RIC1_DROME
ID RIC1_DROME Reviewed; 1429 AA.
AC Q9V3C5; M9PG00;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Guanine nucleotide exchange factor subunit Rich {ECO:0000305};
DE AltName: Full=Protein RIC1 homolog {ECO:0000250|UniProtKB:P40395};
GN Name=Rich; ORFNames=CG9063;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1207; SER-1391 AND SER-1394,
RP AND IDENTIFICATION BY MASS 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 [5]
RP FUNCTION, INTERACTION WITH RAB6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=21835342; DOI=10.1016/j.neuron.2011.06.040;
RA Tong C., Ohyama T., Tien A.C., Rajan A., Haueter C.M., Bellen H.J.;
RT "Rich regulates target specificity of photoreceptor cells and N-cadherin
RT trafficking in the Drosophila visual system via Rab6.";
RL Neuron 71:447-459(2011).
CC -!- FUNCTION: Probable component of a guanine nucleotide exchange factor
CC (GEF) that may be required for efficient fusion of endosome-derived
CC vesicles with the Golgi (By similarity). Plays a role in regulating
CC Rab6-dependent CadN transport in photoreceptor cells which is required
CC for the formation of normal synaptic connections between axons from the
CC inner photoreceptor cells in the eye and postsynaptic cells in the
CC brain medulla layer M6, and for the generation of normal postsynaptic
CC responses. {ECO:0000250|UniProtKB:Q4ADV7, ECO:0000269|PubMed:21835342}.
CC -!- SUBUNIT: Component of a guanine nucleotide exchange factor (GEF)
CC complex (By similarity). Interacts with Rab6.
CC {ECO:0000250|UniProtKB:Q4ADV7, ECO:0000269|PubMed:21835342}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21835342}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21835342}. Note=Colocalizes with Rab6 at the Golgi
CC apparatus.
CC -!- TISSUE SPECIFICITY: In third-instar larvae, detected in most cells of
CC the optic lobes, showing an enrichment in the lamina and the medulla
CC neuropil. At pupal stage, expressed in photoreceptor cells, as well as
CC in the postsynaptic cells that form the lamina plexus and medulla. Also
CC expressed in salivary glands and pupal eye imaginal disks.
CC {ECO:0000269|PubMed:21835342}.
CC -!- DISRUPTION PHENOTYPE: In mutant flies, axons from R7 photoreceptor
CC cells in the eye fail to reach their normal target in brain medulla
CC layer M6, but instead target layer M3. This leads to defects in
CC synaptic signal transmission. Differentiation of photoreceptors is not
CC affected. {ECO:0000269|PubMed:21835342}.
CC -!- SIMILARITY: Belongs to the RIC1 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF51813.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94898.1; -; Genomic_DNA.
DR EMBL; AF181626; AAD55412.1; -; mRNA.
DR RefSeq; NP_001262205.1; NM_001275276.1.
DR RefSeq; NP_649385.1; NM_141128.3.
DR AlphaFoldDB; Q9V3C5; -.
DR BioGRID; 65693; 3.
DR IntAct; Q9V3C5; 2.
DR STRING; 7227.FBpp0078164; -.
DR iPTMnet; Q9V3C5; -.
DR PaxDb; Q9V3C5; -.
DR PRIDE; Q9V3C5; -.
DR EnsemblMetazoa; FBtr0078512; FBpp0078164; FBgn0028500.
DR EnsemblMetazoa; FBtr0334751; FBpp0306792; FBgn0028500.
DR GeneID; 40456; -.
DR KEGG; dme:Dmel_CG9063; -.
DR UCSC; CG9063-RA; d. melanogaster.
DR CTD; 40456; -.
DR FlyBase; FBgn0028500; Rich.
DR VEuPathDB; VectorBase:FBgn0028500; -.
DR eggNOG; KOG2006; Eukaryota.
DR GeneTree; ENSGT00390000002955; -.
DR HOGENOM; CLU_002060_3_1_1; -.
DR InParanoid; Q9V3C5; -.
DR OMA; MVYDRAM; -.
DR OrthoDB; 261419at2759; -.
DR PhylomeDB; Q9V3C5; -.
DR BioGRID-ORCS; 40456; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40456; -.
DR PRO; PR:Q9V3C5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0028500; Expressed in eye disc (Drosophila) and 25 other tissues.
DR Genevisible; Q9V3C5; DM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:FlyBase.
