ARRB_CAEEL
ID ARRB_CAEEL Reviewed; 435 AA.
AC P51485;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-arrestin arr-1 {ECO:0000305};
GN Name=arr-1 {ECO:0000312|WormBase:F53H8.2};
GN ORFNames=F53H8.2 {ECO:0000312|WormBase:F53H8.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15157420; DOI=10.1016/s0896-6273(04)00252-1;
RA Fukuto H.S., Ferkey D.M., Apicella A.J., Lans H., Sharmeen T., Chen W.,
RA Lefkowitz R.J., Jansen G., Schafer W.R., Hart A.C.;
RT "G protein-coupled receptor kinase function is essential for chemosensation
RT in C. elegans.";
RL Neuron 42:581-593(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CHC-1 AND ABP-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=15878875; DOI=10.1074/jbc.m502637200;
RA Palmitessa A., Hess H.A., Bany I.A., Kim Y.M., Koelle M.R., Benovic J.L.;
RT "Caenorhabditus elegans arrestin regulates neural G protein signaling and
RT olfactory adaptation and recovery.";
RL J. Biol. Chem. 280:24649-24662(2005).
RN [4]
RP FUNCTION, IDENTIFICATION IN A DAF-18; ARR-1 AND MPZ-1 COMPLEX, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LEU-435.
RX PubMed=20207731; DOI=10.1074/jbc.m110.104612;
RA Palmitessa A., Benovic J.L.;
RT "Arrestin and the multi-PDZ domain-containing protein MPZ-1 interact with
RT phosphatase and tensin homolog (PTEN) and regulate Caenorhabditis elegans
RT longevity.";
RL J. Biol. Chem. 285:15187-15200(2010).
CC -!- FUNCTION: Adapter protein required for olfactory adaptation and
CC recovery to volatile odorants, probably by desensitization of G-protein
CC coupled receptors (GPCR) (PubMed:15878875). May play a role in
CC clathrin-mediated GPCR endocytosis (PubMed:15878875). Acts as positive
CC regulator of insulin-like daf-2 signaling pathway probably by forming a
CC complex with mpz-1 and phosphatase daf-18 likely resulting in daf-18
CC inhibition (PubMed:20207731). Involved in egg-laying (PubMed:15878875).
CC {ECO:0000269|PubMed:15878875, ECO:0000269|PubMed:20207731}.
CC -!- SUBUNIT: Component of a complex composed of arr-1, daf-18 and mpz-1
CC (PubMed:20207731). Within the complex, interacts (via C-terminus) with
CC mpz-1 (via PDZ domain) and phosphatase daf-18 (PubMed:20207731). May
CC interact (via C-terminus) with clathrin chc-1 and beta-2 adaptin (AP2)
CC apb-1 (PubMed:15878875). {ECO:0000269|PubMed:15878875,
CC ECO:0000269|PubMed:20207731}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:15878875}. Cell
CC projection, dendrite {ECO:0000269|PubMed:15878875}. Note=Localizes to
CC the amphid processes of chemosensory neurons.
CC {ECO:0000269|PubMed:15878875}.
CC -!- TISSUE SPECIFICITY: Expressed in head neurons, nerve ring and ventral
CC nerve cord (at protein level) (PubMed:15878875). Expressed in the
CC nervous system including the nerve ring and the ventral and dorsal
CC nerve cords (PubMed:15878875, PubMed:15157420). Highly expressed in
CC amphid chemosensory neurons AWA, AWB, AWC, ADL and ASH, and in
CC hermaphrodite specific neuron HSN (PubMed:15878875, PubMed:15157420).
CC Also expressed in the intestine (PubMed:15157420).
CC {ECO:0000269|PubMed:15157420, ECO:0000269|PubMed:15878875}.
CC -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates the
CC interaction with the AP-2 complex subunit apb-1.
CC {ECO:0000250|UniProtKB:Q5SW96}.
CC -!- DOMAIN: The C-terminus (aa 369-435) is required for the recovery of
CC chemotaxis from odorant-induced adaptation but is dispensable for
CC behavioral adaptation to chemoattractant isoamyl alcohol.
CC {ECO:0000269|PubMed:15878875}.
