MORN4_DROME
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 03-AUG-2022, entry version 167.
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}.
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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 AlphaFoldDB; Q9VN91; -.
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 capsule and 15 other tissues.
DR ExpressionAtlas; Q9VN91; baseline and differential.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
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