DR GO; GO:0035418; P:protein localization to synapse; IMP:FlyBase.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:FlyBase.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IMP:FlyBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR009771; Ribosome_control_1.
DR InterPro; IPR040096; Ric1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22746; PTHR22746; 1.
DR Pfam; PF07064; RIC1; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; WD repeat.
FT CHAIN 1..1429
FT /note="Guanine nucleotide exchange factor subunit Rich"
FT /id="PRO_0000320664"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 17..55
FT /note="WD 1"
FT REPEAT 64..103
FT /note="WD 2"
FT REPEAT 312..351
FT /note="WD 3"
FT REPEAT 580..621
FT /note="WD 4"
FT REPEAT 862..906
FT /note="WD 5"
FT REGION 8..521
FT /note="Interaction with Rab6"
FT REGION 711..995
FT /note="Interaction with Rab6"
FT REGION 1020..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1429 AA; 159157 MW; EB36175730493335 CRC64;
MYYPVGWPKR VGLALPGESA SIRHICCDAV KILVAAVGDD FLGIWYANPL IPIAYFRRTE
DSLRQYGANQ LIVWKPDSRQ LALLTASGSL LLYQLDFEAN GMGILQQIDP PAASLKRDSA
ELFIKENIPR LSLRELCSVT LGSVITTVCC ISLSELLLAT QSCELLRLQW TELEHAENDL
ELPALSSIKL RDIPFYVQQQ PQQSARNVPP LNRDSYVASL EYSPFIGGCA AVFSDRRAAF
LIANHLRFET DHMHGFWVPD VEDASVCSVN HKFRLLAYGQ ESSAVKVYAI DDATGGLEFS
HRLILTENIL PDSLGSVNEL KWSPDGCVLA VSWTNGGLSL WSTFGALLMS TLSWDFGLNV
DLVCQNPLKI RRLEWSTEGY QLFMLKLHPE KDKSNVLQLQ FVKSALSMNP CMTTSPHILL
QGDDCLYLNQ GNNLELTYAG SHGTFPSSGL GSDEDISGDG DCLELKQSPH TGSILTESKY
WTVLQLPLNY AATNWPIRYA AIDPDGLHLA VAGRTGLAHY SLVTRRWKLF GNESQEKDFV
VSGGLLWWHG FVVMGCYSLL DRTDELRCYP ADCKLDNQYG HKLQVRAPVI SLNSFRHQLI
VLTADGIVSL FNMSKNSAYA LDIECAYELD VKSICIHPAC IVSLTVTNLK NELKPQGQLG
GDQAETIIVN VCGRILMIQR DAGEQVPNTL LATCLASCVE VFWLSHSLER CAMRDCLWLY
SGAHGMRVWL PILPPGRERR EGEQGGAQRL HSFMSKRIML SFPLKLYPLV VLFDNVIVLG
VENESTLYAN EQVSHFSLPF AVMERKSQIY LHKVLRQLIK RNLGYSAWEM AQSCCSLPYF
PHALELLLHE VLEEEATSKQ PIPDAQLPSI LDFIREFPVY LETIVQCARK TEIALWPYLF
SMAGKPKDLF QMCLQSEQLD TAASYLIILQ NLEPSVVSKQ YATMLLDIAL QQRKWELAKD
LIRFLKAIDP NEIDSPRSSM VVNVKIAPPP QVNTQQQVNQ NADAFNMVLG PIARERSFST
TVTSNLPKDK QASGTPGVAP VTESSSAGAP SVVRRRSTKQ RETFCIDLIL QRHARQLLQN
HKLMDLGYMC AYLDFHLVSW LSQESERAAK LDDFAGALQA LHEELDLPIP FPTAAKDDFA
QIRGSLRQTG GGGSSQTSES GYFSLATPNG AATQSPQLQP SIREEEEELQ QPSSLPILKT
RSGSQLSFDN FRYRRLYSLP TSEDDLAVDI LPQKLSIKLR YLLQLFIEAN CTDYALVLSI
LLQDAASISR IVNGIIRSES VHTCRRTESA LKQLSQSTFE HSGSLYRGFV LTLQPHVYLL
EQYIQSLGDA PCSQLQDAGP GTEQGVDVST GLQGLQNEVG EFVPNSQQAN GNQWTVADLN
PNHQRLTRHA SLESNGNAVV ASGSSAHSTP TQRQLSRQNS REREGCRLM
