ZAK2_DICDI
ID ZAK2_DICDI Reviewed; 635 AA.
AC Q552C6; Q75JK1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Dual specificity protein kinase zak2;
DE EC=2.7.12.1;
DE AltName: Full=Tyrosine-protein kinase 4;
DE AltName: Full=Zaphod K Kinase 2;
DE Short=Zaphod kinase 2;
GN Name=zak2; Synonyms=DpyK4, pyk4; ORFNames=DDB_G0276187;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AUTOPHOSPHORYLATION.
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21205787; DOI=10.1242/dev.055335;
RA Kim L., Brzostowski J., Majithia A., Lee N.S., McMains V., Kimmel A.R.;
RT "Combinatorial cell-specific regulation of GSK3 directs cell
RT differentiation and polarity in Dictyostelium.";
RL Development 138:421-430(2011).
RN [3]
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., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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).
CC -!- FUNCTION: Positive regulator of gsk3/gskA activity required for cell
CC pattern formation and a downstream effector of carC. The kinases,
CC gsk3/gskA, zakA and zak2, form part of a signaling pathway that
CC responds to extracellular cyclic AMP. The pathway has a role in
CC transcriptional regulation; required to direct prespore/spore fates
CC during development. Zak2 negatively regulates prestalk differentiation
CC by regulating expression of ecmA. Phosphorylates Y-214 of gsk3/gskA, in
CC vitro. {ECO:0000269|PubMed:21205787}.
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 -!- TISSUE SPECIFICITY: ZakA and zak2 are coexpressed in prestalk cell
CC population, zakA is enriched in pstB populations and zak1 in pstA
CC populations. ZakA and zak2 are coexpressed in prespore cells, zakA
CC expression levels are 10 fold higher than zak2.
CC {ECO:0000269|PubMed:21205787}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the growth phase and throughout
CC the major developmental stages. {ECO:0000269|PubMed:21205787}.
CC -!- PTM: C-terminal tyrosine kinase domain is capable of
CC autophosphorylation, in vitro.
CC -!- DISRUPTION PHENOTYPE: Abnormal morphology of the terminal fruiting
CC body; the sorus, or large spore mass atop an elongated stalk of
CC vacuolated cells, does not form and the stalk structure is expanded.
CC {ECO:0000269|PubMed:21205787}.
CC -!- MISCELLANEOUS: 'Zaphod' is a fictional ex-president of the galaxy with
CC 2 heads.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. TKL Tyr protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000014; EAL69393.1; -; Genomic_DNA.
DR RefSeq; XP_643302.1; XM_638210.1.
DR AlphaFoldDB; Q552C6; -.
DR SMR; Q552C6; -.
DR STRING; 44689.DDB0229958; -.
DR PaxDb; Q552C6; -.
DR PRIDE; Q552C6; -.
DR EnsemblProtists; EAL69393; EAL69393; DDB_G0276187.
DR GeneID; 8620348; -.
DR KEGG; ddi:DDB_G0276187; -.
DR dictyBase; DDB_G0276187; zak2.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_431134_0_0_1; -.
DR InParanoid; Q552C6; -.
DR OMA; NMKKFTV; -.
DR PhylomeDB; Q552C6; -.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q552C6; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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:0030154; P:cell differentiation; IMP:dictyBase.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:dictyBase.
DR GO; GO:0010468; P:regulation of gene expression; IDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..635
FT /note="Dual specificity protein kinase zak2"
FT /id="PRO_0000355202"
FT DOMAIN 9..249
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 299..585
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 635 AA; 72979 MW; 96FC2977A4771AF7 CRC64;
MNSHKKEEWE EISSIGSCNS KSRVLKCRKK NGLIENEKVD IVAVKIINKK FFKRNETDIL
EKIRLFNIPR YYSHAEDDNY IYIYMEYIED KKQLRFKESE IISMIADLTE TLSFLHKHQI
LHRDIKPSNI ILDKNGVLKL IDFGSSIIDQ QQDDGDNICK ESSFAITGTH TYMAPEVKKL
HRSTKKSDVW SLGCTVLEIV GGNPKKIFDG IPIIPNHVSE IMVDFIKRCL IIDPNKRSHM
EELLTHRLIS SMVGQNKNRE NNIEPKFNND YLSSKFPERF APRFEKPKWE IEFNELKFNK
DDTVGGDGFF SVVKKGYYNE TEVAIKLIKK AHGENVTVCD TFYHEVLIIS NLRHPNIVQF
IAACIKFDNK EVNHCIVSEW MSGGNLSQFI SNERKILEIN PHLRVKILLD IAKGMLYSHR
QGIIHRDLTS NNVLLNFRKK KLLNNNSSNN DEQFYDSDEI IAKVCDFGLS SNQSESKKLR
GGSIHYMAPE NLNGSPINEK SDIYSFGLLV WQMFSYASPN TIYSPKEMAS MVSDEKLNYR
PQIPFNVPLK FKELITQCWD RNPLNRPKDF SEIIDKLKDI NQIYFQDNSN ASTISSTAIT
TTISTISISN SGNSSYSTSD DSSTYGSGFY NSGFL
