(data stored in ACNUC26462 zone)

HOGENOM: CAEELIV_PE401

ID   CAEELIV_PE401                        STANDARD;      PRT;   348 AA.
AC   CAEELIV_PE401; Q9TXJ0; Q6V5R5; Q9UAH6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1;
DE   EC=2.7.11 17;AltName: Full=CaM kinase I; Short=CaM-KI; (CAEELIV.PE401).
GN   Name=cmk-1; ORFNames=K07A9.2;
OS   CAENORHABDITIS ELEGANS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Pseudocoelomata; Nematoda;
OC   Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAEELIV.PE401.
CC       Caenorhabditis elegans chromosome IV WS210  sequence 1..17493784
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CMK1_CAEEL
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a calcium-triggered signaling cascade which results in
CC       transcriptional activation, at least in part through
CC       phosphorylation of crh-1. Regulates gene expression, sensory
CC       morphology, and function of the AFD thermosensory neurons.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin results in a conformational change that generates
CC       functional binding sites for both substrate and ATP, and thus
CC       relieves autoinhibition and lowers the Km of substrate binding.
CC       Must be phosphorylated by ckk-1 to be maximally active but this
CC       does not appear to be required for activity in AFD neurons.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=657 uM for syntide-2 (when cmk-1 is not phosphorylated on
CC         Thr-179);
CC         KM=20 uM for syntide-2 (when cmk-1 is phosphorylated on Thr-
CC         179);
CC         Vmax=0.1 mmol/min/mg enzyme (irrespective of phosphorylation
CC         status of Thr-179);
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in head and tail neurons and vulval
CC       muscles.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and interacts in the inactive folded state with the
CC       catalytic domain as a pseudosubstrate (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Changes in thermosensory behavior and
CC       temperature-dependent defects in AFD-specific gene expression.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Caenorhabditis_elegans;K07A9.2;K07A9.2;K07A9.2.
DR   EMBL; AB021864; - ;
DR   EMBL; AF099924; - ;
DR   EMBL; AY350451; - ;
DR   UniProtKB/Swiss-Prot; Q9TXJ0; Q6V5R5; Q9UAH6; -.
DR   EMBL; AB021864; BAA82674.1; -; mRNA.
DR   EMBL; AF099924; AAF23187.1; -; Genomic_DNA.
DR   EMBL; AY350451; AAQ54691.1; -; mRNA.
DR   RefSeq; NP_500139.1; NM_067738.5.
DR   UniGene; Cel.19564; -.
DR   HSSP; P49137; 1NXK.
DR   ProteinModelPortal; Q9TXJ0; -.
DR   SMR; Q9TXJ0; 18-318.
DR   DIP; DIP-26403N; -.
DR   IntAct; Q9TXJ0; 1.
DR   MINT; MINT-1083450; -.
DR   STRING; Q9TXJ0; -.
DR   PRIDE; Q9TXJ0; -.
DR   EnsemblMetazoa; K07A9.2; K07A9.2; K07A9.2.
DR   GeneID; 176989; -.
DR   KEGG; cel:K07A9.2; -.
DR   NMPDR; fig|6239.3.peg.12560; -.
DR   UCSC; K07A9.2; c. elegans.
DR   CTD; 176989; -.
DR   WormBase; K07A9.2; CE25046; WBGene00000553; cmk-1.
DR   InParanoid; Q9TXJ0; -.
DR   OMA; RHNNIVQ; -.
DR   PhylomeDB; Q9TXJ0; -.
DR   NextBio; 894874; -.
DR   ArrayExpress; Q9TXJ0; -.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IDA:WormBase.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:WormBase.
DR   GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:WormBase.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:WormBase.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IMP:WormBase.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:WormBase.
DR   InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   PANTHER; PTHR24347; PTHR24347; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; CAEELIV.PE401; -.
KW   K07A9.2.3310200367fold_1320000031; K07A9.2.3.12110.62fold_1320000031;
KW   Q9TXJ0_CAEEL; Q9UAH6_CAEEL; AB021864; AF099924; AY350451;
KW   Allosteric enzyme; ATP-binding; Calmodulin-binding; Complete proteome;
KW   Developmental protein; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   348 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPLFKRRDGS GPAPNATIRE KYDFRDVLGT GAFSKVFLAE SKSDAGQMYA VKCIDKKALK
     GKEESLENEI KVLRKLRHNN IVQLFDTYDE KQFVYLVMEL VTGGELFDRI VAKGSYTEQD
     ASNLIRQVLE AVGFMHDNGV VHRDLKPENL LYYNQDEDSK IMISDFGLSK TEDSGVMATA
     CGTPGYVAPE VLQQKPYGKA VDVWSIGVIA YILLCGYPPF YDESDANLFA QIIKGEYEFD
     APYWDQISDS AKDFITHLMC CDPEARFTCQ DALSHPWISG NTAYTHDIHG TVAVHLKKSL
     AKRNWKKAYN AAAAIRQLQM LRLSSNSNRL QKQASQQQPE PPTPAFHA
//

If you have problems or comments...

PBIL Back to PBIL home page