RENR_DROME
ID RENR_DROME Reviewed; 320 AA.
AC Q9VHG4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATPase H(+)-transporting accessory protein 2 {ECO:0000303|PubMed:29127204, ECO:0000312|FlyBase:FBgn0037671};
DE AltName: Full=Renin homolog receptor {ECO:0000305};
DE Short=dPRR {ECO:0000303|PubMed:20579879, ECO:0000312|FlyBase:FBgn0037671};
DE Contains:
DE RecName: Full=ATPase H(+)-transporting accessory protein 2 N-terminal fragment {ECO:0000303|PubMed:23292348};
DE Contains:
DE RecName: Full=ATPase H(+)-transporting accessory protein 2 C-terminal fragment {ECO:0000303|PubMed:23292348};
DE Flags: Precursor;
GN Name=ATP6AP2 {ECO:0000303|PubMed:29127204,
GN ECO:0000312|FlyBase:FBgn0037671};
GN Synonyms=VhaM8-9 {ECO:0000312|FlyBase:FBgn0037671},
GN VhaM8.9 {ECO:0000312|FlyBase:FBgn0037671},
GN VhaPRR {ECO:0000303|PubMed:20579879, ECO:0000312|FlyBase:FBgn0037671};
GN ORFNames=CG8444 {ECO:0000312|FlyBase:FBgn0037671};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAK93214.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93214.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAK93214.1};
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FZ AND FZ2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20579883; DOI=10.1016/j.cub.2010.05.028;
RA Buechling T., Bartscherer K., Ohkawara B., Chaudhary V., Spirohn K.,
RA Niehrs C., Boutros M.;
RT "Wnt/Frizzled signaling requires dPRR, the Drosophila homolog of the
RT prorenin receptor.";
RL Curr. Biol. 20:1263-1268(2010).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20579879; DOI=10.1016/j.cub.2010.05.057;
RA Hermle T., Saltukoglu D., Gruenewald J., Walz G., Simons M.;
RT "Regulation of Frizzled-dependent planar polarity signaling by a V-ATPase
RT subunit.";
RL Curr. Biol. 20:1269-1276(2010).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH STAN, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ARG-248 AND ARG-251.
RX PubMed=23292348; DOI=10.1038/emboj.2012.323;
RA Hermle T., Guida M.C., Beck S., Helmstaedter S., Simons M.;
RT "Drosophila ATP6AP2/VhaPRR functions both as a novel planar cell polarity
RT core protein and a regulator of endosomal trafficking.";
RL EMBO J. 32:245-259(2013).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26376863; DOI=10.1093/hmg/ddv380;
RA Dubos A., Castells-Nobau A., Meziane H., Oortveld M.A., Houbaert X.,
RA Iacono G., Martin C., Mittelhaeuser C., Lalanne V., Kramer J.M., Bhukel A.,
RA Quentin C., Slabbert J., Verstreken P., Sigrist S.J., Messaddeq N.,
RA Birling M.C., Selloum M., Stunnenberg H.G., Humeau Y., Schenck A.,
RA Herault Y.;
RT "Conditional depletion of intellectual disability and Parkinsonism
RT candidate gene ATP6AP2 in fly and mouse induces cognitive impairment and
RT neurodegeneration.";
RL Hum. Mol. Genet. 24:6736-6755(2015).
RN [8] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MOTIF, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF LEU-98; 316-LYS--ASN-320; ARG-248 AND ARG-251.
RX PubMed=29127204; DOI=10.1084/jem.20170453;
RA Rujano M.A., Cannata Serio M., Panasyuk G., Peanne R., Reunert J.,
RA Rymen D., Hauser V., Park J.H., Freisinger P., Souche E., Guida M.C.,
RA Maier E.M., Wada Y., Jaeger S., Krogan N.J., Kretz O., Nobre S., Garcia P.,
RA Quelhas D., Bird T.D., Raskind W.H., Schwake M., Duvet S., Foulquier F.,
RA Matthijs G., Marquardt T., Simons M.;
RT "Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with
RT autophagic defects.";
RL J. Exp. Med. 214:3707-3729(2017).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH VHAAC45, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, MOTIF, AND MUTAGENESIS OF 299-ALA--ASN-320 AND 317-LYS--ASN-320.
RX PubMed=29995586; DOI=10.1091/mbc.e18-04-0234;
RA Guida M.C., Hermle T., Graham L.A., Hauser V., Ryan M., Stevens T.H.,
RA Simons M.;
RT "ATP6AP2 functions as a V-ATPase assembly factor in the endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 29:2156-2164(2018).
CC -!- FUNCTION: Multifunctional protein which functions as transmembrane
CC receptor in the planar cell polarity (PCP) and is involved in the
CC assembly of the proton-transporting vacuolar (V)-ATPase protein pump
CC (PubMed:20579883, PubMed:20579879, PubMed:29127204, PubMed:29995586).
