ARRD1_MOUSE
ID ARRD1_MOUSE Reviewed; 434 AA.
AC Q99KN1; A2AIS7; A2AIS8; Q3TDT6; Q8VEG7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
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|MGI:MGI:2446136};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
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).
RN [6]
RP FUNCTION.
RX PubMed=27462458; DOI=10.1038/celldisc.2016.11;
RA Mackenzie K., Foot N.J., Anand S., Dalton H.E., Chaudhary N., Collins B.M.,
RA Mathivanan S., Kumar S.;
RT "Regulation of the divalent metal ion transporter via membrane budding.";
RL Cell Discov. 2:16011-16011(2016).
CC -!- FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases
CC to their specific substrates (PubMed:23886940, PubMed:27462458).
CC Through an ubiquitination-dependent mechanism plays for instance a role
CC in the incorporation of SLC11A2 into extracellular vesicles
CC (PubMed:27462458). More generally, plays a role in the extracellular
CC transport of proteins between cells through the release in the
CC extracellular space of microvesicles (By similarity). By participating
CC to the ITCH-mediated ubiquitination and subsequent degradation of
CC NOTCH1, negatively regulates the NOTCH signaling pathway
CC (PubMed:23886940). {ECO:0000250|UniProtKB:Q8N5I2,
CC ECO:0000269|PubMed:23886940, ECO:0000269|PubMed:27462458}.
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. Interacts with
CC ARRB1 and ARRB2; the interaction is direct. Interacts with TSG101; may
CC recruit TSG101 to the plasma membrane. Interacts (via PPxY motifs) with
CC WWP2 (via WW domains); ubiquitinates ARRDC1. Interacts with SLC11A2;
CC controls the incorporation of SLC11A2 into extracellular vesicles
CC through an ubiquitination-dependent mechanism. Interacts with WWP1 (via
CC WW domains). Interacts with NEDD4 (via WW domains). Interacts with
CC PDCD6IP. {ECO:0000250|UniProtKB:Q8N5I2}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99KN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KN1-2; Sequence=VSP_019543;
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=AAH04091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK170018; BAE41513.1; -; mRNA.
DR EMBL; AL732525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004091; AAH04091.1; ALT_INIT; mRNA.
DR EMBL; BC018501; AAH18501.1; -; mRNA.
DR CCDS; CCDS15741.1; -. [Q99KN1-2]
DR CCDS; CCDS50521.1; -. [Q99KN1-1]
DR RefSeq; NP_001155957.1; NM_001162485.1. [Q99KN1-1]
DR RefSeq; NP_848495.2; NM_178408.3. [Q99KN1-2]
DR AlphaFoldDB; Q99KN1; -.
DR SMR; Q99KN1; -.
DR STRING; 10090.ENSMUSP00000028349; -.
DR iPTMnet; Q99KN1; -.
DR PhosphoSitePlus; Q99KN1; -.
DR EPD; Q99KN1; -.
DR MaxQB; Q99KN1; -.
DR PaxDb; Q99KN1; -.
DR PeptideAtlas; Q99KN1; -.
DR PRIDE; Q99KN1; -.
DR ProteomicsDB; 281836; -. [Q99KN1-1]
DR ProteomicsDB; 281837; -. [Q99KN1-2]
DR Antibodypedia; 49444; 153 antibodies from 25 providers.
DR Ensembl; ENSMUST00000028349; ENSMUSP00000028349; ENSMUSG00000026972. [Q99KN1-1]
DR Ensembl; ENSMUST00000102935; ENSMUSP00000099999; ENSMUSG00000026972. [Q99KN1-2]
DR GeneID; 215705; -.
DR KEGG; mmu:215705; -.
DR UCSC; uc008ipm.2; mouse. [Q99KN1-2]
DR UCSC; uc008ipn.2; mouse. [Q99KN1-1]
DR CTD; 92714; -.
DR MGI; MGI:2446136; Arrdc1.
DR VEuPathDB; HostDB:ENSMUSG00000026972; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000159652; -.
DR HOGENOM; CLU_051966_0_0_1; -.
DR InParanoid; Q99KN1; -.
DR OMA; VRYNNTF; -.
DR OrthoDB; 647994at2759; -.
DR PhylomeDB; Q99KN1; -.
DR TreeFam; TF313650; -.
DR BioGRID-ORCS; 215705; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Arrdc1; mouse.
DR PRO; PR:Q99KN1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99KN1; protein.
DR Bgee; ENSMUSG00000026972; Expressed in granulocyte and 243 other tissues.
DR ExpressionAtlas; Q99KN1; baseline and differential.
DR Genevisible; Q99KN1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
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:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
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 Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..434
FT /note="Arrestin domain-containing protein 1"
FT /id="PRO_0000244346"
FT REGION 292..349
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 292..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019543"
FT CONFLICT 27
FT /note="T -> A (in Ref. 3; AAH18501)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="R -> P (in Ref. 3; AAH18501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 46330 MW; 754B56CCC3988F53 CRC64;
MGRVQLFEIR LSQGRVVYGP GEPLAGTVHL RLGAPLPFRA IRVTCMGSCG VSTKANDGAW
VVEESYFNSS LSLADKGSLP AGEHNFPFQF LLPATAPTSF EGPFGKIVHQ VRASIDTPRF
SKDHKCSLVF YILSPLNLNS IPDIEQPNVA STTKKFSYKL VKTGNVVLTA STDLRGYVVG
QVLRLQADIE NQSGKDTSPV VASLLQKVSY KAKRWIYDVR TIAEVEGTGV KAWRRAQWQE
QILVPALPQS ALPGCSLIHI DYYLQVSMKA PEATVTLPLF VGNIAVNQTP LSPCPGRESS
PGTLSLVVPS APPQEEAEAV ASGPHFSDPV SLSTKSHSQQ QPLSAPLGSV SVTTTEPWVQ
VGSPARHSLH PPLCISIGAT VPYFAEGSAG PVPTTSALIL PPEYSSWGYP YEAPPSYEQS
CGAAGTDLGL IPGS
