CAMKI_MACNP
ID CAMKI_MACNP Reviewed; 345 AA.
AC W0LYS5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1 {ECO:0000305};
DE EC=2.7.11.17 {ECO:0000250|UniProtKB:Q63450};
DE AltName: Full=CaM kinase I {ECO:0000305};
DE Short=MnCaMKI {ECO:0000303|PubMed:24491503};
GN Name=CaMKI {ECO:0000312|EMBL:AHG30903.1};
OS Macrobrachium nipponense (Oriental river shrimp) (Palaemon nipponensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC Palaemonoidea; Palaemonidae; Macrobrachium.
OX NCBI_TaxID=159736 {ECO:0000312|EMBL:AHG30903.1};
RN [1] {ECO:0000312|EMBL:AHG30903.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Hepatopancreas {ECO:0000303|PubMed:24491503};
RX PubMed=24491503; DOI=10.1016/j.gene.2014.01.055;
RA Shen H., Hu Y., Zhang Y., Zhou X., Xu Z.;
RT "Calcium-calmodulin dependent protein kinase I from Macrobrachium
RT nipponense: cDNA cloning and involvement in molting.";
RL Gene 538:235-243(2014).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in
CC the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium
CC influx, regulates transcription activators activity, cell cycle,
CC hormone production, cell differentiation, actin filament organization
CC and neurite outgrowth (By similarity). Involved in molting (Probable).
CC {ECO:0000250|UniProtKB:Q63450, ECO:0000305|PubMed:24491503}.
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 Evidence={ECO:0000250|UniProtKB:Q63450};
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; Evidence={ECO:0000250|UniProtKB:Q63450};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin results in conformational change that relieves intrasteric
CC autoinhibition. {ECO:0000250|UniProtKB:Q63450}.
CC -!- TISSUE SPECIFICITY: Highly expressed in hepatopancreas and to a lesser
CC extent in gills. Low expression in hemocytes, testis, ovary, heart,
CC eyestalk, muscle and epidermis. {ECO:0000269|PubMed:24491503}.
CC -!- DEVELOPMENTAL STAGE: Higher expression level in the premolt stage in
CC hepatopancreas (2.7-fold), muscle (5.2-fold) and epidermis (2.3-fold)
CC compared to the intermolt stage. Expression is down-regulated in the
CC postmolt stage in hepatopancreas and muscle, but remains high in
CC epidermis. {ECO:0000269|PubMed:24491503}.
CC -!- INDUCTION: During molting and in response to eyestalk ablation.
CC {ECO:0000269|PubMed:24491503}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250|UniProtKB:Q63450}.
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; KF469224; AHG30903.1; -; mRNA.
DR AlphaFoldDB; W0LYS5; -.
DR SMR; W0LYS5; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0022404; P:molting cycle process; IEP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS: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 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Calmodulin-binding; Kinase;
KW Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..345
FT /note="Calcium/calmodulin-dependent protein kinase type 1"
FT /id="PRO_0000439089"
FT DOMAIN 31..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..327
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 307..328
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
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 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 345 AA; 39243 MW; A4272B64AF5AEAEA CRC64;
MPLFGSKKET AKKSSKKDKD EGKMPAVEDK YILKDLLGTG AFSQVRLAEV KEDPSRVVAI
KIIDKKALKG KEDSLENEIR VLRRLQHPNI VQLMETYEDR EHVYLIIELV TGGELFDRIV
EKGSYTEKDA SDLIRQVLEA VDYMHDQGVV HRDLKPENLL YYSPDEDSKI MISDFGLSKM
EDSGIMATAC GTPGYVAPEV LAQKPYGKAV DVWSIGVIAY ILLCGYPPFY DENDANLFAQ
ILKGEFEFDS PYWDEISESA KDFIRQLMCV DVEKRYTCKQ ALGHPWISGN AASTENIHSS
VSEQLKKNFA KSRWRQAYHA TAVIRQMRLF ATKQVIVRRK LSESQ
