KCC2D_CHICK
ID KCC2D_CHICK Reviewed; 479 AA.
AC Q5ZKI0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II delta chain;
DE Short=CaM kinase II subunit delta;
DE Short=CaM-kinase II delta chain;
DE Short=CaMK-II subunit delta;
DE EC=2.7.11.17;
GN Name=CAMK2D; ORFNames=RCJMB04_10k21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the central
CC nervous system. {ECO:0000250}.
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=2.7.11.17;
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=2.7.11.17;
CC -!- ACTIVITY REGULATION: Autophosphorylation of CAMK2 plays an important
CC role in the regulation of the kinase activity. {ECO:0000250}.
CC -!- SUBUNIT: CAMK2 is composed of four different chains: alpha, beta,
CC gamma, and delta. The different isoforms assemble into homo- or
CC heteromultimeric holoenzymes composed of 8 to 12 subunits (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AJ720104; CAG31763.1; -; mRNA.
DR RefSeq; NP_001034389.1; NM_001039300.1.
DR AlphaFoldDB; Q5ZKI0; -.
DR SMR; Q5ZKI0; -.
DR STRING; 9031.ENSGALP00000019616; -.
DR PRIDE; Q5ZKI0; -.
DR GeneID; 422688; -.
DR KEGG; gga:422688; -.
DR CTD; 817; -.
DR VEuPathDB; HostDB:geneid_422688; -.
DR eggNOG; KOG0033; Eukaryota.
DR InParanoid; Q5ZKI0; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q5ZKI0; -.
DR PRO; PR:Q5ZKI0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-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; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; SSF54427; 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 2: Evidence at transcript level;
KW ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..479
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT delta chain"
FT /id="PRO_0000277820"
FT DOMAIN 14..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 54203 MW; 240FC3EF445F1A33 CRC64;
MASTATCTRF TDEYQLFEEL GKGAFSVVRR CMKITTGQEY AAKIINTKKL SARDHQKLER
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY
LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT
VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL
KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI IKVTEQLIEA
INNGDFEAYT KICDPGLTSF EPEALGNLVE GMDFHRFYFE NALSKSNKPI HTIILNPHVH
LVGDDAACIA YIRLTQYMDG TGMPKTMQSE ETRVWHRRDG KWQNVHFHRS GSPTVPINA