CC As transmembrane receptor mediates fz/PCP signaling through interaction
CC with fz and stabilizes asymmetric PCP domains through its interaction
CC with stan (PubMed:20579883, PubMed:20579879, PubMed:23292348,
CC PubMed:29995586). Also mediates Wnt/beta-cat signaling through
CC interaction with fz/fz2 (PubMed:20579883, PubMed:20579879). Probably by
CC controlling the assembly of the V-ATPase pump and thus the
CC acidification of the endo-lysosomal system, plays a role in many
CC neuronal processes including synapse morphology and synaptic
CC transmission (PubMed:26376863). {ECO:0000269|PubMed:20579879,
CC ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348,
CC ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:29127204,
CC ECO:0000269|PubMed:29995586}.
CC -!- FUNCTION: [ATPase H(+)-transporting accessory protein 2 N-terminal
CC fragment]: Stabilizes asymmetric Planar Cell Polarity (PCP) domains
CC through its interaction with stan. {ECO:0000269|PubMed:23292348}.
CC -!- SUBUNIT: Interacts with fz and fz2 (PubMed:20579883). Interacts (via N-
CC terminus) with stan (PubMed:23292348). As an accessory component of the
CC multisubunit proton-transporting vacuolar (V)-ATPase protein pump,
CC might interacts with VhaAC45 (PubMed:29995586).
CC {ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348,
CC ECO:0000269|PubMed:29995586}.
CC -!- SUBCELLULAR LOCATION: [ATPase H(+)-transporting accessory protein 2]:
CC Cell membrane {ECO:0000269|PubMed:20579879,
CC ECO:0000269|PubMed:20579883}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20579883}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348,
CC ECO:0000269|PubMed:29995586}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20579883}. Vesicle {ECO:0000269|PubMed:23292348}.
CC Apical cell membrane {ECO:0000269|PubMed:23292348}; Single-pass type I
CC membrane protein {ECO:0000269|PubMed:23292348}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:29995586}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:29995586}. Note=Co-localizes at the apical
CC junctions with stan. {ECO:0000269|PubMed:23292348}.
CC -!- SUBCELLULAR LOCATION: [ATPase H(+)-transporting accessory protein 2 N-
CC terminal fragment]: Secreted {ECO:0000269|PubMed:23292348}.
CC Note=Localization to the planar cell polarity domains depends by stan.
CC {ECO:0000269|PubMed:23292348}.
CC -!- DEVELOPMENTAL STAGE: Expressed in whole larval extracts, fat body and
CC larval brain (PubMed:29127204). At prepupal stages, expressed towards
CC the wing margin; during the junctional remodeling phase relocalizes to
CC intracellular compartments; before prehair formation, enriched at P-D
CC membranes (at protein level) (PubMed:23292348).
CC {ECO:0000269|PubMed:23292348, ECO:0000269|PubMed:29127204}.
CC -!- PTM: Proteolytically cleaved by a furin-like convertase in the trans-
CC Golgi network to generate N- and C-terminal fragments (PubMed:23292348,
CC PubMed:29127204). Cleavage is reduced in the fat body
CC (PubMed:29127204). {ECO:0000269|PubMed:23292348,
CC ECO:0000269|PubMed:29127204}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is lethal
CC (PubMed:20579883). RNAi-mediated knockdown in the wings results in
CC increased apoptosis, endoplasmic reticulum stress and lipid
CC accumulation (PubMed:20579883, PubMed:20579879, PubMed:29127204,
CC PubMed:29995586). This is accompanied by severe growth defects
CC including venation defects, defective wing-hair polarity (as a result
CC of defective fz and stan trafficking) and wg signaling
CC (PubMed:20579883, PubMed:20579879, PubMed:29127204, PubMed:29995586).
CC RNAi-mediated knockdown in the notum causes severe planar polarity
CC defects affecting orientation morphology and number of sensory bristles
CC or microchaetae (PubMed:20579879). RNAi-mediated knockdown in the eye
CC results in defective phototaxis and presynaptic transmission in
CC vacuolated photoreceptor neurons and pigment cells (PubMed:26376863).
CC RNAi-mediated knockdown in neurons leads to defective autophagy and
CC neurodegeneration, impaired synapse morphology, ultrastructural
CC organization and axonal transport of the active zone component brp,
CC ultimately resulting in lethality at different developmental stages
CC (PubMed:26376863). The few adult survivors show strongly reduced
CC spontaneous movements and poor climbing abilities (PubMed:26376863).
CC RNAi-mediated knockdown in the mushroom body results in altered
CC short- and long-term memory (PubMed:26376863). RNAi-mediated knockdown
CC in the fat body results in increased autophagy (PubMed:29127204).
CC {ECO:0000269|PubMed:20579879, ECO:0000269|PubMed:20579883,
CC ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:29127204,
CC ECO:0000269|PubMed:29995586}.
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DR EMBL; AE014297; AAF54350.1; -; Genomic_DNA.
DR EMBL; AY051790; AAK93214.1; -; mRNA.
DR RefSeq; NP_649876.1; NM_141619.3.
DR AlphaFoldDB; Q9VHG4; -.
DR SMR; Q9VHG4; -.
DR STRING; 7227.FBpp0081458; -.
DR PaxDb; Q9VHG4; -.
DR PRIDE; Q9VHG4; -.
