PK2_DICDI
ID PK2_DICDI Reviewed; 479 AA.
AC P28178; Q54GH5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein kinase 2;
DE Short=PK2;
DE EC=2.7.11.1;
GN Name=pkgB; Synonyms=pfkA, pkbr1; ORFNames=DDB_G0290157;
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].
RX PubMed=1996312; DOI=10.1073/pnas.88.4.1115;
RA Haribabu B., Dottin R.P.;
RT "Identification of a protein kinase multigene family of Dictyostelium
RT discoideum: molecular cloning and expression of a cDNA encoding a
RT developmentally regulated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1115-1119(1991).
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 SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, FUNCTION,
RP AND MUTAGENESIS OF THR-309 AND THR-470.
RX PubMed=10873800; DOI=10.1016/s0960-9822(00)00536-4;
RA Meili R., Ellsworth C., Firtel R.A.;
RT "A novel Akt/PKB-related kinase is essential for morphogenesis in
RT Dictyostelium.";
RL Curr. Biol. 10:708-717(2000).
RN [4]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-309 AND
RP THR-470, AND FUNCTION.
RX PubMed=18635356; DOI=10.1016/j.cub.2008.06.068;
RA Kamimura Y., Xiong Y., Iglesias P.A., Hoeller O., Bolourani P.,
RA Devreotes P.N.;
RT "PIP3-independent activation of TorC2 and PKB at the cell's leading edge
RT mediates chemotaxis.";
RL Curr. Biol. 18:1034-1043(2008).
CC -!- FUNCTION: Required for morphogenesis during multicellular development.
CC Phosphorylates talB, gefN, gefS, PI4P 5-kinase and gacQ.
CC {ECO:0000269|PubMed:10873800, ECO:0000269|PubMed:18635356}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor;
CC Cytoplasmic side. Note=Persistently localized on the cell membrane.
CC -!- DEVELOPMENTAL STAGE: Levels increase upon the initiation of development
CC and are maximal during aggregation, decrease 2-3-fold and remain
CC constant throughout the slug stage. A switch from ubiquitous expression
CC in all cells during growth and aggregation in early development to
CC expression restricted to cells found at the top of the mound during tip
CC formation is observed (at protein levels). Encodes a 2.0 kb and a 2.2
CC kb transcript. The smaller one is expressed, at low levels, in
CC vegetative cells, and the larger one during development. Ubiquitously
CC found in early development and then restricted to the apical cells in
CC developing aggregates. {ECO:0000269|PubMed:10873800}.
CC -!- INDUCTION: The 2.2 kb transcript is probably induced by exogenous cAMP
CC via a cell-surface receptor-mediated signal transduction pathway. The
CC smaller transcript is induced by starvation at the onset of
CC development, with transcript levels peaking at 4-8 hours during the
CC aggregation stage. By 8 hours of development, the larger transcript is
CC induced and peaks at the mound stage (12 hours).
CC -!- PTM: Seems to be myristoylated.
CC -!- DISRUPTION PHENOTYPE: pkgB null cells arrest development at the mound
CC stage, have chemotaxis defects and are defective in morphogenesis and
CC multicellular development. Some mounds are able to round up and become
CC almost spherical. Some of the mounds form an aberrant sorus atop an
CC irregular stalk-like structure without proceeding through the normal
CC intermediate stage and without stalk tube. pkbA-/pkgB-cells exhibit
CC growth defects and show stronger chemotaxis and cell-polarity defects
CC than pkbA- cells. They also move slowly and do not aggregate at lower
CC cell densities at which parental strain aggregate normally.
CC {ECO:0000269|PubMed:10873800, ECO:0000269|PubMed:18635356}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR EMBL; M59744; AAA33186.1; -; mRNA.
DR EMBL; AAFI02000158; EAL62350.1; -; Genomic_DNA.
DR PIR; A38578; A38578.
DR RefSeq; XP_635853.1; XM_630761.1.
DR AlphaFoldDB; P28178; -.
DR SMR; P28178; -.
DR STRING; 44689.DDB0191365; -.
DR iPTMnet; P28178; -.
DR PaxDb; P28178; -.
DR EnsemblProtists; EAL62350; EAL62350; DDB_G0290157.
DR GeneID; 8627509; -.
DR KEGG; ddi:DDB_G0290157; -.
DR dictyBase; DDB_G0290157; pkgB.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P28178; -.
DR OMA; HICITDF; -.
DR PhylomeDB; P28178; -.
DR BRENDA; 2.7.11.1; 1939.
DR PRO; PR:P28178; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:dictyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0110094; P:polyphosphate-mediated signaling; IGI:dictyBase.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IGI:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CACAO.
DR GO; GO:0050920; P:regulation of chemotaxis; IGI:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR CDD; cd05123; STKc_AGC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP; Cell membrane; Chemotaxis; Cytoplasm; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..479
FT /note="Protein kinase 2"
FT /id="PRO_0000086546"
FT DOMAIN 153..407
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 408..479
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 159..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 309
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18635356"
FT MUTAGEN 309
FT /note="T->A: Loss of activity; when associated with A-470."
FT /evidence="ECO:0000269|PubMed:10873800"
FT MUTAGEN 470
FT /note="T->A: Loss of activity; when associated with A-309."
FT /evidence="ECO:0000269|PubMed:10873800"
FT CONFLICT 62
FT /note="T -> A (in Ref. 1; AAA33186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52994 MW; 4F1609B2564016D5 CRC64;
MGKGQSKIKN GGSGKPAKAG KPKKGNKNDE TTPTSTPTPT PTPTQQNLDN SAQQQQQQQQ
TTTAAVSLDN KEQQQQQNIP APATQTPITQ TGTPTIEESQ KNTDNNNING ASNEASSSPD
SPNGSGNGND DEDEGPEEVI FSKNKQSATK DDFELLNVIG KGSFGKVMQV KKKGEDKIFA
MKVLRKDAII ARKQVNHTKS EKTILQCISH PFIVNLHYAF QTKDKLYMVL DFVNGGELFF
HLKREGRFSE PRVKIYAAEI VSALDHLHKQ DIVYRDLKPE NILLDSEGHI CITDFGLSKK
IETTDGTFTF CGTPEYLAPE VLNGHGHGCA VDWWSLGTLL YEMLTGLPPF YSQNVSTMYQ
KILNGELKIP TYISPEAKSL LEGLLTREVD KRLGTKGGGE VKQHPWFKNI DWEKLDRKEV
EVHFKPKVKS GTDISQIDPV FTQERPMDSL VETSALGDAM GKDTSFEGFT YVADSILKD
