ID PKD1_DICDI Reviewed; 714 AA.
AC P34100; Q550C5; Q86AR2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Developmentally-regulated protein kinase 1;
DE EC=2.7.11.1;
GN Name=pkaD; Synonyms=PK1; ORFNames=DDB_G0277145;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 299-714, AND DEVELOPMENTAL STAGE.
RX PubMed=1864510; DOI=10.1016/0378-1119(91)90538-m;
RA Buerki E., Anjard C., Scholder J.-C., Reymond C.D.;
RT "Isolation of two genes encoding putative protein kinases regulated during
RT Dictyostelium discoideum development.";
RL Gene 102:57-65(1991).
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 -!- DEVELOPMENTAL STAGE: Expressed in vegetatively growing cells and during
CC development. {ECO:0000269|PubMed:1864510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the AGC Ser/Thr protein kinase
CC family, lacks the AGC-kinase C-terminal domain at the C-terminus.
CC {ECO:0000305}.
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DR EMBL; AAFI02000019; EAL68758.1; -; Genomic_DNA.
DR EMBL; M38794; AAA33239.1; -; mRNA.
DR PIR; PQ0207; PQ0207.
DR RefSeq; XP_642691.1; XM_637599.1.
DR AlphaFoldDB; P34100; -.
DR SMR; P34100; -.
DR STRING; 44689.P34100; -.
DR PaxDb; 44689-DDB0185224; -.
DR EnsemblProtists; EAL68758; EAL68758; DDB_G0277145.
DR GeneID; 8620880; -.
DR KEGG; ddi:DDB_G0277145; -.
DR dictyBase; DDB_G0277145; pkaD.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_387059_0_0_1; -.
DR InParanoid; P34100; -.
DR OMA; FIMEYAG; -.
DR Reactome; R-DDI-163615; PKA activation.
DR Reactome; R-DDI-164378; PKA activation in glucagon signalling.
DR Reactome; R-DDI-180024; DARPP-32 events.
DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-DDI-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-DDI-5610787; Hedgehog 'off' state.
DR Reactome; R-DDI-8963896; HDL assembly.
DR Reactome; R-DDI-9634597; GPER1 signaling.
DR PRO; PR:P34100; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF110; DEVELOPMENTALLY-REGULATED PROTEIN KINASE 1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..714
FT /note="Developmentally-regulated protein kinase 1"
FT /id="PRO_0000086551"
FT DOMAIN 334..589
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 88..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 340..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 299..325
FT /note="IICSSPIVNIPPPFYLDGSIDPVENID -> LFHKAKFQECHKNLISIVHYV
FT AFKVLT (in Ref. 3; AAA33239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 81674 MW; 2C8F7A359D95ED1F CRC64;
MSAILNNYQY IPNNSLNSNN SNNGNNSTIL SLCDNATQLM DIIMREFNEP IFDYNQNSSE
INKSLVKTIK SLLETLTKNL NNINNNINNN ISNNNNNNNN NNNNNNNNNN NNNNINNNNN
FNTPQIIIND NYKLYTPPPA PMLKGLSCEV PFETMEYMQP LDLSNNNISL NNSCNMINND
NNNNNNNNNN NNNNNNNNNN QQQQFYNAPS SNSTPSHSSP SSPTTSSIPF HPNFTLSQDN
FNQQLQNNNN SNNNSNNNNN NNIINNNFLQ NSQQTNQSLQ FSTTQPNLNN FYDIPKQPII
CSSPIVNIPP PFYLDGSIDP VENIDWKRTK ISDFNFYGSL GSGSFGTAKL CRHRGSGLFF
CSKTLRRETI VHEKHKEHVN NEINIMLNIS HPYIVKTYST FNTPTKIHFI MEYAGKKDLF
HHLRANKCFT EQTTKLIVAE IVLAIEYLHA ENIIYRDLKP ENILIDEKGH IKLTDFGFSK
KTVGGKNTSS VCGTFDYMAP EILNSSNGHG KPVDWWALGV VVYELVTGKL PFSNSKESLL
NRKADFQLIF QNSYLSDEIK DFIFQLLSVD PSKRLGTFDS CSIRNHKWFS DINWLHLESK
YQIDGPLSTL NSFINCDFNI NLLKKSKSYT EQQQQQQQLP QQQQQQQQNN QLFNQTLQQQ
NFNFHPIQPQ QQQQQQFFNF QFNNNNFNNN NNNNNNFNEA CTSNTCGGTT ASIF
//
