GRND_DROME
ID GRND_DROME Reviewed; 241 AA.
AC Q9VJ83; Q8SXT4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein grindelwald {ECO:0000303|PubMed:25874673};
DE Flags: Precursor;
GN Name=grnd {ECO:0000303|PubMed:25874673};
GN ORFNames=CG10176 {ECO:0000312|FlyBase:FBgn0032682};
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:AAL89884.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL89884.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL89884.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EGR; TRAF6 AND VELI, AND SUBCELLULAR LOCATION.
RX PubMed=25874673; DOI=10.1038/nature14298;
RA Andersen D.S., Colombani J., Palmerini V., Chakrabandhu K., Boone E.,
RA Roethlisberger M., Toggweiler J., Basler K., Mapelli M., Hueber A.O.,
RA Leopold P.;
RT "The Drosophila TNF receptor Grindelwald couples loss of cell polarity and
RT neoplastic growth.";
RL Nature 522:482-486(2015).
CC -!- FUNCTION: Acts as a receptor for egr. Plays a role in activation of JNK
CC signaling and is required for egr-induced apoptosis. May also play an
CC egr-independent role in cell proliferation.
CC {ECO:0000269|PubMed:25874673}.
CC -!- SUBUNIT: Interacts with egr, Traf6/TRAF2 and veli (via PDZ domain).
CC {ECO:0000269|PubMed:25874673}.
CC -!- INTERACTION:
CC Q9VJ83; Q8MUJ1: egr; NbExp=4; IntAct=EBI-164007, EBI-108054;
CC Q9VJ83; Q9W3I9: Traf6; NbExp=2; IntAct=EBI-164007, EBI-88690;
CC Q9VJ83; Q9VBY7: veli; NbExp=3; IntAct=EBI-164007, EBI-91754;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:25874673}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The name 'grindelwald' comes from the village at the
CC foot of the Eiger mountain in Switzerland after which the egr gene is
CC named. {ECO:0000303|PubMed:25874673}.
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DR EMBL; AE014134; AAF53671.2; -; Genomic_DNA.
DR EMBL; AE014134; AGB93073.1; -; Genomic_DNA.
DR EMBL; AY084146; AAL89884.1; -; mRNA.
DR RefSeq; NP_001260538.1; NM_001273609.1.
DR RefSeq; NP_609880.2; NM_136036.4.
DR PDB; 6ZSY; X-ray; 0.93 A; A=30-81.
DR PDB; 6ZSZ; X-ray; 1.92 A; A=30-81.
DR PDB; 6ZT0; X-ray; 2.02 A; AAAA=30-81.
DR PDBsum; 6ZSY; -.
DR PDBsum; 6ZSZ; -.
DR PDBsum; 6ZT0; -.
DR AlphaFoldDB; Q9VJ83; -.
DR SMR; Q9VJ83; -.
DR DIP; DIP-61584N; -.
DR IntAct; Q9VJ83; 5.
DR STRING; 7227.FBpp0304599; -.
DR GlyGen; Q9VJ83; 1 site.
DR PaxDb; Q9VJ83; -.
DR PRIDE; Q9VJ83; -.
DR DNASU; 35103; -.
DR EnsemblMetazoa; FBtr0300674; FBpp0289898; FBgn0032682.
DR EnsemblMetazoa; FBtr0332321; FBpp0304599; FBgn0032682.
DR GeneID; 35103; -.
DR KEGG; dme:Dmel_CG10176; -.
DR UCSC; CG10176-RA; d. melanogaster.
DR CTD; 35103; -.
DR FlyBase; FBgn0032682; grnd.
DR VEuPathDB; VectorBase:FBgn0032682; -.
DR eggNOG; ENOG502SE1N; Eukaryota.
DR HOGENOM; CLU_1166904_0_0_1; -.
DR InParanoid; Q9VJ83; -.
DR OMA; NRCFQKL; -.
DR OrthoDB; 1619350at2759; -.
DR PhylomeDB; Q9VJ83; -.
DR BioGRID-ORCS; 35103; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35103; -.
DR PRO; PR:Q9VJ83; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032682; Expressed in wing disc and 34 other tissues.
DR Genevisible; Q9VJ83; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IDA:FlyBase.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:FlyBase.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..241
FT /note="Protein grindelwald"
FT /id="PRO_0000434595"
FT TOPO_DOM 28..98
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6ZSY"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6ZSY"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6ZSY"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6ZSY"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6ZSY"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:6ZSY"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:6ZSY"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6ZSY"
SQ SEQUENCE 241 AA; 26267 MW; 4FE090B07514ACC7 CRC64;
MSVRKLSALS LSIGGVPLIP SVSLVAAANG ESRDCHGTIC HPVNEFCYVA TERCHPCIEV
CNNQTHNYDA FLCAKECSAY KTFEPLKAEM LDIQNTQQLI LLLLTILLVL IALRCAFQFL
RWLIGNRCFQ KLMRRLQSKA YPHPATANGK DLNATTIQNL NAINHPGSDL ERAQSQIYSV
AGAAEGSVVT MTTPVSTRYP AENSTTPTTV MTEIGYGYDN QAMVVTPVSE KPSAATIPVA
F
