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Dual specificity protein kinase zakA (EC 2 7 12 1) (Zaphod K Kinase 1) (Zaphod kinase 1) (Zaphod kinase A)

 ZAK1_DICDI              Reviewed;         781 AA.
Q75JK0; Q552C7; Q9U478;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-FEB-2018, entry version 93.
RecName: Full=Dual specificity protein kinase zakA;
EC=2.7.12.1;
AltName: Full=Zaphod K Kinase 1;
Short=Zaphod kinase 1;
AltName: Full=Zaphod kinase A;
Name=zakA; Synonyms=zak1; ORFNames=DDB_G0276025;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-759, FUNCTION, DEVELOPMENTAL STAGE,
AND AUTOPHOSPHORYLATION.
PubMed=10571182; DOI=10.1016/S0092-8674(00)81526-3;
Kim L., Liu J., Kimmel A.R.;
"The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate
specification.";
Cell 99:399-408(1999).
[4]
FUNCTION.
PubMed=17085634; DOI=10.1128/EC.00204-06;
Strmecki L., Bloomfield G., Araki T., Dalton E., Skelton J.,
Schilde C., Harwood A., Williams J.G., Ivens A., Pears C.;
"Proteomic and microarray analyses of the Dictyostelium Zak1-GSK-3
signaling pathway reveal a role in early development.";
Eukaryot. Cell 6:245-252(2007).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
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).
-!- 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. ZakA negatively regulates
prestalk differentiation by regulating expression of ecmB.
Phosphorylates Y-214 of gsk3/gskA, in vitro.
{ECO:0000269|PubMed:10571182, ECO:0000269|PubMed:17085634,
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: Expression is first seen at 5 hours of
development during aggregation, reaching peak expression at slug
stage (15 hours). {ECO:0000269|PubMed:10571182}.
-!- PTM: N-terminal serine/threonine domain is capable of
autophosphorylation, in vitro, but to a lower extent than the
tyrosine kinase domain. May function as a negative regulator of
the tyrosine kinase domain.
-!- PTM: C-terminal tyrosine kinase domain is capable of
autophosphorylation, in vitro.
-!- 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; EAL69312.1; -; Genomic_DNA.
EMBL; AF200688; AAF14631.1; -; mRNA.
RefSeq; XP_643301.1; XM_638209.1.
ProteinModelPortal; Q75JK0; -.
STRING; 44689.DDB0185184; -.
iPTMnet; Q75JK0; -.
PaxDb; Q75JK0; -.
EnsemblProtists; EAL69312; EAL69312; DDB_G0276025.
GeneID; 8620347; -.
KEGG; ddi:DDB_G0276025; -.
dictyBase; DDB_G0276025; zakA.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; Q75JK0; -.
OMA; DLEHENK; -.
PhylomeDB; Q75JK0; -.
PRO; PR:Q75JK0; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IMP:UniProtKB.
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:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0033674; P:positive regulation of kinase activity; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:dictyBase.
GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0042659; P:regulation of cell fate specification; IMP:dictyBase.
GO; GO:0061118; P:regulation of positive chemotaxis to cAMP; IMP:dictyBase.
GO; GO:0007165; P:signal transduction; 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; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR008266; Tyr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 2.
SUPFAM; SSF56112; SSF56112; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
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 1 781 Dual specificity protein kinase zakA.
/FTId=PRO_0000328187.
DOMAIN 9 317 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 379 654 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 385 393 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 171 210 Poly-Asn.
COMPBIAS 337 340 Poly-Asp.
COMPBIAS 672 681 Poly-Asn.
COMPBIAS 758 776 Poly-Asn.
ACT_SITE 132 132 Proton acceptor. {ECO:0000250}.
ACT_SITE 507 507 Proton acceptor. {ECO:0000250}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 406 406 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 261 261 G -> S (in Ref. 3; AAF14631).
{ECO:0000305}.
CONFLICT 759 759 D -> G (in Ref. 3; AAF14631).
{ECO:0000305}.
SEQUENCE 781 AA; 89690 MW; F7AC84F07398782C CRC64;
MHYHNKDDWE EISFIGEGQY GRVIKCRKKN GFILNEQVDY VAIKIISKDK FKRNETDILE
KIRLFNIPRY YSHAEDDNFI YIYMEYIEGE NLANILKTKK QGRFKESRII SMIADLVETL
SFLHKHHVIH RDIKTANLVL DKNKNLKLID FGASTIQNKK QFEQYLNETT NNNNNPNNNN
NNNNNNNNNN NNNNNNNNNN NNINNINNNN DLNGSGSGIS TYLNEQYKQS SFAIIGTFNY
MAPEVKRNYR ATRKSDVWSL GCTIIEMAGG DLSQKLNGIP IIPDHLSDTL KDFLNHCLVI
DPKKRSYMEE LLSHKLIVHI IGPNKSKNYG VEPKFKDDDD FEEIENEKDN YLSSRFPAKF
APQYEKPKWE IEFEELEFDK DDSEGGAGNF GDVKKGLLNE TEVAIKFVKK AHCEAITVCD
TFYHEVLILS NLRHPNIVQF MAACIKYGEK ETNHCIVSEW MSGGNLTQFL MNNHKVLENN
PHLRVKLLTD IAKGILYLHK QHIIHRDLTS NNVLLDFKRE ILPNQLYGSN EFTAKVCDFG
LSSNQSESKK LRGGSIHYMA PENLNGSPIN EKSDIYSFGL LVWQMFSYAP PNTIYSPKEM
ASMVSDPKQN YRPQIPFNVP LKFKELITQC WDRNPLNRPK DFSIIIEKLK EIGLTYNRSS
SNVSPINSPL INNNNNNYNN NHLNSLSSSL NSSPTYYAKT FGDSNSNIDV YHSADSITPI
VSSPPIIKID LTQDDWDSKL KQLDLEHENK SLISISINDN NNNNINNNNT NNNNVNDLGY
C


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