KPC1_APLCA
ID KPC1_APLCA Reviewed; 649 AA.
AC Q16974;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Calcium-dependent protein kinase C;
DE EC=2.7.11.13;
DE AltName: Full=APL I;
GN Name=PRKC1;
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1869917; DOI=10.1523/jneurosci.11-08-02303.1991;
RA Kruger K.E., Sossin W.S., Sacktor T.C., Bergold P.J., Beushausen S.,
RA Schwartz J.H.;
RT "Cloning and characterization of Ca(2+)-dependent and Ca(2+)-independent
RT PKCs expressed in Aplysia sensory cells.";
RL J. Neurosci. 11:2303-2313(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=8449941; DOI=10.1016/s0021-9258(18)53384-6;
RA Sossin W.S., Diaz-Arrastia R., Schwartz J.H.;
RT "Characterization of two isoforms of protein kinase C in the nervous system
RT of Aplysia californica.";
RL J. Biol. Chem. 268:5763-5768(1993).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9668085; DOI=10.1074/jbc.273.30.19040;
RA Pepio A.M., Fan X., Sossin W.S.;
RT "The role of C2 domains in Ca2+-activated and Ca2+-independent protein
RT kinase Cs in aplysia.";
RL J. Biol. Chem. 273:19040-19048(1998).
RN [4]
RP ERRATUM OF PUBMED:9668085.
RA Pepio A.M., Fan X., Sossin W.S.;
RL J. Biol. Chem. 273:22856-22856(1998).
CC -!- FUNCTION: This is calcium-dependent, phospholipid-dependent,
CC serine- and threonine-specific enzyme. Activation of PKC by serotonin
CC results in presynaptic facilitation of depressed sensory-to-motor
CC neuron synapses, which is thought to underlie behavioral
CC dishabituation.
CC -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC phosphorylates a range of cellular proteins. PKC also serves as the
CC receptor for phorbol esters, a class of tumor promoters (By
CC similarity). {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=2.7.11.13;
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=2.7.11.13;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Activated by phosphatidylserine.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Translocated to neuronal
CC membranes.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; M94883; AAA27770.2; -; mRNA.
DR RefSeq; NP_001191415.1; NM_001204486.1.
DR AlphaFoldDB; Q16974; -.
DR SMR; Q16974; -.
DR PRIDE; Q16974; -.
DR GeneID; 100533518; -.
DR OrthoDB; 614710at2759; -.
DR BRENDA; 2.7.11.13; 390.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..649
FT /note="Calcium-dependent protein kinase C"
FT /id="PRO_0000055727"
FT DOMAIN 138..259
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 320..578
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 579..649
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 21..71
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 85..135
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 326..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 649 AA; 74079 MW; A53253399284E330 CRC64;
MEKRVARRGA LRQKNVHEVK NHKFLARFFK QPTFCSHCKD FIWGFGKQGF QCQVCSLVVH
KRCHEFVCFI CPGADKGPDS DATNLHKFKL HSYGSPTFCD HCGSLLYGLL HQGLKCDSCD
MNVHKRCEKN VPLLCGTDHT ERRGRILIKG AVKGSKVLVE ILEAKNLCPM DPNGLADPYV
KVKLIPYDAH KLKLKTKTIK ASLNPVWNES FTVDIGPEDN SKRLSLEVWD WDRTSRNDFM
GSLSFGISEL IKSPVEGWFK LLNQEEGEFY GVPVTDDITE SIQEIKSKMH RSSISSEKRY
PEPDKVQNMS KQDIVRASDF NFLTVLGKGS FGKVVLAERK GTDELYAIKI LKKDVIIQDD
DVECTMIEKR VLALPDKPPF LVQLHSCFQT MDRLYFVMEY VNGGDLMYRI QQEGKFKEPV
AAFYAAEIAI GLFYLHTQGI VYRDLKLDNV MLDAEGHIKI ADFGMCKENI MGDKTTRTFC
GTPDYIAPEI VLYQPYGRSV DWWAYGVLLY EMLAGQPPFD GEDEEELFTS ITDHNVSYPK
ALSREAVSLC KGLLTKTPAK RLGCGPNGER DIKDRAFFRP IQWERIELRE VQPPYKPRIK
SRKDVSNFDR EFTSEAPNVT PTDKLFIMNL DQCEFSGFSY VNPEFVVTV
