ARRD3_HUMAN
ID ARRD3_HUMAN Reviewed; 414 AA.
AC Q96B67; A8K6T8; Q9P2H1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Arrestin domain-containing protein 3;
DE AltName: Full=TBP-2-like inducible membrane protein {ECO:0000303|PubMed:16269462};
DE Short=TLIMP {ECO:0000303|PubMed:16269462};
GN Name=ARRDC3; Synonyms=KIAA1376;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 SUBCELLULAR LOCATION, LACK OF INTERACTION WITH TXN, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=16269462; DOI=10.1210/en.2005-0679;
RA Oka S., Masutani H., Liu W., Horita H., Wang D., Kizaka-Kondoh S.,
RA Yodoi J.;
RT "Thioredoxin-binding protein-2-like inducible membrane protein is a novel
RT vitamin D3 and peroxisome proliferator-activated receptor (PPAR)gamma
RT ligand target protein that regulates PPARgamma signaling.";
RL Endocrinology 147:733-743(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEDD4 AND ADRB2, AND
RP MUTAGENESIS OF 346-PRO--TYR-349 AND 391-PRO--TYR-394.
RX PubMed=20559325; DOI=10.1038/embor.2010.80;
RA Nabhan J.F., Pan H., Lu Q.;
RT "Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to
RT mediate ubiquitination of the beta2-adrenergic receptor.";
RL EMBO Rep. 11:605-611(2010).
RN [6]
RP FUNCTION, INTERACTION WITH ADRB2 AND ADRB3, TISSUE SPECIFICITY, AND
RP INDUCTION BY FASTING.
RX PubMed=21982743; DOI=10.1016/j.cmet.2011.08.011;
RA Patwari P., Emilsson V., Schadt E.E., Chutkow W.A., Lee S., Marsili A.,
RA Zhang Y., Dobrin R., Cohen D.E., Larsen P.R., Zavacki A.M., Fong L.G.,
RA Young S.G., Lee R.T.;
RT "The arrestin domain-containing 3 protein regulates body mass and energy
RT expenditure.";
RL Cell Metab. 14:671-683(2011).
RN [7]
RP INTERACTION WITH WWP1.
RX PubMed=21191027; DOI=10.1128/jvi.02045-10;
RA Rauch S., Martin-Serrano J.;
RT "Multiple interactions between the ESCRT machinery and arrestin-related
RT proteins: implications for PPXY-dependent budding.";
RL J. Virol. 85:3546-3556(2011).
RN [8]
RP FUNCTION, INTERACTION WITH HGS AND NEDD4, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 346-PRO--TYR-349 AND 391-PRO--TYR-394.
RX PubMed=23208550; DOI=10.1038/embor.2012.187;
RA Han S.O., Kommaddi R.P., Shenoy S.K.;
RT "Distinct roles for beta-arrestin2 and arrestin-domain-containing proteins
RT in beta2 adrenergic receptor trafficking.";
RL EMBO Rep. 14:164-171(2013).
RN [9]
RP INTERACTION WITH ITCH.
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 [10] {ECO:0007744|PDB:4N7H}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 342-354 IN COMPLEX WITH NEDD4,
RP AND INTERACTION WITH NEDD4.
RX PubMed=24379409; DOI=10.1074/jbc.m113.527473;
RA Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
RT "Structural and biochemical basis for ubiquitin ligase recruitment by
RT arrestin-related domain-containing protein-3 (ARRDC3).";
RL J. Biol. Chem. 289:4743-4752(2014).
RN [11] {ECO:0007744|PDB:4R7V, ECO:0007744|PDB:4R7X}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-180, INTERACTION WITH ADRB2,
RP AND MUTAGENESIS OF LYS-48; ARG-52; LYS-56; ARG-58; LYS-85; ARG-135; LYS-139
RP AND LYS-153.
RX PubMed=25220262; DOI=10.1002/pro.2549;
RA Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
RT "Insights into beta2-adrenergic receptor binding from structures of the N-
RT terminal lobe of ARRDC3.";
RL Protein Sci. 23:1708-1716(2014).
CC -!- FUNCTION: Adapter protein that plays a role in regulating cell-surface
CC expression of adrenergic receptors and probably also other G protein-
CC coupled receptors (PubMed:20559325, PubMed:21982743, PubMed:23208550).
