ID MORN4_DROME Reviewed; 198 AA. AC Q9VN91; DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-FEB-2022, entry version 165. DE RecName: Full=MORN repeat-containing protein 4 homolog; DE AltName: Full=Retinophilin {ECO:0000312|FlyBase:FBgn0087005}; DE AltName: Full=undertaker {ECO:0000303|PubMed:22496551}; GN Name=rtp {ECO:0000312|FlyBase:FBgn0087005}; GN Synonyms=morn4, uta {ECO:0000303|PubMed:22496551}; ORFNames=CG10233; 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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY. RX PubMed=17285308; DOI=10.1007/s00438-007-0211-7; RA Mecklenburg K.L.; RT "Drosophila retinophilin contains MORN repeats and is conserved in RT humans."; RL Mol. Genet. Genomics 277:481-489(2007). 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 {ECO:0000269|PubMed:12537569}; RC TISSUE=Head {ECO:0000269|PubMed:12537569}; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT ALA-2, RP PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=20107052; DOI=10.1523/jneurosci.4464-09.2010; RA Mecklenburg K.L., Takemori N., Komori N., Chu B., Hardie R.C., RA Matsumoto H., O'Tousa J.E.; RT "Retinophilin is a light-regulated phosphoprotein required to suppress RT photoreceptor dark noise in Drosophila."; RL J. Neurosci. 30:1238-1249(2010). RN [6] RP FUNCTION, INTERACTION WITH NINAC, DISRUPTION PHENOTYPE, AND TISSUE RP SPECIFICITY. RX PubMed=20739554; DOI=10.1523/jneurosci.2709-10.2010; RA Venkatachalam K., Wasserman D., Wang X., Li R., Mills E., Elsaesser R., RA Li H.S., Montell C.; RT "Dependence on a retinophilin/myosin complex for stability of PKC and INAD RT and termination of phototransduction."; RL J. Neurosci. 30:11337-11345(2010). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22496551; DOI=10.1523/jneurosci.4951-11.2012; RA Bhattacharya M.R., Gerdts J., Naylor S.A., Royse E.X., Ebstein S.Y., RA Sasaki Y., Milbrandt J., DiAntonio A.; RT "A model of toxic neuropathy in Drosophila reveals a role for MORN4 in RT promoting axonal degeneration."; RL J. Neurosci. 32:5054-5061(2012). RN [8] RP SUBCELLULAR LOCATION, INTERACTION WITH NINAC, AND TISSUE SPECIFICITY. RX PubMed=25822849; DOI=10.1371/journal.pone.0122502; RA Mecklenburg K.L., Freed S.A., Raval M., Quintero O.A., Yengo C.M., RA O'Tousa J.E.; RT "Invertebrate and vertebrate class III myosins interact with MORN repeat- RT containing adaptor proteins."; RL PLoS ONE 10:E0122502-E0122502(2015). CC -!- FUNCTION: Plays a role in promoting axonal degeneration following CC neuronal injury by toxic insult or trauma (PubMed:22496551). Organizes CC rhabdomeric components to suppress random activation of the CC phototransduction cascade and thus increases the signaling fidelity of CC dark-adapted photoreceptors (PubMed:20107052). The rtp/ninaC complex is CC required for stability of inad and inac and the normal termination of CC phototransduction in the retina (PubMed:20739554). CC {ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:20739554, CC ECO:0000269|PubMed:22496551}. CC -!- SUBUNIT: Interacts with ninaC. {ECO:0000269|PubMed:25822849}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20107052, CC ECO:0000269|PubMed:25822849}. Note=Co-localizes with ninaC in the CC rhabdomere membrane. {ECO:0000269|PubMed:20107052, CC ECO:0000269|PubMed:25822849}. CC -!