PR:P54677; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1180
FT /note="Phosphatidylinositol 4-kinase"
FT /id="PRO_0000088826"
FT DOMAIN 1..206
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 895..1164
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 15..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..907
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1030..1038
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1049..1073
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 15..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138
FT /note="T -> N (in Ref. 2; AAA85725)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="H -> L (in Ref. 2; AAA85725)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..253
FT /note="ND -> KC (in Ref. 2; AAA85725)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="D -> N (in Ref. 2; AAA85725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1180 AA; 132681 MW; 1AB9290C91445F32 CRC64;
MNKISDTIII TSTSNEDEVD NNNNNNNLKE IDRSPRVNNN NNNILTNVNN NKNNTITSSG
GSDSSSSSSN NNNNKIKKSK KHKEKEHMDS IVKLYSGKFD SWMVICHLFK YRDNPGIVDF
LCNKMYNLED KDIDFYITQL CILLINQPHD QKASFSSLAR FILDRCASSF RFAIKAYWIF
QAFEEDGEKN LFSIEGSVYL HSPSTSPKDV PMYSNDQIVP IDLDKIYNQS QYDDDDFDLS
DDDGGFEIIK KNDHHYENDH HIENDPKKDI NSNNNNNNNI NNNNSNNDDN NNNEILPNEN
SDNSINDENN QYGNSNNNNN ISGENDNIKI DINSQNKSDS NIETLNSTLC EETKTSPIKD
DMENNNNNNN NNNNNNNNNN NNNNINNNNI NNNNINNNNN INYGHINGSL STLDGIGQPY
ISQPNDPIEN ITQILKRNRI IYKKVEEKKE LATRLREFCE MSVITCSRPL ITRPRTSSLP
SPLISYNSGK IGGNYHKILS PSSVDSTSLI SEDDKIIEKE EEDNVVEDDD DDEVNSEDFI
PTATTTATTT TTTIPNHLSK TTSGVGINSN SSTPININSA GAGAGGGGEI NHIGYDDISY
LDKCKTPPAE SKLSDHDFEF ELSKSHRCDY LNDILSFIQK LAHISKILLP IPIDLRQAKL
KHEISLLNIN LPLGLYVPLW QSSNHHCVVR IPPEEVKILN SRERVPFLLV LEVIESEHEA
LSSNIFEVVS SYLQYTTGNS ALKKDDIKRK YYSEKFKKSF LNSSINSTIS NSSDSCTTET
TTTSPVATSP TLPINIPHSK LINDGSNSIS KSLPVTPTQS TVLNNLISTS TAISPPSQQQ
QLPSPSNTTT TTTTTTTNTN NTTTTTTTTT TTLSTSPTNE KILNENKQNS SPFGESWQEK
IERYKKISPF GDYPNWRLYS VIVKTGDDCR QEQMAVQLIS KFDEIWKETR LPLYLRPYSI
LVTSSGGGII ETIPDTMSLH NLKKSTPGFT TLLNYFKSTY GDPSGLRFRT AQSNFIESMA
AYSIVTYILQ IKDRHNGNIL IDKEGHIVHI DFGFILSNSP GNISFESAPF KLTQELVDVM
GGIQSGQFQY FKVLCVRGLI EARKQVDKII SLIEIMMSGP KMSCFVGGKE VIEQLKARFF
LDVNERECST LVENLISYSI DHFKTRYYDK YQSWLNGIYQ
