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Arrestin domain-containing protein 3 (TBP-2-like inducible membrane protein) (TLIMP)

 ARRD3_HUMAN             Reviewed;         414 AA.
Q96B67; A8K6T8; Q9P2H1;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 126.
RecName: Full=Arrestin domain-containing protein 3;
AltName: Full=TBP-2-like inducible membrane protein {ECO:0000303|PubMed:16269462};
Short=TLIMP {ECO:0000303|PubMed:16269462};
Name=ARRDC3; Synonyms=KIAA1376;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, LACK OF INTERACTION WITH TXN, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=16269462; DOI=10.1210/en.2005-0679;
Oka S., Masutani H., Liu W., Horita H., Wang D., Kizaka-Kondoh S.,
Yodoi J.;
"Thioredoxin-binding protein-2-like inducible membrane protein is a
novel vitamin D3 and peroxisome proliferator-activated receptor
(PPAR)gamma ligand target protein that regulates PPARgamma
signaling.";
Endocrinology 147:733-743(2006).
[5]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEDD4 AND ADRB2, AND
MUTAGENESIS OF 346-PRO--TYR-349 AND 391-PRO--TYR-394.
PubMed=20559325; DOI=10.1038/embor.2010.80;
Nabhan J.F., Pan H., Lu Q.;
"Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to
mediate ubiquitination of the beta2-adrenergic receptor.";
EMBO Rep. 11:605-611(2010).
[6]
FUNCTION, INTERACTION WITH ADRB2 AND ADRB3, TISSUE SPECIFICITY, AND
INDUCTION BY FASTING.
PubMed=21982743; DOI=10.1016/j.cmet.2011.08.011;
Patwari P., Emilsson V., Schadt E.E., Chutkow W.A., Lee S.,
Marsili A., Zhang Y., Dobrin R., Cohen D.E., Larsen P.R.,
Zavacki A.M., Fong L.G., Young S.G., Lee R.T.;
"The arrestin domain-containing 3 protein regulates body mass and
energy expenditure.";
Cell Metab. 14:671-683(2011).
[7]
INTERACTION WITH WWP1.
PubMed=21191027; DOI=10.1128/JVI.02045-10;
Rauch S., Martin-Serrano J.;
"Multiple interactions between the ESCRT machinery and arrestin-
related proteins: implications for PPXY-dependent budding.";
J. Virol. 85:3546-3556(2011).
[8]
FUNCTION, INTERACTION WITH HGS AND NEDD4, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 346-PRO--TYR-349 AND 391-PRO--TYR-394.
PubMed=23208550; DOI=10.1038/embor.2012.187;
Han S.O., Kommaddi R.P., Shenoy S.K.;
"Distinct roles for beta-arrestin2 and arrestin-domain-containing
proteins in beta2 adrenergic receptor trafficking.";
EMBO Rep. 14:164-171(2013).
[9]
INTERACTION WITH ITCH.
PubMed=23886940; DOI=10.1242/jcs.130500;
Puca L., Chastagner P., Meas-Yedid V., Israel A., Brou C.;
"Alpha-arrestin 1 (ARRDC1) and beta-arrestins cooperate to mediate
Notch degradation in mammals.";
J. Cell Sci. 126:4457-4468(2013).
[10] {ECO:0000244|PDB:4N7H}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 342-354 IN COMPLEX WITH
NEDD4, AND INTERACTION WITH NEDD4.
PubMed=24379409; DOI=10.1074/jbc.M113.527473;
Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
"Structural and biochemical basis for ubiquitin ligase recruitment by
arrestin-related domain-containing protein-3 (ARRDC3).";
J. Biol. Chem. 289:4743-4752(2014).
[11] {ECO:0000244|PDB:4R7V, ECO:0000244|PDB:4R7X}
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-180, INTERACTION WITH
ADRB2, AND MUTAGENESIS OF LYS-48; ARG-52; LYS-56; ARG-58; LYS-85;
ARG-135; LYS-139 AND LYS-153.
PubMed=25220262; DOI=10.1002/pro.2549;
Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
"Insights into beta2-adrenergic receptor binding from structures of
the N-terminal lobe of ARRDC3.";
Protein Sci. 23:1708-1716(2014).