- TISSUE SPECIFICITY: Retina. Expressed primarily in the phototransducing CC compartment of photoreceptor cells, the rhabdomeres and its expression CC is dependent on ninaC protein (at protein level). CC {ECO:0000269|PubMed:17285308, ECO:0000269|PubMed:20107052, CC ECO:0000269|PubMed:25822849}. CC -!- PTM: phosphorylated under dark conditions and is dephosphorylated by CC light exposure. {ECO:0000269|PubMed:20107052}. CC -!- DISRUPTION PHENOTYPE: Severed rtp null axons show significantly reduced CC and delayed axonal degeneration following axotomy whereas wild-type CC axons degenerate within the first 24 hrs (PubMed:22496551). Rtp-null CC mutant flies exhibit age-dependent impairment in the termination of CC phototransduction in the retina (PubMed:20739554). Photoreceptors show CC a conspicuously high level of spontaneous dark noise (PubMed:20107052). CC {ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:20739554, CC ECO:0000269|PubMed:22496551}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ333317; ABC61052.1; -; Genomic_DNA. DR EMBL; DQ324736; ABC74791.1; -; mRNA. DR EMBL; AE014297; AAF52057.1; -; Genomic_DNA. DR EMBL; AY060630; AAL28178.1; -; mRNA. DR RefSeq; NP_649520.1; NM_141263.3. DR SMR; Q9VN91; -. DR IntAct; Q9VN91; 12. DR STRING; 7227.FBpp0078467; -. DR iPTMnet; Q9VN91; -. DR PaxDb; Q9VN91; -. DR PRIDE; Q9VN91; -. DR DNASU; 40627; -. DR EnsemblMetazoa; FBtr0078825; FBpp0078467; FBgn0087005. DR GeneID; 40627; -. DR KEGG; dme:Dmel_CG10233; -. DR UCSC; CG10233-RA; d. melanogaster. DR CTD; 107997; -. DR FlyBase; FBgn0087005; rtp. DR VEuPathDB; VectorBase:FBgn0087005; -. DR eggNOG; KOG0231; Eukaryota. DR GeneTree; ENSGT00940000168493; -. DR HOGENOM; CLU_113346_0_0_1; -. DR InParanoid; Q9VN91; -. DR OMA; WFPDGAK; -. DR OrthoDB; 1532474at2759; -. DR PhylomeDB; Q9VN91; -. DR BioGRID-ORCS; 40627; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 40627; -. DR PRO; PR:Q9VN91; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0087005; Expressed in head and 27 other tissues. DR ExpressionAtlas; Q9VN91; baseline and differential. DR GO; GO:0016028; C:rhabdomere; IDA:UniProtKB. DR GO; GO:0033583; C:rhabdomere membrane; IDA:UniProtKB. DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB. DR GO; GO:0048678; P:response to axon injury; IMP:UniProtKB. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR InterPro; IPR003409; MORN. DR Pfam; PF02493; MORN; 4. DR SMART; SM00698; MORN; 4. PE 1: Evidence at protein level; KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Repeat; KW Sensory transduction; Vision. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:20107052" FT CHAIN 2..198 FT /note="MORN repeat-containing protein 4 homolog" FT /id="PRO_0000441656" FT REPEAT 64..87 FT /note="MORN 1" FT /evidence="ECO:0000255" FT REPEAT 88..109 FT /note="MORN 2" FT /evidence="ECO:0000255" FT REPEAT 111..132 FT /note="MORN 3" FT /evidence="ECO:0000255" FT REPEAT 134..153 FT /note="MORN 4" FT /evidence="ECO:0000255" FT REGION 23..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:20107052" SQ SEQUENCE 198 AA; 22739 MW; DA2FBD3F026083DB CRC64; MAMDDYDDDM SSVGVTTARI ENQHQQHPHQ QGQHGHHQQG QGQSQYSAGA VKVGGWRYED ASRYIGEWNQ RGQKHGIGHL QFADGTRYDG QFQEGLSQGV GCLWFADGAK YEGEFHQGWF HGNGIFWRAD GMKYEGEFRG GKIWGLGLLT FQDFTHGFPR NEGFFQDCRF MRRRRCPEVV QRAQKCALMA RSQCEHPY //