DROME:KPC2

Species (Taxon ID)	Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s)	inaC (synonyms: PKC2)
Protein Name(s)	Protein kinase C, eye isozyme Eye-PKC Inactivation no after-potential C protein Protein INAC Photoreceptor-specific PKC dPKC53E(EY)
External Links
UniProt	P13677
EMBL	J04845 AE013599 BT004495
PIR	A32392
RefSeq	NP_476863.1
UniGene	Dm.4688
ProteinModelPortal	P13677
SMR	P13677
BioGrid	62602
DIP	DIP-54N
IntAct	P13677
MINT	MINT-922757
STRING	7227.FBpp0086196
PaxDb	P13677
PRIDE	P13677
EnsemblMetazoa	FBtr0087047
GeneID	36897
KEGG	dme:Dmel_CG6518
CTD	36897
FlyBase	FBgn0004784
eggNOG	COG0515
GeneTree	ENSGT00770000120449
InParanoid	P13677
KO	K02677
OMA	MELPMNE
OrthoDB	EOG77M8QM
PhylomeDB	P13677
Reactome	REACT_180303 REACT_180649 REACT_181313 REACT_184300 REACT_184321 REACT_209150 REACT_210687 REACT_211983 REACT_219169 REACT_237476 REACT_254810 REACT_259532 REACT_261064 REACT_263519 REACT_271456
SignaLink	P13677
GenomeRNAi	36897
NextBio	800933
Proteomes	UP000000803
Bgee	P13677
GO	GO:0016027 GO:0005886 GO:0016028 GO:0005524 GO:0004697 GO:0004674 GO:0008270 GO:0016062 GO:0019722 GO:0016477 GO:0016059 GO:0050962 GO:0008585 GO:0006909 GO:0030845 GO:0007602 GO:0006468 GO:0045471 GO:0009416 GO:0007601
Gene3D	2.60.40.150
InterPro	IPR000961 IPR000008 IPR020454 IPR011009 IPR002219 IPR017892 IPR000719 IPR017441 IPR014375 IPR002290 IPR008271
Pfam	PF00130 PF00168 PF00069 PF00433
PIRSF	PIRSF000550
PRINTS	PR00360 PR00008
SMART	SM00109 SM00239 SM00133 SM00220
SUPFAM	SSF49562 SSF56112
PROSITE	PS51285 PS50004 PS00107 PS50011 PS00108 PS00479 PS50081

