PRK2_CAEEL
ID PRK2_CAEEL Reviewed; 441 AA.
AC Q20443;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase prk-2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P11309};
DE AltName: Full=PIM-related kinase 2 {ECO:0000312|WormBase:F45H7.4};
GN Name=prk-2 {ECO:0000312|WormBase:F45H7.4};
GN ORFNames=F45H7.4 {ECO:0000312|WormBase:F45H7.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=21115607; DOI=10.1242/dev.055350;
RA Zheng Q., Schaefer A.M., Nonet M.L.;
RT "Regulation of C. elegans presynaptic differentiation and neurite branching
RT via a novel signaling pathway initiated by SAM-10.";
RL Development 138:87-96(2011).
CC -!- FUNCTION: Involved in the negative regulation of synaptic
CC differentiation in PLM neurons. {ECO:0000269|PubMed:21115607}.
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 Evidence={ECO:0000250|UniProtKB:P11309};
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; Evidence={ECO:0000250|UniProtKB:P11309};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11309};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. PIM subfamily. {ECO:0000305}.
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DR EMBL; Z34800; CAA84323.2; -; Genomic_DNA.
DR PIR; T22255; T22255.
DR RefSeq; NP_497696.2; NM_065295.5.
DR AlphaFoldDB; Q20443; -.
DR SMR; Q20443; -.
DR STRING; 6239.F45H7.4.1; -.
DR PaxDb; Q20443; -.
DR EnsemblMetazoa; F45H7.4.1; F45H7.4.1; WBGene00004183.
DR EnsemblMetazoa; F45H7.4.2; F45H7.4.2; WBGene00004183.
DR GeneID; 175437; -.
DR KEGG; cel:CELE_F45H7.4; -.
DR CTD; 175437; -.
DR WormBase; F45H7.4; CE31517; WBGene00004183; prk-2.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000163427; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q20443; -.
DR OMA; EWFLHSL; -.
DR OrthoDB; 930292at2759; -.
DR PhylomeDB; Q20443; -.
DR PRO; PR:Q20443; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004183; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Neurogenesis; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..441
FT /note="Serine/threonine-protein kinase prk-2"
FT /id="PRO_0000432384"
FT DOMAIN 31..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 441 AA; 49769 MW; BA67320F60BA0334 CRC64;
MKKLASLQFF NLKLLLNGES SRGFSKFKKN YKLKAELGRG GFGVVYRAVR TCDNALVAVK
FIERSNVKEW ARINGEQVPM EICMLAKCSK VRGVIRLLDW YSIPEGFLIV MERPYPCIDM
FDFIKGQGKI SEDMARFLFR QIAVTVHECV QNRVLHRDLK DENIVIDLVT GSTKLIDFGA
ATVLRRSQYS DFQGTRLYCP PEWFLHSLYL GREAAVWSLG VLLYNSLNGR LPFRNEKDIC
TAHLLGPLPF FVPVSAEVKD LISKCLTFDP FQRCSLEAIL NHPWVKQQTL SWDALTKNKV
QKKTSESSDD HHSETLGDHS ETEEDRSPPT SSVSQQPGSA DEGVGLSASS SNTHNQKKPN
HKEFRMAKTS LLAPPTSIEM KAAVQASKTP TQFNVHTALK NQRQIKKHHS PQPPNSTVLT
ALRRAMSREA QNRISGVFSQ D
