KPC2_APLCA
ID KPC2_APLCA Reviewed; 743 AA.
AC Q16975;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Calcium-independent protein kinase C;
DE EC=2.7.11.13;
DE AltName: Full=APL II;
GN Name=PRKC2;
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 DOMAIN C2.
RX PubMed=8346555; DOI=10.1016/0968-0004(93)90189-t;
RA Sossin W.S., Schwartz J.H.;
RT "Ca(2+)-independent protein kinase Cs contain an amino-terminal domain
RT similar to the C2 consensus sequence.";
RL Trends Biochem. Sci. 18:207-208(1993).
RN [4]
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 [5]
RP ERRATUM OF PUBMED:9668085.
RA Pepio A.M., Fan X., Sossin W.S.;
RL J. Biol. Chem. 273:22856-22856(1998).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9477951; DOI=10.1021/bi971841u;
RA Pepio A.M., Sossin W.S.;
RT "The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits
RT phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive
RT manner.";
RL Biochemistry 37:1256-1263(1998).
CC -!- FUNCTION: This is calcium-independent, phospholipid-dependent,
CC serine- and threonine-specific enzyme.
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 -!- ACTIVITY REGULATION: Requires high levels of phosphatidylserine to be
CC activated. The presence of the C2 domain lowers the affinity of protein
CC kinase C activators for the C1 domains and this inhibition can be
CC removed by phosphatidylserine. Phosphatidic acid, however, is much more
CC potent than phosphatidylserine in reducing C2 domain-mediated
CC inhibition, suggesting that phosphatidic acid may be a required
CC cofactor for the activation of APL II.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in nervous tissues, ovotestis and gut.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M94884; AAA27771.1; -; mRNA.
DR RefSeq; NP_001191401.1; NM_001204472.1.
DR AlphaFoldDB; Q16975; -.
DR SMR; Q16975; -.
DR GeneID; 100533493; -.
DR OrthoDB; 222529at2759; -.
DR BRENDA; 2.7.11.13; 390.
DR GO; GO:0016020; C:membrane; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR CDD; cd05591; STKc_nPKC_epsilon; 1.
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; IPR034669; nPKC_epsilon.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PIRSF000551; PKC_delta; 1.
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; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..743
FT /note="Calcium-independent protein kinase C"
FT /id="PRO_0000055728"
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 403..663
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 665..736
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 176..226
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 247..297
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 311..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 527
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 409..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 743 AA; 84414 MW; 4C982C563CA2B659 CRC64;
MSRRAKMVFN GSVKIKVCEA VDLKPTDFSL RLQKGSTKEK ASQMIEPYVN IDVDEVYIAK
TTTKPKSVKP QWVWNEDFTS EVHNGQNVNL TVFHDAAIPP DEFVANCTIP FDDVKGKSDF
WIDLEPNGKL HVVIELCGSA TEAAESTPKE KVFKEKEGML NRRRGAMRRR VHQVNGHKFM
AMFFRQPTFC SLCRDFIWGL GKQGYQCQVC TCVVHKRCHQ HIVTKCPGSR DVANDEVTGK
RFNINVPHRF NVHNYRRPTF CDHCGSLLYG LVRQGLQCDV CKMNIHKRCQ KNVANNCGTN
TRDMAQILQE MGISGDKLRP KTKKLSISES HESPNKSSPM HERSLSSPIP VIQDSDEAQP
GEMGLPSDSL PVNASNEHQG SRTRSPSSDR SRSHHSRISL HDFNFIKVLG KGSFGKVMLA
EKKGTDEVYA IKVLKKDVII QDDDVECTMT EKRILALSAK HPFLTALHSS FQTKERLFFV
MEYVNGGDLM FQIQRARKFD EPRARFYAAE VTLALMFLHR HGIIYRDLKL DNILLDAEGH
CKIADFGMCK EGMTENKLTQ TFCGTPDYIA PEILQELKYD ASVDWWALGV LMYEMMAGQP
PFEADNEDDL FESILHDDVL YPVWLSKEAV SILKGFMTKN PAKRLGCVTT QGCEKAILVH
PFFHEKIDWE ALEQRKVKPP FKPKIKNKTD ANNFDRDFTS EDPVLTPVDP AVIKTINQEE
FRGFSFANPD YGKLEMEASG QAH