-!- FUNCTION: Adapter protein that plays a role in regulating cell-
surface expression of adrenergic receptors and probably also other
G protein-coupled receptors (PubMed:20559325, PubMed:21982743,
PubMed:23208550). Plays a role in NEDD4-mediated ubiquitination
and endocytosis af activated ADRB2 and subsequent ADRB2
degradation (PubMed:20559325, PubMed:23208550). May recruit NEDD4
to ADRB2 (PubMed:20559325). Alternatively, may function as adapter
protein that does not play a major role in recruiting NEDD4 to
ADRB2, but rather plays a role in a targeting ADRB2 to endosomes
(PubMed:23208550). {ECO:0000269|PubMed:20559325,
ECO:0000269|PubMed:23208550}.
-!- SUBUNIT: Interacts (via PPxY motifs) with NEDD4 (via WW domains)
(PubMed:20559325, PubMed:23208550, PubMed:24379409). Interacts
with ADRB2 (PubMed:20559325, PubMed:21982743, PubMed:25220262).
Interacts with ADRB3 (PubMed:21982743). Interacts with HGS (via
PPxY motifs) (PubMed:23208550). Does not bind TXN (thioredoxin)
(PubMed:16269462). Interacts with ITCH (PubMed:23886940).
Interacts with WWP1 (via WW domains) (PubMed:21191027).
{ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325,
ECO:0000269|PubMed:21191027, ECO:0000269|PubMed:21982743,
ECO:0000269|PubMed:23208550, ECO:0000269|PubMed:23886940,
ECO:0000269|PubMed:24379409, ECO:0000269|PubMed:25220262}.
-!- INTERACTION:
P07550:ADRB2; NbExp=6; IntAct=EBI-2875665, EBI-491169;
O95817:BAG3; NbExp=7; IntAct=EBI-2875665, EBI-747185;
Q96GG9:DCUN1D1; NbExp=7; IntAct=EBI-2875665, EBI-740086;
O60760:HPGDS; NbExp=7; IntAct=EBI-2875665, EBI-10187349;
P16144:ITGB4; NbExp=3; IntAct=EBI-2875665, EBI-948678;
Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-2875665, EBI-399246;
Q9UBU8-2:MORF4L1; NbExp=3; IntAct=EBI-2875665, EBI-10288852;
Q96DC9:OTUB2; NbExp=5; IntAct=EBI-2875665, EBI-746259;
O43189:PHF1; NbExp=4; IntAct=EBI-2875665, EBI-530034;
O75886:STAM2; NbExp=5; IntAct=EBI-2875665, EBI-373258;
P21580:TNFAIP3; NbExp=5; IntAct=EBI-2875665, EBI-527670;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-2875665, EBI-5235829;
Q96LR5:UBE2E2; NbExp=5; IntAct=EBI-2875665, EBI-2129763;
Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-2875665, EBI-947187;
O00308:WWP2; NbExp=4; IntAct=EBI-2875665, EBI-743923;
Q9UGI0:ZRANB1; NbExp=4; IntAct=EBI-2875665, EBI-527853;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16269462,
ECO:0000269|PubMed:23208550}. Cell membrane
{ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325,
ECO:0000269|PubMed:23208550}; Peripheral membrane protein
{ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325};
Cytoplasmic side {ECO:0000269|PubMed:16269462,
ECO:0000269|PubMed:20559325}. Lysosome
{ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}.
Endosome {ECO:0000269|PubMed:16269462,
ECO:0000269|PubMed:23208550}. Early endosome
{ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}.
Note=Associated with plasma membrane, as well as with endosomes
and lysosomes during endocytosis (PubMed:16269462,
PubMed:23208550, PubMed:20559325). {ECO:0000269|PubMed:16269462,
ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, placenta,
kidney, lung, liver, blood, adrenal gland, lymph node, mammary
gland, thyroid, and trachea (PubMed:16269462, PubMed:21982743).
Very low levels in colon, thymus, spleen, small intestine, bladder
and bone marrow (PubMed:16269462). Strong expression in
differentiated adipocytes compared to preadipocytes
(PubMed:16269462). Detected in omental fat and subcutaneous fat
tissue (PubMed:21982743). {ECO:0000269|PubMed:16269462}.
