ARRD1_RAT
ID ARRD1_RAT Reviewed; 434 AA.
AC B0BNL6; Q68FT0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Arrestin domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Alpha-arrestin 1 {ECO:0000303|PubMed:23886940};
GN Name=Arrdc1 {ECO:0000312|RGD:1309961};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH ARRB1 AND ARRB2.
RX PubMed=23886940; DOI=10.1242/jcs.130500;
RA Puca L., Chastagner P., Meas-Yedid V., Israel A., Brou C.;
RT "Alpha-arrestin 1 (ARRDC1) and beta-arrestins cooperate to mediate Notch
RT degradation in mammals.";
RL J. Cell Sci. 126:4457-4468(2013).
CC -!- FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases
CC to their specific substrates. Through an ubiquitination-dependent
CC mechanism plays for instance a role in the incorporation of SLC11A2
CC into extracellular vesicles. More generally, plays a role in the
CC extracellular transport of proteins between cells through the release
CC in the extracellular space of microvesicles. By participating in the
CC ITCH-mediated ubiquitination and subsequent degradation of NOTCH1,
CC negatively regulates the NOTCH signaling pathway.
CC {ECO:0000250|UniProtKB:Q8N5I2}.
CC -!- SUBUNIT: Interacts (via PPxY motifs) with ITCH (via WW domains); the
CC interaction is direct and participates in the recruitment of the
CC ubiquitin-protein ligase ITCH to the NOTCH1 receptor (By similarity).
CC Interacts with ARRB1 and ARRB2; the interaction is direct
CC (PubMed:23886940). Interacts with TSG101; may recruit TSG101 to the
CC plasma membrane. Interacts (via PPxY motifs) with WWP2 (via WW
CC domains); ubiquitinates ARRDC1. Interacts with SLC11A2; controls the
CC incorporation of SLC11A2 into extracellular vesicles through an
CC ubiquitination-dependent mechanism. Interacts with WWP1 (via WW
CC domains). Interacts with NEDD4 (via WW domains). Interacts with PDCD6IP
CC (By similarity). {ECO:0000250|UniProtKB:Q8N5I2,
CC ECO:0000269|PubMed:23886940}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8N5I2}.
CC Note=Also found in extracellular vesicles different from exosomes.
CC {ECO:0000250|UniProtKB:Q8N5I2}.
CC -!- DOMAIN: The PPxY motifs mediate interaction with WW domain-containing
CC ubiquitin-protein ligases. {ECO:0000250|UniProtKB:Q8N5I2}.
CC -!- PTM: Ubiquitinated. Ubiquitination by WWP2; promotes localization to
CC extracellular microvesicles. Ubiquitinated by WWP1.
CC {ECO:0000250|UniProtKB:Q8N5I2}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79372.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR07051236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC158871; AAI58872.1; -; mRNA.
DR EMBL; BC079372; AAH79372.1; ALT_INIT; mRNA.
DR EMBL; CH474001; EDL93653.1; -; Genomic_DNA.
DR RefSeq; NP_001094240.1; NM_001100770.1.
DR AlphaFoldDB; B0BNL6; -.
DR SMR; B0BNL6; -.
DR STRING; 10116.ENSRNOP00000010169; -.
DR iPTMnet; B0BNL6; -.
DR PhosphoSitePlus; B0BNL6; -.
DR PaxDb; B0BNL6; -.
DR Ensembl; ENSRNOT00000010169; ENSRNOP00000010169; ENSRNOG00000007622.
DR GeneID; 366001; -.
DR KEGG; rno:366001; -.
DR CTD; 92714; -.
DR RGD; 1309961; Arrdc1.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000159652; -.
DR HOGENOM; CLU_051966_0_0_1; -.
DR InParanoid; B0BNL6; -.
DR OMA; VRYNNTF; -.
DR OrthoDB; 647994at2759; -.
DR PhylomeDB; B0BNL6; -.
DR TreeFam; TF313650; -.
DR PRO; PR:B0BNL6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000007622; Expressed in lung and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:1990763; F:arrestin family protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006858; P:extracellular transport; ISS:UniProtKB.
DR GO; GO:0140112; P:extracellular vesicle biogenesis; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..434
FT /note="Arrestin domain-containing protein 1"
FT /id="PRO_0000442290"
FT REGION 295..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 401..404
FT /note="PPxY motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q8N5I2"
FT MOTIF 414..417
FT /note="PPxY motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q8N5I2"
FT COMPBIAS 327..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 234
FT /note="R -> S (in Ref. 3; AAH79372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 46109 MW; C6786C48F2A1AC4B CRC64;
MGRVQLFEIR LSQGRVVYSP GEPLAGAVHL RLGAPLPFRA IRVTCMGSCG VSNKANDGAW
VVEESYFNSS LSLADKGSLP PGEHNFPFQF LLPATAPTSF EGPFGKIVHQ VRASIDTPRF
SKDHKCSLVF YILSPLNLNS IPDIEQPNVA STTKKFSYKL VKTGSVVLTA STDLRGYVVG
QVLRLQADIE NQSGKDTSPV VASLLQKVSY KAKRWIYDVR TIAEVEGTGV KAWRHAQWQE
QILVPALPQS ALPGCSLIHI DYYLQVSMKA PEATVTLPLF VGNIAVNQTP LSPCPGPGSS
PGLLSPVVPS APPQEEAEAV ASGPHFSDPV SLSTKSHSQQ QPLSTTLGSV SVTTIEPCVQ
VGSPARHSLH PPLCISIGAT VPYFAEGSGG PVPTTSALIL PPEYSSWGYP YEAPPSYEQS
CGAGGTDVGL IPGS