DR DNASU; 41104; -.
DR EnsemblMetazoa; FBtr0081978; FBpp0081458; FBgn0037671.
DR GeneID; 41104; -.
DR KEGG; dme:Dmel_CG8444; -.
DR UCSC; CG8444-RA; d. melanogaster.
DR CTD; 10159; -.
DR FlyBase; FBgn0037671; ATP6AP2.
DR VEuPathDB; VectorBase:FBgn0037671; -.
DR eggNOG; KOG4737; Eukaryota.
DR GeneTree; ENSGT00390000008856; -.
DR HOGENOM; CLU_065819_0_0_1; -.
DR InParanoid; Q9VHG4; -.
DR OMA; CDINFEQ; -.
DR OrthoDB; 1179410at2759; -.
DR PhylomeDB; Q9VHG4; -.
DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VHG4; -.
DR BioGRID-ORCS; 41104; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41104; -.
DR PRO; PR:Q9VHG4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037671; Expressed in adult hindgut (Drosophila) and 46 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IMP:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IDA:FlyBase.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0098930; P:axonal transport; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
DR GO; GO:0048104; P:establishment of body hair or bristle planar orientation; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0042331; P:phototaxis; IMP:FlyBase.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IGI:UniProtKB.
DR InterPro; IPR012493; Renin_rcpt.
DR PANTHER; PTHR13351; PTHR13351; 1.
DR Pfam; PF07850; Renin_r; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..320
FT /note="ATPase H(+)-transporting accessory protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5015100291"
FT CHAIN 18..248
FT /note="ATPase H(+)-transporting accessory protein 2 N-
FT terminal fragment"
FT /evidence="ECO:0000269|PubMed:23292348"
FT /id="PRO_0000447860"
FT CHAIN 252..320
FT /note="ATPase H(+)-transporting accessory protein 2 C-
FT terminal fragment"
FT /evidence="ECO:0000269|PubMed:23292348"
FT /id="PRO_0000447861"
FT TOPO_DOM 18..277
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 317..320
FT /note="Mediates retrograde transport to the ER"
FT /evidence="ECO:0000269|PubMed:29127204,
FT ECO:0000269|PubMed:29995586"
FT SITE 248..249
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000269|PubMed:23292348,
FT ECO:0000269|PubMed:29127204"
FT SITE 251..252
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000269|PubMed:23292348,
FT ECO:0000269|PubMed:29127204"
FT MUTAGEN 98
FT /note="L->S: Reduces protein stability and increases N-
FT glycosylation levels of proteins which targets the
FT misfolded protein to degradation. Impairs autophagy and
FT mTOR signaling. Reduces eclosion rate with few adult
FT escapers showing poor mobility, decreased or absent
FT climbing capabilities, blistered winds and reduced size and
FT death within 3-4 days. In the brain, results in neural
FT development defects in the optic lobe. In the fat body,
FT increases lipid droplets size and total triglycerides."
FT /evidence="ECO:0000269|PubMed:29127204"
FT MUTAGEN 248
FT /note="R->A: Prevents cleavage; when associated with A-
FT 251."
FT /evidence="ECO:0000269|PubMed:23292348,
FT ECO:0000269|PubMed:29127204"
FT MUTAGEN 251
FT /note="R->A: Prevents cleavage; when associated with A-
FT 248."
FT /evidence="ECO:0000269|PubMed:23292348,
FT ECO:0000269|PubMed:29127204"
FT MUTAGEN 299..320
FT /note="Missing: Lethal in the late larval stage with few
FT adult escapers showing poor mobility, decreased or absent
FT climbing capabilities, blistered wings, reduced head size
FT and death within 3-4 days after eclosion. Impairs
FT localization to the endoplasmic reticulum, enhances
FT cleavage and protein stability."
FT /evidence="ECO:0000269|PubMed:29127204,
FT ECO:0000269|PubMed:29995586"
FT MUTAGEN 317..320
FT /note="Missing: Survive till late pupal stage. Impairs
FT localization to the endoplasmic reticulum and autophagy
FT degradation. In the fat body, increases lipid droplets size
FT and total triglycerides."
FT /evidence="ECO:0000269|PubMed:29127204,
FT ECO:0000269|PubMed:29995586"
SQ SEQUENCE 320 AA; 34421 MW; 401BCEAAA4FBA7E5 CRC64;
MLRVFVIFSL FIAAINASGE FTVLNRPKAI SFKGNDALES HYVGDVLYAS MGNAVSGDTN
WNGLTINDPF NLAKGVILVH VQGIGHVTTA GNVKTYELTG SGTDASLNAL AAELEAANEP
VCDINFEQFD DGVQAWKSCF GDFEAPAAKP TKHLNPSLHT ADKQFLQEVG FINSAADHLA
EMAKPSNVLM LRVSVDGVAK AHGEKSVAVE EANKLLSAAI SRLLAASQKS SDSVLFVQTT
EKDVAASRAK RDTIAASTTN PYNLAVYYGS DYPVIFNIIL WFMVVFGLSL LAICYAIAAM
DPGRDSIIYR MTSTRIKKDN
