ID RIG_DROME Reviewed; 1235 AA.
AC Q86BY9; Q86P78; Q9V957;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Protein rigor mortis;
GN Name=rig; ORFNames=CG30149;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ECR; SVP; USP; HR39 AND HR46.
RX PubMed=14645129; DOI=10.1242/dev.00920;
RA Gates J., Lam G., Ortiz J.A., Losson R., Thummel C.S.;
RT "rigor mortis encodes a novel nuclear receptor interacting protein required
RT for ecdysone signaling during Drosophila larval development.";
RL Development 131:25-36(2004).
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; TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-290; SER-351;
RP SER-354; THR-355; SER-357 AND THR-411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20452345; DOI=10.1016/j.yexcr.2010.05.001;
RA Cauchi R.J., Sanchez-Pulido L., Liu J.L.;
RT "Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components
RT of U bodies.";
RL Exp. Cell Res. 316:2354-2364(2010).
CC -!- FUNCTION: Nuclear receptor cofactor for the ecdysone-regulated
CC processes of molting and puparium formation. Acts downstream from
CC ecdysone biosynthesis and release to control the expression of specific
CC ecdysone-regulated genes such as Eip74EF (E74).
CC {ECO:0000269|PubMed:14645129}.
CC -!- SUBUNIT: Interacts with nuclear receptors EcR, svp (seven up), usp
CC (ultraspiracle), Hr39 and Hr3. {ECO:0000269|PubMed:14645129}.
CC -!- INTERACTION:
CC Q86BY9; Q05192: Hr39; NbExp=2; IntAct=EBI-422757, EBI-75048;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=During second and third
CC instar larval development, it is localized primarily to the cytoplasm
CC of cells in the brain and imaginal disks (tissues that are fated to
CC form specific parts of the adult fly during metamorphosis). Also
CC localized to the cytoplasm of larval salivary gland cells during the
CC second and early third instar stages. It however, begins to shift into
CC the nucleus of these cells in the mid-third instar maintaining this
CC localization through the end of larval development. At puparium
CC formation, it shuttles out of the nucleus of salivary gland cells to
CC become more abundant in the cytoplasm. A similar dynamic movement
CC occurs in cells of the larval midgut during third instar development.
CC Component of U bodies.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and salivary glands of early
CC and late second instar larvae. Expressed in nurse cells and oocytes.
CC {ECO:0000269|PubMed:14645129, ECO:0000269|PubMed:20452345}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which is
CC usually essential for the association with nuclear receptors.
CC {ECO:0000250}.
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DR EMBL; AY274835; AAP31582.1; -; mRNA.
DR EMBL; AE013599; AAF57440.3; -; Genomic_DNA.
DR EMBL; BT003437; AAO39440.1; -; mRNA.
DR RefSeq; NP_611499.3; NM_137655.3.
DR AlphaFoldDB; Q86BY9; -.
DR BioGRID; 62984; 7.
DR ComplexPortal; CPX-8008; Survival motor neuron complex, Gem4A variant.
DR ComplexPortal; CPX-8066; Survival motor neuron complex, Gem4B variant.
DR ComplexPortal; CPX-8067; Survival motor neuron complex, Gem4C variant.
DR IntAct; Q86BY9; 6.
DR STRING; 7227.FBpp0085564; -.
DR iPTMnet; Q86BY9; -.
DR PaxDb; 7227-FBpp0085564; -.
DR EnsemblMetazoa; FBtr0086252; FBpp0085564; FBgn0250850.
DR GeneID; 37335; -.
DR KEGG; dme:Dmel_CG30149; -.
DR AGR; FB:FBgn0250850; -.
DR CTD; 37335; -.
DR FlyBase; FBgn0250850; rig.
DR VEuPathDB; VectorBase:FBgn0250850; -.
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_279538_0_0_1; -.
DR InParanoid; Q86BY9; -.
DR OMA; DVSPMWG; -.
DR OrthoDB; 2954862at2759; -.
DR PhylomeDB; Q86BY9; -.
DR SignaLink; Q86BY9; -.
DR BioGRID-ORCS; 37335; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37335; -.
DR PRO; PR:Q86BY9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0250850; Expressed in ovary and 13 other cell types or tissues.
DR Genevisible; Q86BY9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071254; C:cytoplasmic U snRNP body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0007591; P:molting cycle, chitin-based cuticle; IMP:UniProtKB.
