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 16-OCT-2019, entry version 157. DE RecName: Full=MORN repeat-containing protein 4 homolog; DE AltName: Full=Retinophilin {ECO:0000244|FlyBase:FBgn0087005}; DE AltName: Full=undertaker {ECO:0000303|PubMed:22496551}; GN Name=rtp {ECO:0000244|FlyBase:FBgn0087005}; GN Synonyms=morn4, uta {ECO:0000303|PubMed:22496551}; ORFNames=CG10233; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic 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., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., 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 RP DISRUPTION 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., RA Elsaesser R., Li H.S., Montell C.; RT "Dependence on a retinophilin/myosin complex for stability of PKC and RT INAD 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 RT repeat-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). CC Organizes rhabdomeric components to suppress random activation of CC the phototransduction cascade and thus increases the signaling CC fidelity of dark-adapted photoreceptors (PubMed:20107052). The CC rtp/ninaC complex is required for stability of inad and inac and CC the normal termination of phototransduction in the retina CC (PubMed:20739554). {ECO:0000269|PubMed:20107052, CC ECO:0000269|PubMed:20739554, 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 CC phototransducing compartment of photoreceptor cells, the CC rhabdomeres and its expression is dependent on ninaC protein (at CC protein level). {ECO:0000269|PubMed:17285308, CC ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:25822849}. CC -!- PTM: phosphorylated under dark conditions and is dephosphorylated CC by light exposure. {ECO:0000269|PubMed:20107052}. CC -!- DISRUPTION PHENOTYPE: Severed rtp null axons show significantly CC reduced and delayed axonal degeneration following axotomy whereas CC wild-type axons degenerate within the first 24 hrs CC (PubMed:22496551). Rtp-null mutant flies exhibit age-dependent CC impairment in the termination of phototransduction in the retina CC (PubMed:20739554). Photoreceptors show a conspicuously high level CC 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; 2. DR STRING; 7227.FBpp0078467; -. DR iPTMnet; Q9VN91; -. DR PaxDb; Q9VN91; -. DR PRIDE; Q9VN91; -. 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 eggNOG; KOG0231; Eukaryota. DR eggNOG; COG4642; LUCA. DR GeneTree; ENSGT00940000168493; -. DR InParanoid; Q9VN91; -. DR OMA; FWRSDGM; -. DR OrthoDB; 1532474at2759; -. DR PhylomeDB; Q9VN91; -. DR GenomeRNAi; 40627; -. DR PRO; PR:Q9VN91; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0087005; Expressed in 21 organ(s), highest expression level in head. 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:1901555; P:response to paclitaxel; 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; Complete proteome; Membrane; Phosphoprotein; KW Reference proteome; Repeat; Sensory transduction; Vision. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20107052}. FT CHAIN 2 198 MORN repeat-containing protein 4 homolog. FT /FTId=PRO_0000441656. FT REPEAT 64 87 MORN 1. {ECO:0000255}. FT REPEAT 88 109 MORN 2. {ECO:0000255}. FT REPEAT 111 132 MORN 3. {ECO:0000255}. FT REPEAT 134 153 MORN 4. {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {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 //