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:9651370^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q24008	P	Seeded From UniProt	complete
	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:9651370^[1]	ECO:0000316		UniProtKB:Q24008	P	Figure 7	complete CACAO 10118
involved_in	GO:0035556	intracellular signal transduction	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003744 FB:FBgn0010379 MGI:MGI:97601 PANTHER:PTN000683254 PomBase:SPAC1B9.02c PomBase:SPAC22E12.14c PomBase:SPAPB18E9.02c RGD:3395 RGD:3399 RGD:61925 RGD:620968 RGD:67383 SGD:S000000201 UniProtKB:O15530 UniProtKB:P31749 UniProtKB:Q15208 UniProtKB:Q9NRM7 UniProtKB:Q9Y2H1	P	Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:87986 PANTHER:PTN000683254 RGD:2081 RGD:3395 RGD:3399 RGD:3668 RGD:61925 SGD:S000001609 SGD:S000001861 SGD:S000002898 SGD:S000005460 UniProtKB:A0A1D5PUY5 UniProtKB:P31749 UniProtKB:P41743 UniProtKB:Q02156 UniProtKB:Q05513 UniProtKB:Q05655 WB:WBGene00000102 WB:WBGene00000103 WB:WBGene00004033 WB:WBGene00004034 WB:WBGene00004789 WB:WBGene00006599	P	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003091 FB:FBgn0003744 FB:FBgn0010379 FB:FBgn0260399 FB:FBgn0261854 MGI:MGI:104874 MGI:MGI:2182368 MGI:MGI:87986 MGI:MGI:894676 MGI:MGI:97595 MGI:MGI:97596 MGI:MGI:97599 MGI:MGI:97602 PANTHER:PTN000683254 PomBase:SPAC1B9.02c PomBase:SPAC22E12.14c PomBase:SPAC24B11.11c PomBase:SPAC821.12 PomBase:SPAPB18E9.02c PomBase:SPCC576.15c RGD:2081 RGD:2082 RGD:3399 RGD:3668 RGD:620146 RGD:620968 RGD:62390 SGD:S000001248 SGD:S000001609 SGD:S000001861 SGD:S000002898 SGD:S000003324 SGD:S000005105 SGD:S000005460 SGD:S000006315 TAIR:locus:2088515 UniProtKB:O15530 UniProtKB:O95835 UniProtKB:P05771 UniProtKB:P17252 UniProtKB:P31749 UniProtKB:P31751 UniProtKB:P41743 UniProtKB:Q02156 UniProtKB:Q04759 UniProtKB:Q05513 UniProtKB:Q05655 UniProtKB:Q09013 UniProtKB:Q15208 UniProtKB:Q16512 UniProtKB:Q16513 UniProtKB:Q96GX5 UniProtKB:Q9NRM7 UniProtKB:Q9XF67 UniProtKB:Q9Y243 UniProtKB:Q9Y2H1 WB:WBGene00000102 WB:WBGene00000103 WB:WBGene00004034 WB:WBGene00004789 WB:WBGene00006599 dictyBase:DDB_G0268620	F	Seeded From UniProt	complete
involved_in	GO:2000370	positive regulation of clathrin-dependent endocytosis	PMID:25639794^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0003091	P	Seeded From UniProt	complete
colocalizes_with	GO:0005768	endosome	PMID:25639794^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045471	response to ethanol	PMID:18675322^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009416	response to light stimulus	PMID:18256265^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0050962	detection of light stimulus involved in sensory perception	PMID:16914683^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016028	rhabdomere	PMID:16301334^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0030845	phospholipase C-inhibiting G protein-coupled receptor signaling pathway	PMID:16005297^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016477	cell migration	PMID:11970894^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008585	female gonad development	PMID:11970894^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:10908587^[10]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:10908587^[10]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:10611962^[11]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016059	deactivation of rhodopsin mediated signaling	PMID:8510756^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:8510756^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:1962207^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016028	rhabdomere	PMID:1962207^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016059	deactivation of rhodopsin mediated signaling	PMID:1962207^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007602	phototransduction	PMID:1962207^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0003218	P	Seeded From UniProt	complete
involved_in	GO:0016059	deactivation of rhodopsin mediated signaling	PMID:1961249^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016062	adaptation of rhodopsin mediated signaling	PMID:1961249^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004697	protein kinase C activity	PMID:2720775^[15]	ECO:0000250	sequence similarity evidence used in manual assertion	protein_id:AAA41871.1	F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000961 InterPro:IPR017892	F	Seeded From UniProt	complete
enables	GO:0004697	protein kinase C activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014375	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR000961 InterPro:IPR014375 InterPro:IPR017441 InterPro:IPR017892	F	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR000961 InterPro:IPR008271 InterPro:IPR014375 InterPro:IPR017892	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014375	F	Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002219	P	Seeded From UniProt	complete
enables	GO:0004697	protein kinase C activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.13	F	Seeded From UniProt	complete
part_of	GO:0016027	inaD signaling complex	PMID:12765677^[16] PMID:10611962^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016059	deactivation of rhodopsin mediated signaling	PMID:11707492^[17] PMID:10611962^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019722	calcium-mediated signaling	PMID:10611962^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0050896	response to stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0716	P	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
involved_in	GO:0007601	visual perception	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0844	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Adamski, FM et al. (1998) Interaction of eye protein kinase C and INAD in Drosophila. Localization of binding domains and electrophysiological characterization of a loss of association in transgenic flies. J. Biol. Chem. 273 17713-9 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 Lee, KA et al. (2015) Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via Hedgehog-induced signaling endosomes. Cell Host Microbe 17 191-204 PubMed GONUTS page
↑ Chen, J et al. (2008) A protein kinase C activity localized to neuropeptide Y-like neurons mediates ethanol intoxication in Drosophila melanogaster. Neuroscience 156 42-7 PubMed GONUTS page
↑ Wang, N et al. (2008) Role of protein phosphatase 2A in regulating the visual signaling in Drosophila. J. Neurosci. 28 1444-51 PubMed GONUTS page
↑ Popescu, DC et al. (2006) Scaffolding protein INAD regulates deactivation of vision by promoting phosphorylation of transient receptor potential by eye protein kinase C in Drosophila. J. Neurosci. 26 8570-7 PubMed GONUTS page
↑ Wang, T et al. (2005) Dissecting independent channel and scaffolding roles of the Drosophila transient receptor potential channel. J. Cell Biol. 171 685-94 PubMed GONUTS page
↑ Gu, Y et al. (2005) Mechanisms of light adaptation in Drosophila photoreceptors. Curr. Biol. 15 1228-34 PubMed GONUTS page
↑ ^9.0 ^9.1 Cohen, ED et al. (2002) DWnt4 regulates cell movement and focal adhesion kinase during Drosophila ovarian morphogenesis. Dev. Cell 2 437-48 PubMed GONUTS page
↑ ^10.0 ^10.1 Morrison, DK et al. (2000) Protein kinases and phosphatases in the Drosophila genome. J. Cell Biol. 150 F57-62 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Montell, C (1999) Visual transduction in Drosophila. Annu. Rev. Cell Dev. Biol. 15 231-68 PubMed GONUTS page
↑ ^12.0 ^12.1 Hardie, RC et al. (1993) Protein kinase C is required for light adaptation in Drosophila photoreceptors. Nature 363 634-7 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Smith, DP et al. (1991) Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C. Science 254 1478-84 PubMed GONUTS page
↑ ^14.0 ^14.1 Ranganathan, R et al. (1991) A Drosophila mutant defective in extracellular calcium-dependent photoreceptor deactivation and rapid desensitization. Nature 354 230-2 PubMed GONUTS page
↑ Schaeffer, E et al. (1989) Isolation and characterization of two new drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells. Cell 57 403-12 PubMed GONUTS page
↑ Harteneck, C () Proteins modulating TRP channel function. Cell Calcium 33 303-10 PubMed GONUTS page
↑ Hardie, RC (2001) Phototransduction in Drosophila melanogaster. J. Exp. Biol. 204 3403-9 PubMed GONUTS page

