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Database: UniProt
Entry: P54675
LinkDB: P54675
Original site: P54675 
ID   PI3K3_DICDI             Reviewed;        1697 AA.
AC   P54675; Q553Z1; Q869X9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   29-OCT-2014, entry version 98.
DE   RecName: Full=Phosphatidylinositol 3-kinase 3;
DE            Short=PI3-kinase;
DE            Short=PI3K;
DE            Short=PtdIns-3-kinase;
DE            EC=2.7.1.137;
GN   Name=pikC; Synonyms=pik3; ORFNames=DDB_G0275011;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-1697.
RC   STRAIN=AX3;
RX   PubMed=7565716;
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
RT   Vps34p PI 3-kinase homologs during growth and development.";
RL   Mol. Cell. Biol. 15:5645-5656(1995).
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC       1-phosphatidyl-1D-myo-inositol 3-phosphate.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00879, ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
CC   -!- SIMILARITY: Contains 1 C2 PI3K-type domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
CC   -!- SIMILARITY: Contains 1 PI3K-RBD domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00879}.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00269}.
CC   -!- SIMILARITY: Contains 1 PIK helical domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00878}.
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DR   EMBL; AAFI02000013; EAL69786.1; -; Genomic_DNA.
DR   EMBL; U23478; AAA85723.1; -; mRNA.
DR   PIR; T18274; T18274.
DR   RefSeq; XP_643820.1; XM_638728.1.
DR   ProteinModelPortal; P54675; -.
DR   STRING; 44689.DDB_0185203; -.
DR   EnsemblProtists; DDB0185203; DDB0185203; DDB_G0275011.
DR   GeneID; 8619867; -.
DR   KEGG; ddi:DDB_G0275011; -.
DR   dictyBase; DDB_G0275011; pikC.
DR   eggNOG; COG5032; -.
DR   InParanoid; P54675; -.
DR   KO; K00922; -.
DR   OMA; LIHESIG; -.
DR   PhylomeDB; P54675; -.
DR   BRENDA; 2.7.1.137; 1939.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:RefGenome.
DR   GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:dictyBase.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:RefGenome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006928; P:cellular component movement; IGI:dictyBase.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; TAS:GOC.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K_C2_dom.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR001263; PInositide-3_kin_accessory_dom.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF54236; SSF54236; 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; PS51547; PI3K_C2; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN         1   1697       Phosphatidylinositol 3-kinase 3.
FT                                /FTId=PRO_0000088824.
FT   DOMAIN      737    823       PI3K-RBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00879}.
FT   DOMAIN      888   1036       C2 PI3K-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00880}.
FT   DOMAIN     1060   1238       PIK helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00878}.
FT   DOMAIN     1333   1596       PI3K/PI4K. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00269}.
FT   REPEAT     1622   1626       1.
FT   REPEAT     1627   1631       2.
FT   REPEAT     1632   1636       3.
FT   REPEAT     1642   1646       4.
FT   REPEAT     1647   1651       5.
FT   REGION     1622   1651       5 X 5 AA approximate repeats.
FT   REGION     1659   1672       7 X 2 AA tandem repeats of K-E.
FT   COMPBIAS    170    196       Poly-Asn.
FT   COMPBIAS    210    222       Poly-Asn.
FT   COMPBIAS    312    338       Poly-Asn.
FT   COMPBIAS    351    366       Poly-Asn.
FT   COMPBIAS    457    490       Poly-Asn.
FT   COMPBIAS    495    502       Poly-Asn.
FT   COMPBIAS    596    600       Poly-Ser.
FT   COMPBIAS    832    849       Poly-Gln.
FT   COMPBIAS   1681   1687       Poly-Asn.
FT   CONFLICT   1159   1159       A -> T (in Ref. 3; AAA85723).
FT                                {ECO:0000305}.