-!- INDUCTION: By troglitazone and pioglitazone (selective PPARG
agonists), by prostaglandin J2 (PGJ2) and by L165,041 (a PPARD
ligand), by vitamin D3 and, to a lesser extent, by phorbol
myristate acetate (PMA) in the promyelocytic leukemia HL-60 cells.
No induction by retinoic acid, nor by clofibrate (a specific PPARA
agonist) (PubMed:16269462). Up-regulated by fasting
(PubMed:21982743). {ECO:0000269|PubMed:16269462,
ECO:0000269|PubMed:21982743}.
-!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92614.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB037797; BAA92614.1; ALT_INIT; mRNA.
EMBL; AK291753; BAF84442.1; -; mRNA.
EMBL; BC015928; AAH15928.1; -; mRNA.
EMBL; BC053619; AAH53619.1; -; mRNA.
CCDS; CCDS34202.1; -.
RefSeq; NP_065852.1; NM_020801.3.
UniGene; Hs.24684; -.
PDB; 4N7H; X-ray; 1.70 A; B=342-354.
PDB; 4R7V; X-ray; 1.73 A; A=1-165.
PDB; 4R7X; X-ray; 2.61 A; A/B=1-180.
PDBsum; 4N7H; -.
PDBsum; 4R7V; -.
PDBsum; 4R7X; -.
ProteinModelPortal; Q96B67; -.
SMR; Q96B67; -.
BioGrid; 121616; 37.
IntAct; Q96B67; 41.
STRING; 9606.ENSP00000265138; -.
iPTMnet; Q96B67; -.
PhosphoSitePlus; Q96B67; -.
BioMuta; ARRDC3; -.
DMDM; 74731205; -.
MaxQB; Q96B67; -.
PaxDb; Q96B67; -.
PeptideAtlas; Q96B67; -.
PRIDE; Q96B67; -.
DNASU; 57561; -.
Ensembl; ENST00000265138; ENSP00000265138; ENSG00000113369.
GeneID; 57561; -.
KEGG; hsa:57561; -.
UCSC; uc003kjz.3; human.
CTD; 57561; -.
DisGeNET; 57561; -.
EuPathDB; HostDB:ENSG00000113369.8; -.
GeneCards; ARRDC3; -.
HGNC; HGNC:29263; ARRDC3.
MIM; 612464; gene.
neXtProt; NX_Q96B67; -.
OpenTargets; ENSG00000113369; -.
PharmGKB; PA134925765; -.
eggNOG; KOG3780; Eukaryota.
eggNOG; ENOG41102NY; LUCA.
GeneTree; ENSGT00550000074356; -.
HOGENOM; HOG000237328; -.
HOVERGEN; HBG066469; -.
InParanoid; Q96B67; -.
OMA; PWLLPMK; -.
OrthoDB; EOG091G0B0Y; -.
PhylomeDB; Q96B67; -.
TreeFam; TF313650; -.
ChiTaRS; ARRDC3; human.
GenomeRNAi; 57561; -.
PRO; PR:Q96B67; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113369; -.
CleanEx; HS_ARRDC3; -.
Genevisible; Q96B67; HS.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0031699; F:beta-3 adrenergic receptor binding; IDA:MGI.
GO; GO:0060613; P:fat pad development; IEA:Ensembl.
GO; GO:0031651; P:negative regulation of heat generation; IEA:Ensembl.
GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
GO; GO:0044252; P:negative regulation of multicellular organismal metabolic process; IEA:Ensembl.
GO; GO:0071879; P:positive regulation of adrenergic receptor signaling pathway; IEA:Ensembl.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IPI:MGI.
GO; GO:0043588; P:skin development; IEA:Ensembl.
GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
InterPro; IPR011021; Arrestin-like_N.
InterPro; IPR011022; Arrestin_C-like.
InterPro; IPR014756; Ig_E-set.
Pfam; PF02752; Arrestin_C; 1.
Pfam; PF00339; Arrestin_N; 1.
SMART; SM01017; Arrestin_C; 1.