[PMID:9651370-1] 1.0 ^1.1 Adamski, FM et al. (1998) Interaction of eye protein kinase C and INAD in Drosophila. Localization of binding domains and electrophysiological characterization of a loss of association in transgenic flies. J. Biol. Chem. 273 17713-9 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25639794-3] 3.0 ^3.1 Lee, KA et al. (2015) Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via Hedgehog-induced signaling endosomes. Cell Host Microbe 17 191-204 PubMed GONUTS page

[PMID:18675322-4] Chen, J et al. (2008) A protein kinase C activity localized to neuropeptide Y-like neurons mediates ethanol intoxication in Drosophila melanogaster. Neuroscience 156 42-7 PubMed GONUTS page

[PMID:18256265-5] Wang, N et al. (2008) Role of protein phosphatase 2A in regulating the visual signaling in Drosophila. J. Neurosci. 28 1444-51 PubMed GONUTS page

[PMID:16914683-6] Popescu, DC et al. (2006) Scaffolding protein INAD regulates deactivation of vision by promoting phosphorylation of transient receptor potential by eye protein kinase C in Drosophila. J. Neurosci. 26 8570-7 PubMed GONUTS page

[PMID:16301334-7] Wang, T et al. (2005) Dissecting independent channel and scaffolding roles of the Drosophila transient receptor potential channel. J. Cell Biol. 171 685-94 PubMed GONUTS page

[PMID:16005297-8] Gu, Y et al. (2005) Mechanisms of light adaptation in Drosophila photoreceptors. Curr. Biol. 15 1228-34 PubMed GONUTS page

[PMID:11970894-9] 9.0 ^9.1 Cohen, ED et al. (2002) DWnt4 regulates cell movement and focal adhesion kinase during Drosophila ovarian morphogenesis. Dev. Cell 2 437-48 PubMed GONUTS page

[PMID:10908587-10] 10.0 ^10.1 Morrison, DK et al. (2000) Protein kinases and phosphatases in the Drosophila genome. J. Cell Biol. 150 F57-62 PubMed GONUTS page

[PMID:10611962-11] 11.0 ^11.1 ^11.2 ^11.3 Montell, C (1999) Visual transduction in Drosophila. Annu. Rev. Cell Dev. Biol. 15 231-68 PubMed GONUTS page

[PMID:8510756-12] 12.0 ^12.1 Hardie, RC et al. (1993) Protein kinase C is required for light adaptation in Drosophila photoreceptors. Nature 363 634-7 PubMed GONUTS page

[PMID:1962207-13] 13.0 ^13.1 ^13.2 ^13.3 Smith, DP et al. (1991) Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C. Science 254 1478-84 PubMed GONUTS page

[PMID:1961249-14] 14.0 ^14.1 Ranganathan, R et al. (1991) A Drosophila mutant defective in extracellular calcium-dependent photoreceptor deactivation and rapid desensitization. Nature 354 230-2 PubMed GONUTS page

[PMID:2720775-15] Schaeffer, E et al. (1989) Isolation and characterization of two new drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells. Cell 57 403-12 PubMed GONUTS page

[PMID:12765677-16] Harteneck, C () Proteins modulating TRP channel function. Cell Calcium 33 303-10 PubMed GONUTS page

[PMID:11707492-17] Hardie, RC (2001) Phototransduction in Drosophila melanogaster. J. Exp. Biol. 204 3403-9 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

DROME:KPC2

Contents

Annotations

Notes

References

a

b

c

d

e

f

h

i

k

m

n

o

p

r

s

t

v

z

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools