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   28-MAR-2018, entry version 146.
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}.
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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   UniGene; Dm.9865; -.
DR   SMR; Q9VN91; -.
DR   IntAct; Q9VN91; 6.
DR   STRING; 7227.FBpp0078467; -.
DR   PaxDb; 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; ENSGT00730000111173; -.
DR   OMA; HGVPRNE; -.
DR   OrthoDB; EOG091G0WNQ; -.
DR   GenomeRNAi; 40627; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0087005; -.
DR   ExpressionAtlas; Q9VN91; 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: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
//