P13677 (KPC2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C, eye isozyme
EC=2.7.11.13

Alternative name(s):
Eye-PKC
Inactivation no after-potential C protein
Short name=Protein INAC
Photoreceptor-specific PKC
dPKC53E(EY)

Gene names

Name:	inaC
Synonyms:	PKC2
ORF Names:	CG6518

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. This isozyme is a negative regulator of the visual transduction cascade and has been shown to be required for photoreceptor cell inactivation and light adaptation. Negative regulation is dependent on interaction with scaffolding protein inaD. Ref.1
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Tissue specificity	Exclusively expressed in photoreceptor cells. Ref.1
Developmental stage	Expression primarily in adults. Ref.1
Domain	Tetrapeptide ligand at C-terminus is tethered to inaD by interaction with the second PDZ domain.
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
Biological process	Sensory transduction Vision
Domain	Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	adaptation of rhodopsin mediated signaling Inferred from mutant phenotype. Source: FlyBase calcium-mediated signaling Traceable author statement. Source: FlyBase cellular component movement Inferred from mutant phenotype. Source: FlyBase deactivation of rhodopsin mediated signaling Inferred from mutant phenotype. Source: FlyBase female gonad development Inferred from mutant phenotype. Source: FlyBase inhibition of phospholipase C activity involved in G-protein coupled receptor signaling pathway Inferred from mutant phenotype. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase response to ethanol Inferred from direct assay. Source: FlyBase
Cellular component	inaD signaling complex Traceable author statement. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.5. Source: UniProtKB protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
inaD	Q24008	2	EBI-130595,EBI-195326

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Protein kinase C, eye isozyme		PRO_0000055731
Regions
	Domain	206 – 295	90	C2
	Domain	371 – 629	259	Protein kinase
	Domain	630 – 700	71	AGC-kinase C-terminal
	Zinc finger	71 – 121	51	Phorbol-ester/DAG-type 1
	Zinc finger	136 – 186	51	Phorbol-ester/DAG-type 2
	Nucleotide binding	377 – 385	9	ATP By similarity
Sites
	Active site	495	1	Proton acceptor By similarity
	Binding site	400	1	ATP By similarity
Experimental info
	Mutagenesis	697	1	I → E: No interaction with inaD. Ref.5
	Mutagenesis	697	1	I → K: 90% reduced interaction with inaD. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P13677 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 41B6BFF7FF3F6F8F	FASTA	700	79,844
	10 20 30 40 50 60 MAAAAVATPG ATVLPPSVPS AAPGAKAPAA GAGKGPGNLL EITGEANIVN YMKNRLRKGA 70 80 90 100 110 120 MKRKGLEMVN GHRFGVRFFK NPTYCGHCKD FIWGFGKQGF QCEECRFNIH QKCCKFVVFK 130 140 150 160 170 180 CPGKDTDFDA DCAKVKHGWI STTYTTPTFC DECGLLLHGV AHQGVKCENC NLNVHHACQE 190 200 210 220 230 240 TVPPMCGADI SEVRGKLLLY VELKGNNLKV DIKEAANLIP MDTNGFSDPY IAVQMHPDRS 250 260 270 280 290 300 GRTKKKTKTI QKNLNPVFNE TFTFELQPQD RDKRLLIEVW DWDRTSRNDF MGSFSFSLEE 310 320 330 340 350 360 LQKEPVDGWY KFLSQVEGEH YNIPCVDAFN DIARLRDEVR HDRRPNEKRR MDNKDMPHNM 370 380 390 400 410 420 SKRDMIRAAD FNFVKVIGKG SFGKVLLAER RGTDELYAVK VLRKDVIIQT DDMELPMNEK 430 440 450 460 470 480 KILALSGRPP FLVSMHSCFQ TMDRLFFVME YCKGGDLMYH MQQYGRFKES VAIFYAVEVA 490 500 510 520 530 540 IALFFLHERD IIYRDLKLDN ILLDGEGHVK LVDFGLSKEG VTERQTTRTF CGTPNYMAPE 550 560 570 580 590 600 IVSYDPYSIA ADWWSFGVLL FEFMAGQAPF EGDDETTVFR NIKDKKAVFP KHFSVEAMDI 610 620 630 640 650 660 ITSFLTKKPN NRLGAGRYAR QEITTHPFFR NVDWDKAEAC EMEPPIKPMI KHRKDISNFD 670 680 690 700 DAFTKEKTDL TPTDKLFMMN LDQNDFIGFS FMNPEFITII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two new Drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells." Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C. Cell 57:403-412(1989) [PubMed: 2720775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"The second PDZ domain of INAD is a type I domain involved in binding to eye protein kinase C. Mutational analysis and naturally occurring variants." Kumar R., Shieh B.-H. J. Biol. Chem. 276:24971-24977(2001) [PubMed: 11342563] [Abstract] Cited for: MUTAGENESIS OF ILE-697, INTERACTION WITH INAD.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04845 mRNA. Translation: AAA28817.1. AE013599 Genomic DNA. Translation: AAF57934.1. BT004495 mRNA. Translation: AAO42659.1.
PIR	A32392.
RefSeq	NP_476863.1. NM_057515.2.
UniGene	Dm.4688.
3D structure databases
ProteinModelPortal	P13677.
SMR	P13677. Positions 68-698.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-54N.
IntAct	P13677. 3 interactions.
MINT	MINT-922757.
STRING	P13677.
Proteomic databases
PRIDE	P13677.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087047; FBpp0086196; FBgn0004784.
GeneID	36897.
KEGG	dme:Dmel_CG6518.
NMPDR	fig|7227.3.peg.5848.
Organism-specific databases
CTD	36897.
FlyBase	FBgn0004784. inaC.
Phylogenomic databases
eggNOG	inNOG09369.
GeneTree	EMGT00050000001097.
InParanoid	P13677.
OMA	MELPMNE.
OrthoDB	EOG4P8D02.
PhylomeDB	P13677.
Gene expression databases
ArrayExpress	P13677.
Bgee	P13677.
GermOnline	CG6518. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR020477. C2_dom. IPR018029. C2_membr_targeting. IPR020454. DAG/PE-bd. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR014375. Protein_kinase_C_a/b/g. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K02677.
Pfam	PF00130. C1_1. 2 hits. PF00168. C2. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000550. PKC_alpha. 1 hit.
PRINTS	PR00360. C2DOMAIN. PR00008. DAGPEDOMAIN.
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF56112. Kinase_like. 1 hit.
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...
Other
NextBio	800933.

Entry information

Entry name

KPC2_DROME

Accession

Primary (citable) accession number: P13677
Secondary accession number(s): Q9V7V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project