Reviewed, UniProtKB/Swiss-Prot Q16975 (KPC2_APLCA)

Names and origin

Protein names

Recommended name:
    Calcium-independent protein kinase C
    EC=2.7.11.13
Alternative name(s):
    APL II

Gene names

Name:

PRKC2

Organism

Aplysia californica (California sea hare)

Taxonomic identifier

6500 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Mollusca › Gastropoda › Orthogastropoda › Apogastropoda › Heterobranchia › Euthyneura › Opisthobranchia › Aplysiomorpha › Aplysioidea › Aplysiidae › Aplysia

Protein attributes

Sequence length	743 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Requires high levels of phosphatidylserine to be activated. The presence of the C2 domain lowers the affinity of protein kinase C activators for the C1 domains and this inhibition can be removed by phosphatidylserine. Phosphatidic acid, however, is much more potent than phosphatidylserine in reducing C2 domain-mediated inhibition, suggesting that phosphatidic acid may be a required cofactor for the activation of APL II.
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Expressed in nervous tissues, ovotestis and gut.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 743	743	Calcium-independent protein kinase C		PRO_0000055728
Regions
	Domain	1 – 108	108	C2
	Domain	403 – 663	261	Protein kinase
	Domain	665 – 736	72	AGC-kinase C-terminal
	Zinc finger	176 – 226	51	Phorbol-ester/DAG-type 1
	Zinc finger	247 – 297	51	Phorbol-ester/DAG-type 2
	Nucleotide binding	409 – 417	9	ATP By similarity
Sites
	Active site	527	1	Proton acceptor By similarity
	Binding site	432	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q16975-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4C982C563CA2B659	FASTA	743	84,414
	10 20 30 40 50 60 MSRRAKMVFN GSVKIKVCEA VDLKPTDFSL RLQKGSTKEK ASQMIEPYVN IDVDEVYIAK 70 80 90 100 110 120 TTTKPKSVKP QWVWNEDFTS EVHNGQNVNL TVFHDAAIPP DEFVANCTIP FDDVKGKSDF 130 140 150 160 170 180 WIDLEPNGKL HVVIELCGSA TEAAESTPKE KVFKEKEGML NRRRGAMRRR VHQVNGHKFM 190 200 210 220 230 240 AMFFRQPTFC SLCRDFIWGL GKQGYQCQVC TCVVHKRCHQ HIVTKCPGSR DVANDEVTGK 250 260 270 280 290 300 RFNINVPHRF NVHNYRRPTF CDHCGSLLYG LVRQGLQCDV CKMNIHKRCQ KNVANNCGTN 310 320 330 340 350 360 TRDMAQILQE MGISGDKLRP KTKKLSISES HESPNKSSPM HERSLSSPIP VIQDSDEAQP 370 380 390 400 410 420 GEMGLPSDSL PVNASNEHQG SRTRSPSSDR SRSHHSRISL HDFNFIKVLG KGSFGKVMLA 430 440 450 460 470 480 EKKGTDEVYA IKVLKKDVII QDDDVECTMT EKRILALSAK HPFLTALHSS FQTKERLFFV 490 500 510 520 530 540 MEYVNGGDLM FQIQRARKFD EPRARFYAAE VTLALMFLHR HGIIYRDLKL DNILLDAEGH 550 560 570 580 590 600 CKIADFGMCK EGMTENKLTQ TFCGTPDYIA PEILQELKYD ASVDWWALGV LMYEMMAGQP 610 620 630 640 650 660 PFEADNEDDL FESILHDDVL YPVWLSKEAV SILKGFMTKN PAKRLGCVTT QGCEKAILVH 670 680 690 700 710 720 PFFHEKIDWE ALEQRKVKPP FKPKIKNKTD ANNFDRDFTS EDPVLTPVDP AVIKTINQEE 730 740 FRGFSFANPD YGKLEMEASG QAH

References

[1]	"Cloning and characterization of Ca(2+)-dependent and Ca(2+)-independent PKCs expressed in Aplysia sensory cells." Kruger K.E., Sossin W.S., Sacktor T.C., Bergold P.J., Beushausen S., Schwartz J.H. J. Neurosci. 11:2303-2313(1991) [PubMed: 1869917] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of two isoforms of protein kinase C in the nervous system of Aplysia californica." Sossin W.S., Diaz-Arrastia R., Schwartz J.H. J. Biol. Chem. 268:5763-5768(1993) [PubMed: 8449941] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Ca(2+)-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence." Sossin W.S., Schwartz J.H. Trends Biochem. Sci. 18:207-208(1993) [PubMed: 8346555] [Abstract] Cited for: DOMAIN C2.
[4]	"The role of C2 domains in Ca2+-activated and Ca2+-independent protein kinase Cs in aplysia." Pepio A.M., Fan X., Sossin W.S. J. Biol. Chem. 273:19040-19048(1998) [PubMed: 9668085] [Abstract] Cited for: CHARACTERIZATION.
[5]	Erratum Pepio A.M., Fan X., Sossin W.S. J. Biol. Chem. 273:22856-22856(1998)
[6]	"The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner." Pepio A.M., Sossin W.S. Biochemistry 37:1256-1263(1998) [PubMed: 9477951] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M94884 mRNA. Translation: AAA27771.1.
3D structure databases
HSSP	HSSP built from PDB template 1GMI based on UniProtKB P09216.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.11.13. 629.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR020454. DAG/PE_bd. IPR015745. PKC. IPR017892. Pkinase_C. IPR014376. Prot_kin_PKC_delta. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
Pfam	PF00130. C1_1. 2 hits. PF00168. C2. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000551. PKC_delta. 1 hit.
PRINTS	PR00008. DAGPEDOMAIN.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS50004. C2. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 2 hits. PS50081. ZF_DAG_PE_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPC2_APLCA

Accession

Primary (citable) accession number: Q16975

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)