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Protein

Protein kinase C, eye isozyme

Gene

inaC

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei400 – 4001ATPPROSITE-ProRule annotation
Active sitei495 – 4951Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri71 – 12151Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri136 – 18651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi377 – 3859ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein kinase C activity Source: FlyBase
  • protein kinase C activity Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • adaptation of rhodopsin mediated signaling Source: CACAO
  • calcium-mediated signaling Source: FlyBase
  • cell migration Source: FlyBase
  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • detection of light stimulus involved in sensory perception Source: FlyBase
  • female gonad development Source: FlyBase
  • phagocytosis Source: FlyBase
  • phospholipase C-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  • phototransduction Source: FlyBase
  • positive regulation of clathrin-mediated endocytosis Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • response to ethanol Source: FlyBase
  • response to light stimulus Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-111933. Calmodulin induced events.
R-DME-114516. Disinhibition of SNARE formation.
R-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1433559. Regulation of KIT signaling.
R-DME-2179392. EGFR Transactivation by Gastrin.
R-DME-3000170. Syndecan interactions.
R-DME-399997. Acetylcholine regulates insulin secretion.
R-DME-416993. Trafficking of GluR2-containing AMPA receptors.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.
R-DME-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-DME-5218921. VEGFR2 mediated cell proliferation.
R-DME-76005. Response to elevated platelet cytosolic Ca2+.
SignaLinkiP13677.

Names & Taxonomyi

Protein namesi
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 namesi
Name:inaC
Synonyms:PKC2
ORF Names:CG6518
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004784. inaC.

Subcellular locationi

GO - Cellular componenti

  • inaD signaling complex Source: FlyBase
  • intracellular Source: GOC
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi697 – 6971I → E: No interaction with inaD. 1 Publication
Mutagenesisi697 – 6971I → K: 90% reduced interaction with inaD. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700Protein kinase C, eye isozymePRO_0000055731Add
BLAST

Proteomic databases

PaxDbiP13677.
PRIDEiP13677.

Expressioni

Tissue specificityi

Exclusively expressed in photoreceptor cells.1 Publication

Developmental stagei

Expression primarily in adults.1 Publication

Gene expression databases

BgeeiP13677.
GenevisibleiP13677. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
inaDQ240082EBI-130595,EBI-195326

Protein-protein interaction databases

BioGridi62602. 5 interactions.
DIPiDIP-54N.
IntActiP13677. 5 interactions.
MINTiMINT-922757.
STRINGi7227.FBpp0086196.

Structurei

3D structure databases

ProteinModelPortaliP13677.
SMRiP13677. Positions 70-697.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 29590C2PROSITE-ProRule annotationAdd
BLAST
Domaini371 – 629259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini630 – 70071AGC-kinase C-terminalAdd
BLAST

Domaini

Tetrapeptide ligand at C-terminus is tethered to inaD by interaction with the second PDZ domain.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri71 – 12151Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri136 – 18651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0696. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
InParanoidiP13677.
KOiK02677.
OMAiPNNRLGA.
OrthoDBiEOG77M8QM.
PhylomeDBiP13677.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequencei

Sequence statusi: Complete.

