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MORN repeat-containing protein 4 homolog (Retinophilin) (undertaker)

 MORN4_DROME             Reviewed;         198 AA.
Q9VN91;
27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
10-OCT-2018, entry version 151.
RecName: Full=MORN repeat-containing protein 4 homolog;
AltName: Full=Retinophilin {ECO:0000244|FlyBase:FBgn0087005};
AltName: Full=undertaker {ECO:0000303|PubMed:22496551};
Name=rtp {ECO:0000244|FlyBase:FBgn0087005};
Synonyms=morn4, uta {ECO:0000303|PubMed:22496551}; ORFNames=CG10233;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=17285308; DOI=10.1007/s00438-007-0211-7;
Mecklenburg K.L.;
"Drosophila retinophilin contains MORN repeats and is conserved in
humans.";
Mol. Genet. Genomics 277:481-489(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Head {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT ALA-2,
PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=20107052; DOI=10.1523/JNEUROSCI.4464-09.2010;
Mecklenburg K.L., Takemori N., Komori N., Chu B., Hardie R.C.,
Matsumoto H., O'Tousa J.E.;
"Retinophilin is a light-regulated phosphoprotein required to suppress
photoreceptor dark noise in Drosophila.";
J. Neurosci. 30:1238-1249(2010).
[6]
FUNCTION, INTERACTION WITH NINAC, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=20739554; DOI=10.1523/JNEUROSCI.2709-10.2010;
Venkatachalam K., Wasserman D., Wang X., Li R., Mills E.,
Elsaesser R., Li H.S., Montell C.;
"Dependence on a retinophilin/myosin complex for stability of PKC and
INAD and termination of phototransduction.";
J. Neurosci. 30:11337-11345(2010).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22496551; DOI=10.1523/JNEUROSCI.4951-11.2012;
Bhattacharya M.R., Gerdts J., Naylor S.A., Royse E.X., Ebstein S.Y.,
Sasaki Y., Milbrandt J., DiAntonio A.;
"A model of toxic neuropathy in Drosophila reveals a role for MORN4 in
promoting axonal degeneration.";
J. Neurosci. 32:5054-5061(2012).
[8]
SUBCELLULAR LOCATION, INTERACTION WITH NINAC, AND TISSUE SPECIFICITY.
PubMed=25822849; DOI=10.1371/journal.pone.0122502;
Mecklenburg K.L., Freed S.A., Raval M., Quintero O.A., Yengo C.M.,
O'Tousa J.E.;
"Invertebrate and vertebrate class III myosins interact with MORN
repeat-containing adaptor proteins.";
PLoS ONE 10:E0122502-E0122502(2015).
-!- FUNCTION: Plays a role in promoting axonal degeneration following
neuronal injury by toxic insult or trauma (PubMed:22496551).
Organizes rhabdomeric components to suppress random activation of
the phototransduction cascade and thus increases the signaling
fidelity of dark-adapted photoreceptors (PubMed:20107052). The
rtp/ninaC complex is required for stability of inad and inac and
the normal termination of phototransduction in the retina
(PubMed:20739554). {ECO:0000269|PubMed:20107052,
ECO:0000269|PubMed:20739554, ECO:0000269|PubMed:22496551}.
-!- SUBUNIT: Interacts with ninaC. {ECO:0000269|PubMed:25822849}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20107052,
ECO:0000269|PubMed:25822849}. Note=Co-localizes with ninaC in the
rhabdomere membrane. {ECO:0000269|PubMed:20107052,
ECO:0000269|PubMed:25822849}.
-!- TISSUE SPECIFICITY: Retina. Expressed primarily in the
phototransducing compartment of photoreceptor cells, the
rhabdomeres and its expression is dependent on ninaC protein (at
protein level). {ECO:0000269|PubMed:17285308,
ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:25822849}.
-!- PTM: phosphorylated under dark conditions and is dephosphorylated
by light exposure. {ECO:0000269|PubMed:20107052}.
-!- DISRUPTION PHENOTYPE: Severed rtp null axons show significantly
reduced and delayed axonal degeneration following axotomy whereas
wild-type axons degenerate within the first 24 hrs
(PubMed:22496551). Rtp-null mutant flies exhibit age-dependent
impairment in the termination of phototransduction in the retina
(PubMed:20739554). Photoreceptors show a conspicuously high level
of spontaneous dark noise (PubMed:20107052).
{ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:20739554,
ECO:0000269|PubMed:22496551}.
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EMBL; DQ333317; ABC61052.1; -; Genomic_DNA.
EMBL; DQ324736; ABC74791.1; -; mRNA.
EMBL; AE014297; AAF52057.1; -; Genomic_DNA.
EMBL; AY060630; AAL28178.1; -; mRNA.
RefSeq; NP_649520.1; NM_141263.3.
UniGene; Dm.9865; -.
ProteinModelPortal; Q9VN91; -.
SMR; Q9VN91; -.
IntAct; Q9VN91; 2.
STRING; 7227.FBpp0078467; -.
PaxDb; Q9VN91; -.
PRIDE; Q9VN91; -.
EnsemblMetazoa; FBtr0078825; FBpp0078467; FBgn0087005.
GeneID; 40627; -.
KEGG; dme:Dmel_CG10233; -.
UCSC; CG10233-RA; d. melanogaster.
CTD; 107997; -.
FlyBase; FBgn0087005; rtp.
eggNOG; KOG0231; Eukaryota.
eggNOG; COG4642; LUCA.
GeneTree; ENSGT00730000111173; -.
InParanoid; Q9VN91; -.
OMA; HGVPRNE; -.
OrthoDB; EOG091G0WNQ; -.
PhylomeDB; Q9VN91; -.
GenomeRNAi; 40627; -.
PRO; PR:Q9VN91; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0087005; Expressed in 21 organ(s), highest expression level in head.
ExpressionAtlas; Q9VN91; baseline and differential.
GO; GO:0016028; C:rhabdomere; IDA:UniProtKB.
GO; GO:0033583; C:rhabdomere membrane; IDA:UniProtKB.
GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
GO; GO:0048678; P:response to axon injury; IMP:UniProtKB.
GO; GO:1901555; P:response to paclitaxel; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR003409; MORN.
Pfam; PF02493; MORN; 4.
SMART; SM00698; MORN; 4.
1: Evidence at protein level;
Acetylation; Complete proteome; Membrane; Phosphoprotein;
Reference proteome; Repeat; Sensory transduction; Vision.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20107052}.
CHAIN 2 198 MORN repeat-containing protein 4 homolog.
/FTId=PRO_0000441656.
REPEAT 64 87 MORN 1. {ECO:0000255}.
REPEAT 88 109 MORN 2. {ECO:0000255}.
REPEAT 111 132 MORN 3. {ECO:0000255}.
REPEAT 134 153 MORN 4. {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:20107052}.
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


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