KPC2_DROME
ID KPC2_DROME Reviewed; 700 AA.
AC P13677; Q9V7V5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Protein kinase C, eye isozyme;
DE EC=2.7.11.13;
DE AltName: Full=Eye-PKC;
DE AltName: Full=Inactivation no after-potential C protein;
DE Short=Protein INAC;
DE AltName: Full=Photoreceptor-specific PKC;
DE AltName: Full=dPKC53E(EY);
GN Name=inaC; Synonyms=PKC2; ORFNames=CG6518;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=2720775; DOI=10.1016/0092-8674(89)90915-x;
RA Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.;
RT "Isolation and characterization of two new Drosophila protein kinase C
RT genes, including one specifically expressed in photoreceptor cells.";
RL Cell 57:403-412(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP MUTAGENESIS OF ILE-697, AND INTERACTION WITH INAD.
RX PubMed=11342563; DOI=10.1074/jbc.m103570200;
RA Kumar R., Shieh B.-H.;
RT "The second PDZ domain of INAD is a type I domain involved in binding to
RT eye protein kinase C. Mutational analysis and naturally occurring
RT variants.";
RL J. Biol. Chem. 276:24971-24977(2001).
RN [6]
RP FUNCTION, AND INDUCTION BY BACTERIAL URACIL.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
CC -!- FUNCTION: This is a calcium-activated, phospholipid-dependent,
CC serine- and threonine-specific enzyme. This isozyme is a negative
CC regulator of the visual transduction cascade and has been shown to be
CC required for photoreceptor cell inactivation and light adaptation.
CC Negative regulation is dependent on interaction with scaffolding
CC protein inaD. Acts in a hh-signaling pathway which regulates the Duox-
CC dependent gut immune response to bacterial uracil; required for the
CC activation of Cad99C and consequently Cad99C-dependent endosome
CC formation, which is essential for the Duox-dependent production of
CC reactive oxygen species (ROS) in response to intestinal bacterial
CC infection (PubMed:25639794). {ECO:0000269|PubMed:25639794}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- INTERACTION:
CC P13677; Q24008: inaD; NbExp=2; IntAct=EBI-130595, EBI-195326;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in photoreceptor cells.
CC {ECO:0000269|PubMed:2720775}.
CC -!- DEVELOPMENTAL STAGE: Expression primarily in adults.
CC {ECO:0000269|PubMed:2720775}.
CC -!- INDUCTION: Up-regulated in the midgut epithelium in response to
CC bacterial uracil. {ECO:0000269|PubMed:25639794}.
CC -!- DOMAIN: Tetrapeptide ligand at C-terminus is tethered to inaD by
CC interaction with the second PDZ domain.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; J04845; AAA28817.1; -; mRNA.
DR EMBL; AE013599; AAF57934.1; -; Genomic_DNA.
DR EMBL; BT004495; AAO42659.1; -; mRNA.
DR PIR; A32392; A32392.
DR RefSeq; NP_476863.1; NM_057515.3.
DR AlphaFoldDB; P13677; -.
DR SMR; P13677; -.
DR BioGRID; 62602; 7.
DR DIP; DIP-54N; -.
DR IntAct; P13677; 6.
DR STRING; 7227.FBpp0086196; -.
DR PaxDb; P13677; -.
DR PRIDE; P13677; -.
DR DNASU; 36897; -.
DR EnsemblMetazoa; FBtr0087047; FBpp0086196; FBgn0004784.
DR GeneID; 36897; -.
DR KEGG; dme:Dmel_CG6518; -.
DR CTD; 36897; -.
DR FlyBase; FBgn0004784; inaC.
DR VEuPathDB; VectorBase:FBgn0004784; -.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000167637; -.
DR HOGENOM; CLU_000288_54_2_1; -.
DR InParanoid; P13677; -.
DR OMA; TTHPFFR; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; P13677; -.
DR Reactome; R-DME-111933; Calmodulin induced events.
DR Reactome; R-DME-114516; Disinhibition of SNARE formation.
DR Reactome; R-DME-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DME-76005; Response to elevated platelet cytosolic Ca2+.
DR SignaLink; P13677; -.
DR BioGRID-ORCS; 36897; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36897; -.
DR PRO; PR:P13677; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004784; Expressed in head capsule and 8 other tissues.
DR Genevisible; P13677; DM.
DR GO; GO:0016027; C:inaD signaling complex; TAS:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
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:0004697; F:protein kinase C activity; ISS:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0050962; P:detection of light stimulus involved in sensory perception; IMP:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0030845; P:phospholipase C-inhibiting G protein-coupled receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IGI:FlyBase.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IGI:FlyBase.
DR GO; GO:0045471; P:response to ethanol; IDA:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 2.
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; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
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; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
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; Calcium; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision; Zinc; Zinc-finger.
FT CHAIN 1..700
FT /note="Protein kinase C, eye isozyme"
FT /id="PRO_0000055731"
FT DOMAIN 189..310
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 371..629
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 630..700
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 71..121
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 136..186
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 495
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 377..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 697
FT /note="I->E: No interaction with inaD."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 697
FT /note="I->K: 90% reduced interaction with inaD."
FT /evidence="ECO:0000269|PubMed:11342563"
SQ SEQUENCE 700 AA; 79844 MW; 41B6BFF7FF3F6F8F CRC64;
MAAAAVATPG ATVLPPSVPS AAPGAKAPAA GAGKGPGNLL EITGEANIVN YMKNRLRKGA
MKRKGLEMVN GHRFGVRFFK NPTYCGHCKD FIWGFGKQGF QCEECRFNIH QKCCKFVVFK
CPGKDTDFDA DCAKVKHGWI STTYTTPTFC DECGLLLHGV AHQGVKCENC NLNVHHACQE
TVPPMCGADI SEVRGKLLLY VELKGNNLKV DIKEAANLIP MDTNGFSDPY IAVQMHPDRS
GRTKKKTKTI QKNLNPVFNE TFTFELQPQD RDKRLLIEVW DWDRTSRNDF MGSFSFSLEE
LQKEPVDGWY KFLSQVEGEH YNIPCVDAFN DIARLRDEVR HDRRPNEKRR MDNKDMPHNM
SKRDMIRAAD FNFVKVIGKG SFGKVLLAER RGTDELYAVK VLRKDVIIQT DDMELPMNEK
KILALSGRPP FLVSMHSCFQ TMDRLFFVME YCKGGDLMYH MQQYGRFKES VAIFYAVEVA
IALFFLHERD IIYRDLKLDN ILLDGEGHVK LVDFGLSKEG VTERQTTRTF CGTPNYMAPE
IVSYDPYSIA ADWWSFGVLL FEFMAGQAPF EGDDETTVFR NIKDKKAVFP KHFSVEAMDI
ITSFLTKKPN NRLGAGRYAR QEITTHPFFR NVDWDKAEAC EMEPPIKPMI KHRKDISNFD
DAFTKEKTDL TPTDKLFMMN LDQNDFIGFS FMNPEFITII