P13677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAVATPG ATVLPPSVPS AAPGAKAPAA GAGKGPGNLL EITGEANIVN
60 70 80 90 100
YMKNRLRKGA MKRKGLEMVN GHRFGVRFFK NPTYCGHCKD FIWGFGKQGF
110 120 130 140 150
QCEECRFNIH QKCCKFVVFK CPGKDTDFDA DCAKVKHGWI STTYTTPTFC
160 170 180 190 200
DECGLLLHGV AHQGVKCENC NLNVHHACQE TVPPMCGADI SEVRGKLLLY
210 220 230 240 250
VELKGNNLKV DIKEAANLIP MDTNGFSDPY IAVQMHPDRS GRTKKKTKTI
260 270 280 290 300
QKNLNPVFNE TFTFELQPQD RDKRLLIEVW DWDRTSRNDF MGSFSFSLEE
310 320 330 340 350
LQKEPVDGWY KFLSQVEGEH YNIPCVDAFN DIARLRDEVR HDRRPNEKRR
360 370 380 390 400
MDNKDMPHNM SKRDMIRAAD FNFVKVIGKG SFGKVLLAER RGTDELYAVK
410 420 430 440 450
VLRKDVIIQT DDMELPMNEK KILALSGRPP FLVSMHSCFQ TMDRLFFVME
460 470 480 490 500
YCKGGDLMYH MQQYGRFKES VAIFYAVEVA IALFFLHERD IIYRDLKLDN
510 520 530 540 550
ILLDGEGHVK LVDFGLSKEG VTERQTTRTF CGTPNYMAPE IVSYDPYSIA
560 570 580 590 600
ADWWSFGVLL FEFMAGQAPF EGDDETTVFR NIKDKKAVFP KHFSVEAMDI
610 620 630 640 650
ITSFLTKKPN NRLGAGRYAR QEITTHPFFR NVDWDKAEAC EMEPPIKPMI
660 670 680 690 700
KHRKDISNFD DAFTKEKTDL TPTDKLFMMN LDQNDFIGFS FMNPEFITII
Length:700
Mass (Da):79,844
Last modified:April 1, 1990 - v1
Checksum:i41B6BFF7FF3F6F8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04845 mRNA. Translation: AAA28817.1.
AE013599 Genomic DNA. Translation: AAF57934.1.
BT004495 mRNA. Translation: AAO42659.1.
PIRiA32392.
RefSeqiNP_476863.1. NM_057515.3.
UniGeneiDm.4688.

Genome annotation databases

EnsemblMetazoaiFBtr0087047; FBpp0086196; FBgn0004784.
GeneIDi36897.
KEGGidme:Dmel_CG6518.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04845 mRNA. Translation: AAA28817.1.
AE013599 Genomic DNA. Translation: AAF57934.1.
BT004495 mRNA. Translation: AAO42659.1.
PIRiA32392.
RefSeqiNP_476863.1. NM_057515.3.
UniGeneiDm.4688.

3D structure databases

ProteinModelPortaliP13677.
SMRiP13677. Positions 70-697.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62602. 5 interactions.
DIPiDIP-54N.
IntActiP13677. 5 interactions.
MINTiMINT-922757.
STRINGi7227.FBpp0086196.

Proteomic databases

PaxDbiP13677.
PRIDEiP13677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087047; FBpp0086196; FBgn0004784.
GeneIDi36897.
KEGGidme:Dmel_CG6518.

Organism-specific databases

CTDi36897.
FlyBaseiFBgn0004784. inaC.

Phylogenomic databases

eggNOGiKOG0696. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
InParanoidiP13677.
KOiK02677.
OMAiPNNRLGA.
OrthoDBiEOG77M8QM.
PhylomeDBiP13677.

Enzyme and pathway databases

ReactomeiR-DME-111933. Calmodulin induced events.
R-DME-114516. Disinhibition of SNARE formation.
R-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1433559. Regulation of KIT signaling.
R-DME-2179392. EGFR Transactivation by Gastrin.
R-DME-3000170. Syndecan interactions.
R-DME-399997. Acetylcholine regulates insulin secretion.
R-DME-416993. Trafficking of GluR2-containing AMPA receptors.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.
R-DME-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-DME-5218921. VEGFR2 mediated cell proliferation.
R-DME-76005. Response to elevated platelet cytosolic Ca2+.
SignaLinkiP13677.

Miscellaneous databases

GenomeRNAii36897.
PROiP13677.

Gene expression databases

BgeeiP13677.
GenevisibleiP13677. DM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-697, INTERACTION WITH INAD.

Entry informationi

Entry nameiKPC2_DROME
AccessioniPrimary (citable) accession number: P13677
Secondary accession number(s): Q9V7V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.