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Dual specificity protein kinase zak2 (EC 2 7 12 1) (Tyrosine-protein kinase 4) (Zaphod K Kinase 2) (Zaphod kinase 2)

 ZAK2_DICDI              Reviewed;         635 AA.
Q552C6; Q75JK1;
25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
20-JUN-2018, entry version 88.
RecName: Full=Dual specificity protein kinase zak2;
EC=2.7.12.1;
AltName: Full=Tyrosine-protein kinase 4;
AltName: Full=Zaphod K Kinase 2;
Short=Zaphod kinase 2;
Name=zak2; Synonyms=DpyK4, pyk4; ORFNames=DDB_G0276187;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND AUTOPHOSPHORYLATION.
PubMed=8898113; DOI=10.1016/0014-5793(96)01053-8;
Adler K., Gerisch G., von Hugo U., Lupas A., Schweiger A.;
"Classification of tyrosine kinases from Dictyostelium discoideum with
two distinct, complete or incomplete catalytic domains.";
FEBS Lett. 395:286-292(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=21205787; DOI=10.1242/dev.055335;
Kim L., Brzostowski J., Majithia A., Lee N.S., McMains V.,
Kimmel A.R.;
"Combinatorial cell-specific regulation of GSK3 directs cell
differentiation and polarity in Dictyostelium.";
Development 138:421-430(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
-!- FUNCTION: Positive regulator of gsk3/gskA activity required for
cell pattern formation and a downstream effector of carC. The
kinases, gsk3/gskA, zakA and zak2, form part of a signaling
pathway that responds to extracellular cyclic AMP. The pathway has
a role in transcriptional regulation; required to direct
prespore/spore fates during development. Zak2 negatively regulates
prestalk differentiation by regulating expression of ecmA.
Phosphorylates Y-214 of gsk3/gskA, in vitro.
{ECO:0000269|PubMed:21205787}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- TISSUE SPECIFICITY: ZakA and zak2 are coexpressed in prestalk cell
population, zakA is enriched in pstB populations and zak1 in pstA
populations. ZakA and zak2 are coexpressed in prespore cells, zakA
expression levels are 10 fold higher than zak2.
{ECO:0000269|PubMed:21205787}.
-!- DEVELOPMENTAL STAGE: Expressed during the growth phase and
throughout the major developmental stages.
{ECO:0000269|PubMed:21205787}.
-!- PTM: C-terminal tyrosine kinase domain is capable of
autophosphorylation, in vitro.
-!- DISRUPTION PHENOTYPE: Abnormal morphology of the terminal fruiting
body; the sorus, or large spore mass atop an elongated stalk of
vacuolated cells, does not form and the stalk structure is
expanded. {ECO:0000269|PubMed:21205787}.
-!- MISCELLANEOUS: 'Zaphod' is a fictional ex-president of the galaxy
with 2 heads.
-!- SIMILARITY: In the N-terminal section; belongs to the protein
kinase superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the protein
kinase superfamily. TKL Tyr protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AAFI02000014; EAL69393.1; -; Genomic_DNA.
RefSeq; XP_643302.1; XM_638210.1.
ProteinModelPortal; Q552C6; -.
STRING; 44689.DDB0229958; -.
PaxDb; Q552C6; -.
EnsemblProtists; EAL69393; EAL69393; DDB_G0276187.
GeneID; 8620348; -.
KEGG; ddi:DDB_G0276187; -.
dictyBase; DDB_G0276187; zak2.
eggNOG; KOG0192; Eukaryota.
eggNOG; KOG0198; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; Q552C6; -.
OMA; TMDYLHS; -.
PhylomeDB; Q552C6; -.
PRO; PR:Q552C6; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IC:dictyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:dictyBase.
GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:dictyBase.
GO; GO:0042659; P:regulation of cell fate specification; IMP:dictyBase.
GO; GO:0010468; P:regulation of gene expression; IDA:dictyBase.
GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR008266; Tyr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00220; S_TKc; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Developmental protein; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1 635 Dual specificity protein kinase zak2.
/FTId=PRO_0000355202.
DOMAIN 9 249 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 299 585 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 305 313 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 589 627 Ser-rich.
ACT_SITE 124 124 Proton acceptor. {ECO:0000250}.
ACT_SITE 427 427 Proton acceptor. {ECO:0000250}.
BINDING 45 45 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 326 326 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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


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