PYK3_DICDI
ID PYK3_DICDI Reviewed; 1338 AA.
AC Q54I36; Q23846; Q23927;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dual specificity protein kinase pyk3;
DE EC=2.7.12.1;
DE AltName: Full=Tyrosine-protein kinase 3;
GN Name=pyk3; Synonyms=DpyK3, pkyA; ORFNames=DDB_G0289001;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND AUTOPHOSPHORYLATION.
RC STRAIN=AX2;
RX PubMed=8898113; DOI=10.1016/0014-5793(96)01053-8;
RA Adler K., Gerisch G., von Hugo U., Lupas A., Schweiger A.;
RT "Classification of tyrosine kinases from Dictyostelium discoideum with two
RT distinct, complete or incomplete catalytic domains.";
RL FEBS Lett. 395:286-292(1996).
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., 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 [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18657170; DOI=10.1111/j.1440-169x.2008.01058.x;
RA Lee N.-S., Rodriguez M., Kim B., Kim L.;
RT "Dictyostelium kinase DPYK3 negatively regulates STATc signaling in cell
RT fate decision.";
RL Dev. Growth Differ. 50:607-613(2008).
CC -!- FUNCTION: Involved in the development. Negatively regulates tyrosine
CC phosphorylation and activation state of dstC/STATc, probably by
CC activating a dstC/STATc phosphatase. {ECO:0000269|PubMed:18657170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- DEVELOPMENTAL STAGE: Expression is initially low during the vegetative
CC stage, but increases after 5 and 15 hours of development. Up-regulation
CC of the expression at the postaggregative stages is observed.
CC {ECO:0000269|PubMed:18657170}.
CC -!- DOMAIN: The truncated N-terminal protein kinase domain lacks most of
CC its classical characteristics and in vitro, has no activity.
CC -!- DOMAIN: The protein kinase domain 1 is predicted to be catalytically
CC inactive.
CC -!- PTM: C-terminal tyrosine kinase domain is capable of
CC autophosphorylation, in vitro.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; U01064; AAB04169.1; -; mRNA.
DR EMBL; U64830; AAB04999.1; -; Genomic_DNA.
DR EMBL; AAFI02000129; EAL62916.1; -; Genomic_DNA.
DR PIR; T18287; T18287.
DR RefSeq; XP_636435.1; XM_631343.1.
DR AlphaFoldDB; Q54I36; -.
DR SMR; Q54I36; -.
DR STRING; 44689.DDB0191218; -.
DR PaxDb; Q54I36; -.
DR EnsemblProtists; EAL62916; EAL62916; DDB_G0289001.
DR GeneID; 8626928; -.
DR KEGG; ddi:DDB_G0289001; -.
DR dictyBase; DDB_G0289001; pyk3.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_258584_0_0_1; -.
DR InParanoid; Q54I36; -.
DR OMA; PPCIFTE; -.
DR PRO; PR:Q54I36; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IGI:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:dictyBase.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1338
FT /note="Dual specificity protein kinase pyk3"
FT /id="PRO_0000354056"
FT DOMAIN 693..1014
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1057..1309
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 699..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 727
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1063..1071
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1084
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 917..920
FT /note="APEM -> GTET (in Ref. 1; AAB04169)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="I -> F (in Ref. 1; AAB04169/AAB04999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="E -> G (in Ref. 1; AAB04999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="W -> R (in Ref. 1; AAB04169)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="K -> R (in Ref. 1; AAB04999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="F -> S (in Ref. 1; AAB04999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1119
FT /note="C -> R (in Ref. 1; AAB04169/AAB04999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1338 AA; 149944 MW; 029B57F88678BE48 CRC64;
MDSFNNNNNN NNNNNNNNNN INGEGITLRT LLNSCTNTSS NEQLIVNNVN KNSNIINNIN
INNTPSPIST CINVNKIELR GSSNGIFLNS KIKVPLPNST LLEQQQDGAD EQDKKQQSLS
DKNILFSSGD KEFLNHGSNN IITDQNTLLY QLQQQQQKEK EKENDEIMNH DDIIGYNEEN
EDNFFNEGMD PILAHSIEHH LHNHHHHHGE FDTQENEDTS GESSDESENI DEVLVYTEDI
ESEKEKKRER LITSPPSFDP HTLYSMSQSL LNCSLNNNNN NNNSISSPSS SINNSGNNIN
LNNSGNNNVN SNNNTNIINN SNDNFISQPL FNPLSMPNNE QYELLPNPTT TTSTITSTTT
TTTITNLPPA LPSFPSSSSI KSLKNSFGSN SITSSGELNN VFSSSMSPPM SPPNRNVRSL
TFPGTNPINC INTSVINSIT ANTNCINHHH HHHQHNHHNH HQGHNNINNS GHIRKSADDT
VTLSPTLSSG SSSTSSSNPH HPNHNHQKGL NNKTLEKLSC TRKEIYELIE KKESLIEKQN
LIDEGYSENA DSFENLSEEI QKINEKIIEL ENLITSLSNS NSNWSLNGSS TSTISCNPLS
PRSMNPSSST SSTSSNLTNS LRKFSQELKI ELRPLDLRAE LYSSINTSPR GSASISGGSG
SGGGGNNNGC FKTSSNSSIN SPIQFFENEN ESIDSYEKKN EEQFESLTQL IRENQLYTKP
IEFKEIKLLE KLESNSKSSN IWQIEYKSTQ LVLKQPKDQD SDKNIEKRKQ LFNGSNVSGS
NNSGSSGGNN HNHHHCNNSN GSNSEVIPSK YTMIQHKNLG LLVGWCGDSI IFESFKGMNS
LHDLIHRDGL KIDMALFIKI SKDIASVMGL LHSKDVAHGN LTSRSIYLDR FQIVKVSFPK
LNATDLNNPA IEPRYMAPEM TRMEEDQISC SIDVYAYAFV LWEALTSHLP FRKFNDISVA
AKVAYENLRP KIPTSCPLII RKLINRCWAP LPSDRPTFND ILKLFDHLEG KLFFSSPGIL
WSLNNDQEVE RELQKKERFN EITEFLRGKK EIKFDEVAIV EKVGAGSFAN VFLGIWNGYK
VAIKILKNES ISNDEKFIKE VSSLIKSHHP NVVTFMGACI DPPCIFTEYL QGGSLYDVLH
IQKIKLNPLM MYKMIHDLSL GMEHLHSIQM LHRDLTSKNI LLDEFKNIKI ADFGLATTLS
DDMTLSGITN PRWRSPELTK GLVYNEKVDV YSFGLVVYEI YTGKIPFEGL DGTASAAKAA
FENYRPAIPP DCPVSLRKLI TKCWASDPSQ RPSFTEILTE LETMKSKFIK QLSFLNDLIQ
NPDDDYNNNL NYDEEVDS