SUPFAM; SSF81296; SSF81296; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm; Endosome;
Lysosome; Membrane; Reference proteome; Repeat.
CHAIN 1 414 Arrestin domain-containing protein 3.
/FTId=PRO_0000244349.
MOTIF 346 349 PPxY motif 1. {ECO:0000305}.
MOTIF 391 394 PPxY motif 2. {ECO:0000305}.
MUTAGEN 48 48 K->E: Abolishes interaction with ADRB2;
when associated with E-52; E-85 and E-
139. {ECO:0000269|PubMed:25220262}.
MUTAGEN 52 52 R->E: Abolishes interaction with ADRB2;
when associated with E-48; E-85 and E-
139. {ECO:0000269|PubMed:25220262}.
MUTAGEN 56 56 K->E: Nearly abolishes interaction with
ADRB2; when associated with E-58; E-135
and E-153. {ECO:0000269|PubMed:25220262}.
MUTAGEN 58 58 R->E: Nearly abolishes interaction with
ADRB2; when associated with E-56; E-135
and E-153. {ECO:0000269|PubMed:25220262}.
MUTAGEN 85 85 K->E: Abolishes interaction with ADRB2;
when associated with E-48; E-52 and E-
139. {ECO:0000269|PubMed:25220262}.
MUTAGEN 135 135 R->E: Nearly abolishes interaction with
ADRB2; when associated with E-56; E-58
and E-153. {ECO:0000269|PubMed:25220262}.
MUTAGEN 139 139 K->E: Abolishes interaction with ADRB2;
when associated with E-48; E-52 and E-85.
{ECO:0000269|PubMed:25220262}.
MUTAGEN 153 153 K->E: Nearly abolishes interaction with
ADRB2; when associated with E-56; E-58
and E-135. {ECO:0000269|PubMed:25220262}.
MUTAGEN 346 349 PPSY->AASA: Strongly reduces interaction
with NEDD4. Abolishes interaction with
NEDD4; when associated with 391-A--A-394.
Abolishes interaction with HGS; when
associated with 391-A--A-394.
{ECO:0000269|PubMed:20559325,
ECO:0000269|PubMed:23208550}.
MUTAGEN 391 394 PPLY->AALA: Abolishes interaction with
NEDD4; when associated with 346-A--A-349.
{ECO:0000269|PubMed:20559325}.
CONFLICT 12 12 S -> G (in Ref. 2; BAF84442).
{ECO:0000305}.
STRAND 5 13 {ECO:0000244|PDB:4R7V}.
STRAND 29 40 {ECO:0000244|PDB:4R7V}.
STRAND 42 61 {ECO:0000244|PDB:4R7V}.
STRAND 73 90 {ECO:0000244|PDB:4R7V}.
STRAND 103 105 {ECO:0000244|PDB:4R7V}.
STRAND 107 117 {ECO:0000244|PDB:4R7V}.
STRAND 130 143 {ECO:0000244|PDB:4R7V}.
STRAND 150 155 {ECO:0000244|PDB:4R7V}.
HELIX 349 351 {ECO:0000244|PDB:4N7H}.
SEQUENCE 414 AA; 46395 MW; 9B02190E1BA90B1D CRC64;
MVLGKVKSLT ISFDCLNDSN VPVYSSGDTV SGRVNLEVTG EIRVKSLKIH ARGHAKVRWT
ESRNAGSNTA YTQNYTEEVE YFNHKDILIG HERDDDNSEE GFHTIHSGRH EYAFSFELPQ
TPLATSFEGR HGSVRYWVKA ELHRPWLLPV KLKKEFTVFE HIDINTPSLL SPQAGTKEKT
LCCWFCTSGP ISLSAKIERK GYTPGESIQI FAEIENCSSR MVVPKAAIYQ TQAFYAKGKM
KEVKQLVANL RGESLSSGKT ETWNGKLLKI PPVSPSILDC SIIRVEYSLM VYVDIPGAMD
LFLNLPLVIG TIPLHPFGSR TSSVSSQCSM NMNWLSLSLP ERPEAPPSYA EVVTEEQRRN
NLAPVSACDD FERALQGPLF AYIQEFRFLP PPLYSEIDPN PDQSADDRPS CPSR


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