FT   CONFLICT   1175   1175       M -> L (in Ref. 3; AAA85723).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1697 AA;  192942 MW;  C5442DC2C3202E32 CRC64;
     MRQIVTGVIH QTTQSQQIPN VINSNQIQFS NEPMVVGSIE DFDIDSEVPP LAINLQRSIN
     NNNNNNNNNN NNNNNNNNNN NNNNNNNTQP CTTVFLDRDS CVNVKATIDL LKEQLEFTIK
     DLIDFKENYD KLESTEQFKQ WSNLIKNIKE NSLNNSNIYL TIPTTQNLIN NNNNNNNNNN
     NNNNNNNNNN NNNNNNVIIP SASTENKEEN DNNNSNNNNN INLSPDSSIT KDINITENKI
     TEIKTTETKE TSTGTSPLEK SPSKGFIISP KKPEEENEIE GETINNIAIT NYTQGPSMLT
     LMKKKLENIK KNNNNNNNNG NGNNNSNNNN SNSNNNNNGI SPSSSPPSHL NGNNNNNNSN
     NTNSNNTTNA TTNSVGFSIT MTNSNSLSVS KRMNKFKSWT SSKPTSSSIG FASSPQNNGK
     PLNISGSSRF FTSRQDSKID LLKSPSSSPP TQSDIFNENN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN EELINNNNNN NNDENYKIEE TEESLKELLE KEKLENEERE KILKERNEID
     NLKKKNHLSK GYFMRACNAS NDDGLEEEDI PLQDEHWETN VIVLLPCRHH VKVPGSSSSS
     IDSIRQLAWA SGKMQGHLNL EKDEKFFTLR WCNKDVVFDQ DTPLGHLIQY NLNYNNPTQK
     PTNIKLELVL EDELCKERLV DLQSLEINNG RPSIWKSHID DVLSFNRKLR ELAMLAKPQS
     NVPAARLTPY PPPKTIPEFF VIRVHLFKNQ TKSLRCANNH TAFSLMTILS EKLKNTTPFD
     PTQYRFLITG INQYVDPNVP LLSVEYIVEK IKRKGEIDLT MVELLSLGLI IQQQQQQQQQ
     QQQQQQQQQI ENIDDENILK LNNGILNVLS KIEKPIREKD NCISSLTVTE NLQVRLLHAH
     EIFASKASEI IGTDSPSIQL FIEAAVYFGG ELLATQSSKL VSFQDTVVWN EWVNIPLAVS
     NIPNGARMCL GLNARYRGDI FNIGWVGHRL FDSKGILNTF APFSLLLWPG KINPIGTCVD
     NLESKDQAII IAFEFKDYVV PKTIHYEDDL IELISKDENG NELPVVTMEE MDRVEQIILQ
     DPLYSLNKEE RLLIWKSRYF CHTKPQALSK LLQSVEWTNY KQVGEAFQLL KIWPTLSAVD
     ALELLDPKFA DCVEIREYAV KCLDQMSDYE LEIYMLQLVQ AIKHDVFHNS VLSLFLIGRV
     WQNMQVLGHP FFWHLRADID NQEVCERFRV LSSGFLRYAP TQLMESFKRE ITTLRILENL
     AKRVKEVPYE KRKQYVENNL REEQSFPTEL FVPFDPSIRI LNIIPEKCKS MDSAKVPLWV
     TFKNADPFAP PLQMIAKTGD DLRQDILTLQ LLRLMDHMWK SQDLDLHMTI YRCIATGMGT
     GLIEVVPNSE TAARIQAGAG GVSGAFKQTP IANWLKNHNQ TENSYQKAVS KFTLSCAGYC
     VATYVLGIGD RHNDNIMVDI HGHLFHIDFG HFLGNFKTFA GFQREKAPFV LTPDFVYVIG
     GKDSPNFAFF VDICCKAFNI IRSNAHVFIN MFELMLSTGI PELRSENDIV YLRDKFRLDL
     TDAEASEYFK KLIHESIGTL TTTINFAIHI MAHRKNLVSG NSAPKIGSAS SLNLNKNKPS
     SQSKLDLSRS DLSRSDSSRS DSSRLDLSRS DKKNNKDNKE KEKEKEKEKE KENNDNNDKD
     NNNNSNNDTE KENSIDK
//
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