CC -!- DISRUPTION PHENOTYPE: No effect on the response to the aversive
CC chemical stimulus octanol or to volatile attractants (PubMed:15157420).
CC Behavioral adaptation to prolonged exposure to isoamyl alcohol or
CC benzaldehyde is impaired (PubMed:15878875). Recovery of chemotaxis from
CC odorant-induced adaptation is impaired (PubMed:15878875). Moderate
CC reduction in chemotaxis towards volatile attractant diacetyl but not
CC towards isoamyl alcohol and benzaldehyde (PubMed:15878875). Slight
CC defect in egg-laying (PubMed:15878875). Increased lifespan and nuclear
CC localization of daf-16 (PubMed:20207731). Reduced lifespan in a daf-16
CC (mu86) mutant background or in a mpz-1 RNAi-mediated knockdown
CC background (PubMed:20207731). {ECO:0000269|PubMed:15157420,
CC ECO:0000269|PubMed:15878875, ECO:0000269|PubMed:20207731}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; FO080855; CCD67242.1; -; Genomic_DNA.
DR PIR; T34297; T34297.
DR RefSeq; NP_508183.1; NM_075782.4.
DR AlphaFoldDB; P51485; -.
DR SMR; P51485; -.
DR BioGRID; 45399; 3.
DR ComplexPortal; CPX-3881; arr-1-mpz-1-daf-18 complex.
DR STRING; 6239.F53H8.2; -.
DR EPD; P51485; -.
DR PaxDb; P51485; -.
DR PeptideAtlas; P51485; -.
DR EnsemblMetazoa; F53H8.2.1; F53H8.2.1; WBGene00000195.
DR GeneID; 180446; -.
DR KEGG; cel:CELE_F53H8.2; -.
DR UCSC; F53H8.2; c. elegans.
DR CTD; 180446; -.
DR WormBase; F53H8.2; CE28831; WBGene00000195; arr-1.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_1_0_1; -.
DR InParanoid; P51485; -.
DR OMA; LYLAHEQ; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; P51485; -.
DR Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-CEL-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P51485; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000195; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0062049; C:protein phosphatase inhibitor complex; IC:ComplexPortal.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR GO; GO:0032501; P:multicellular organismal process; IGI:WormBase.
DR GO; GO:0040010; P:positive regulation of growth rate; IGI:WormBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Cell projection; Reference proteome; Sensory transduction.
FT CHAIN 1..435
FT /note="Beta-arrestin arr-1"
FT /id="PRO_0000205202"
FT REGION 358..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..394
FT /note="Clathrin box"
FT /evidence="ECO:0000250|UniProtKB:Q5SW96"
FT MOTIF 404..414
FT /note="[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif"
FT /evidence="ECO:0000250|UniProtKB:Q5SW96"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 432..435
FT /note="Missing: Prevents interaction with mpz-1."
FT /evidence="ECO:0000269|PubMed:20207731"
FT MUTAGEN 435
FT /note="L->A: Increases lifespan. Prevents interaction with
FT mpz-1."
FT /evidence="ECO:0000269|PubMed:20207731"
SQ SEQUENCE 435 AA; 48458 MW; 1340E033655C5CB7 CRC64;
MVDEDKKSGT RVFKKTSPNG KITTYLGKRD FIDRGDYVDL IDGMVLIDEE YIKDNRKVTA
HLLAAFRYGR EDLDVLGLTF RKDLISETFQ VYPQTDKSIS RPLSRLQERL KRKLGANAFP
FWFEVAPKSA SSVTLQPAPG DTGKPCGVDY ELKTFVAVTD GSSGEKPKKS ALSNTVRLAI
RKLTYAPFES RPQPMVDVSK YFMMSSGLLH MEVSLDKEMY YHGESISVNV HIQNNSNKTV
KKLKIYIIQV ADICLFTTAS YSCEVARIES NEGFPVGPGG TLSKVFAVCP LLSNNKDKRG
LALDGQLKHE DTNLASSTIL DSKTSKESLG IVVQYRVKVR AVLGPLNGEL FAELPFTLTH
SKPPESPERT DRGLPSIEAT NGSEPVDIDL IQLHEELEPR YDDDLIFEDF ARMRLHGNDS
EDQPSPSANL PPSLL
