ARRB_DROME
ID ARRB_DROME Reviewed; 401 AA.
AC P19107; Q9VSN6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Phosrestin-1;
DE AltName: Full=49 kDa arrestin-like protein;
DE AltName: Full=Arrestin-2;
DE AltName: Full=Arrestin-B;
DE AltName: Full=Phosrestin I;
GN Name=Arr2; Synonyms=ArrB; ORFNames=CG5962;
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 [GENOMIC DNA].
RX PubMed=2158671; DOI=10.1126/science.2158671;
RA Yamada T., Takeuchi Y., Kmoroi N., Kobayashi H., Sakai Y., Hotta Y.,
RA Matsumoto H.;
RT "A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an
RT arrestin homolog.";
RL Science 248:483-486(1990).
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 PHOSPHORYLATION, AND PROBABLE FUNCTION.
RX PubMed=1905538; DOI=10.1016/0006-291x(91)90683-x;
RA Matsumoto H., Yamada T.;
RT "Phosrestins I and II: arrestin homologs which undergo differential light-
RT induced phosphorylation in the Drosophila photoreceptor in vivo.";
RL Biochem. Biophys. Res. Commun. 177:1306-1312(1991).
RN [5]
RP PHOSPHORYLATION AT SER-366.
RX PubMed=8185954; DOI=10.1016/0896-6273(94)90309-3;
RA Matsumoto H., Kurien B.T., Takagi Y., Kahn E.S., Kinumi T., Komori N.,
RA Yamada T., Hayashi F., Isono K., Pak W.L.;
RT "Phosrestin I undergoes the earliest light-induced phosphorylation by a
RT calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors.";
RL Neuron 12:997-1010(1994).
CC -!- FUNCTION: Probably plays an important role in the photoreceptor
CC transduction.
CC -!- TISSUE SPECIFICITY: Inner and outer segments, and the inner plexiform
CC regions of the retina.
CC -!- PTM: Phosphorylated upon light exposure. {ECO:0000269|PubMed:1905538,
CC ECO:0000269|PubMed:8185954}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; M32141; AAA28833.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50380.1; -; Genomic_DNA.
DR PIR; A34856; A34856.
DR RefSeq; NP_523976.1; NM_079252.3.
DR AlphaFoldDB; P19107; -.
DR SMR; P19107; -.
DR BioGRID; 64400; 15.
DR DIP; DIP-20598N; -.
DR IntAct; P19107; 3.
DR MINT; P19107; -.
DR STRING; 7227.FBpp0076326; -.
DR iPTMnet; P19107; -.
DR PaxDb; P19107; -.
DR DNASU; 38993; -.
DR EnsemblMetazoa; FBtr0076599; FBpp0076326; FBgn0000121.
DR GeneID; 38993; -.
DR KEGG; dme:Dmel_CG5962; -.
DR CTD; 38993; -.
DR FlyBase; FBgn0000121; Arr2.
DR VEuPathDB; VectorBase:FBgn0000121; -.
DR eggNOG; KOG3865; Eukaryota.
DR HOGENOM; CLU_033484_1_1_1; -.
DR InParanoid; P19107; -.
DR OMA; QFYLVPL; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; P19107; -.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P19107; -.
DR BioGRID-ORCS; 38993; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Arr2; fly.
DR GenomeRNAi; 38993; -.
DR PRO; PR:P19107; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000121; Expressed in head capsule and 17 other tissues.
DR ExpressionAtlas; P19107; baseline and differential.
DR Genevisible; P19107; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0016029; C:subrhabdomeral cisterna; IDA:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0002046; F:opsin binding; TAS:FlyBase.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0002032; P:desensitization of G protein-coupled receptor signaling pathway by arrestin; IMP:FlyBase.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR GO; GO:0016060; P:metarhodopsin inactivation; IMP:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.640; -; 1.
DR Gene3D; 2.60.40.840; -; 1.
DR InterPro; IPR000698; Arrestin.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR017864; Arrestin_CS.
DR InterPro; IPR014753; Arrestin_N.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11792; PTHR11792; 1.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR PRINTS; PR00309; ARRESTIN.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS00295; ARRESTINS; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..401
FT /note="Phosrestin-1"
FT /id="PRO_0000205217"
FT MOD_RES 366
FT /note="Phosphoserine; by CaMK"
FT /evidence="ECO:0000269|PubMed:8185954"
FT VARIANT 109
FT /note="N -> S"
FT CONFLICT 111
FT /note="Y -> H (in Ref. 1; AAA28833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 45029 MW; 12C776E0DA8F0D87 CRC64;
MVVSVKVFKK ATPNGKVTFY LGRRDFIDHI DYCDPVDGVI VVEPDYLKNR KVFGQLATTY
RYGREEDEVM GVKFSKELIL CREQIVPMTN PNMEMTPMQE KLVRKLGSNA YPFTFHFPPN
SPSSVTLQQE GDDNGKPLGV EYTIRAFVGD SEDDRQHKRS MVSLVIKKLQ YAPLNRGQRL
PSSLVSKGFT FSNGKISLEV TLDREIYYHG EKTAATVQVS NNSKKSVKSI KCFIVQHTEI
TMVNAQFSKH VAQLETKEGC PITPGANLTK TFYLIPLAAN NKDRHGIALD GHLKDEDVNL
ASSTMVQEGK STGDACGIVI SYSVRIKLNC GTLGGEMQTD VPFKLLQPAP GTIEKKRSNA
MKKMKSIEQH RNVKGYYQDD DDNIVFEDFA KMRMNNVNMA D