DR GO; GO:0035075; P:response to ecdysone; IMP:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:FlyBase.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR46362; GEM-ASSOCIATED PROTEIN 5; 1.
DR PANTHER; PTHR46362:SF1; GEM-ASSOCIATED PROTEIN 5; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 3.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat.
FT CHAIN 1..1235
FT /note="Protein rigor mortis"
FT /id="PRO_0000051199"
FT REPEAT 55..102
FT /note="WD 1"
FT REPEAT 430..469
FT /note="WD 2"
FT REPEAT 475..512
FT /note="WD 3"
FT REPEAT 565..605
FT /note="WD 4"
FT REPEAT 611..650
FT /note="WD 5"
FT REPEAT 690..730
FT /note="WD 6"
FT REPEAT 739..779
FT /note="WD 7"
FT REPEAT 788..828
FT /note="WD 8"
FT REGION 227..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 443..447
FT /note="LXXLL motif"
FT COMPBIAS 238..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 119
FT /note="H -> N (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> V (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="E -> D (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="V -> L (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="D -> E (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="E -> K (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="S -> T (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="S -> T (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="R -> K (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="P -> S (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="T -> S (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="S -> T (in Ref. 4; AAO39440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1235 AA; 137829 MW; 015E185A6941F451 CRC64;
MNSQVMYHNV PTPPGNVSLA AAAPDGGLLY AGIRCINYIS APPANGEQPQ VVTMSTRINI
LALDVSPMWG LGNGGPTKPF AIVGDDLSVQ VWDCALGEAV IGHKAHQHQH EARDVRVVHH
TTNSVLMSYL ANGNILSMDA SDLVIYCVAS NTYCRRSTFI SPRNHQLTMV RCSPYNDNLF
AVGTAMGNVL VCDLRKMNIV YKFHGHKAPI CGLAWREVPA AEDEKTNNLA LSAEEWRSRN
GGQEEKPKTK PPPLTKSKAA ESDDPFDIYN FDHLEYEFGA PIAERRRKSS EDCGGEFVGL
EKPAGAAVLD FVEACESVKA ELLASRQEDK TQHVEVTLHD CEPTKPTGPL SDASTISNKN
DASDSTEGSL EVIQYSSSSD DAVIVDGEAA KPKREVLHHI YHQAEVHASG TPQTKSEPQS
NLQVVPAISA ETISLTSVNS THLETLLVSI DGDEVMMIWN TNTGAHAGKN YSKSKTAGKL
NNVYWLNNHV IVSLSRHQLF FWSVEFERKM LRYKISKDKS HSCHLQDIVS FACDSSKEMI
WLCRNNRQIG MMNPKTGRMA DFYGTVAFGV RAMAECPDDM NKIALGCSDR RVAFFDISKL
TTSCLPIDSV YVSSNVYCLA WSPNCLELAF GTFDGTVGIL DVERMKVKTH LRTPHKKEVY
SLVWQDHFIY FIVNRVLGFF DLRKSKIEPT IVNCISRPSY LSIRDSFLFV GTDDGLLQIH
ERDSGMEKSW SPFIRQSALF ARYVTDIAWC PLDSNKFAVS GNDRSVYVME FQPTERNWKT
LHTFTANTEK ASITSMRWSH TQKHLLLTFH IEGKVCLWNC NAPEKPPLTI TYHCPMWCGM
FLPTNENIIM CSGKALSVEL IDIKDALEGD EKSICPKVDA LLNVKWASKS LTQPYAPVLT
AAEKKRQRRD QRKAAAKLEV DVANKDQKKI QESVTAVIDN PTNDKCTQET PVEEMLEALS
LDKEQNNRSA KECPKCKEQS PDSFTHSRTC LYLTQKELNK SALEKLAIVL TEDSAKIDKS
VLISKLFSSK VMAKELIATE LTNLKHSNTK DIAPLCLAMS TFKLREELEQ HIANKTLTER
HVSLAPSVSF TLWQDCCRAY AKQMEEKGYI MHAATYLFSQ GMQSEAIKLF LANEYYKEAL
VHARICLPAT DPLIKTVINN WLEHLEGTGN FAAAALICVL DNEMLRGYSY LRKYRNCTPE
IADLMDQIKR IGQLGGVLDG CAPNEPIHNG STAEH
//