CC Plays a role in NEDD4-mediated ubiquitination and endocytosis af
CC activated ADRB2 and subsequent ADRB2 degradation (PubMed:20559325,
CC PubMed:23208550). May recruit NEDD4 to ADRB2 (PubMed:20559325).
CC Alternatively, may function as adapter protein that does not play a
CC major role in recruiting NEDD4 to ADRB2, but rather plays a role in a
CC targeting ADRB2 to endosomes (PubMed:23208550).
CC {ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23208550}.
CC -!- SUBUNIT: Interacts (via PPxY motifs) with NEDD4 (via WW domains)
CC (PubMed:20559325, PubMed:23208550, PubMed:24379409). Interacts with
CC ADRB2 (PubMed:20559325, PubMed:21982743, PubMed:25220262). Interacts
CC with ADRB3 (PubMed:21982743). Interacts with HGS (via PPxY motifs)
CC (PubMed:23208550). Does not bind TXN (thioredoxin) (PubMed:16269462).
CC Interacts with ITCH (PubMed:23886940). Interacts with WWP1 (via WW
CC domains) (PubMed:21191027). {ECO:0000269|PubMed:16269462,
CC ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:21191027,
CC ECO:0000269|PubMed:21982743, ECO:0000269|PubMed:23208550,
CC ECO:0000269|PubMed:23886940, ECO:0000269|PubMed:24379409,
CC ECO:0000269|PubMed:25220262}.
CC -!- INTERACTION:
CC Q96B67; P07550: ADRB2; NbExp=6; IntAct=EBI-2875665, EBI-491169;
CC Q96B67; O95817: BAG3; NbExp=10; IntAct=EBI-2875665, EBI-747185;
CC Q96B67; P41182: BCL6; NbExp=3; IntAct=EBI-2875665, EBI-765407;
CC Q96B67; Q8IVM0: CCDC50; NbExp=3; IntAct=EBI-2875665, EBI-723996;
CC Q96B67; P32320: CDA; NbExp=5; IntAct=EBI-2875665, EBI-9250559;
CC Q96B67; Q96GG9: DCUN1D1; NbExp=10; IntAct=EBI-2875665, EBI-740086;
CC Q96B67; O95967: EFEMP2; NbExp=3; IntAct=EBI-2875665, EBI-743414;
CC Q96B67; O95208-2: EPN2; NbExp=3; IntAct=EBI-2875665, EBI-12135243;
CC Q96B67; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2875665, EBI-6658203;
CC Q96B67; O60760: HPGDS; NbExp=9; IntAct=EBI-2875665, EBI-10187349;
CC Q96B67; Q96J02: ITCH; NbExp=3; IntAct=EBI-2875665, EBI-1564678;
CC Q96B67; P16144: ITGB4; NbExp=3; IntAct=EBI-2875665, EBI-948678;
CC Q96B67; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-2875665, EBI-399246;
CC Q96B67; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-2875665, EBI-10288852;
CC Q96B67; P46934: NEDD4; NbExp=3; IntAct=EBI-2875665, EBI-726944;
CC Q96B67; Q96PU5-2: NEDD4L; NbExp=5; IntAct=EBI-2875665, EBI-6955201;
CC Q96B67; Q96CV9: OPTN; NbExp=3; IntAct=EBI-2875665, EBI-748974;
CC Q96B67; Q96DC9: OTUB2; NbExp=8; IntAct=EBI-2875665, EBI-746259;
CC Q96B67; O43189: PHF1; NbExp=5; IntAct=EBI-2875665, EBI-530034;
CC Q96B67; P54646: PRKAA2; NbExp=3; IntAct=EBI-2875665, EBI-1383852;
CC Q96B67; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-2875665, EBI-14093916;
CC Q96B67; P63244: RACK1; NbExp=3; IntAct=EBI-2875665, EBI-296739;
CC Q96B67; Q9NS91: RAD18; NbExp=3; IntAct=EBI-2875665, EBI-2339393;
CC Q96B67; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2875665, EBI-358489;
CC Q96B67; O75886: STAM2; NbExp=6; IntAct=EBI-2875665, EBI-373258;
CC Q96B67; P21580: TNFAIP3; NbExp=6; IntAct=EBI-2875665, EBI-527670;
CC Q96B67; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-2875665, EBI-74615;
CC Q96B67; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-2875665, EBI-5235829;
CC Q96B67; P62987: UBA52; NbExp=3; IntAct=EBI-2875665, EBI-357304;
CC Q96B67; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-2875665, EBI-749370;
CC Q96B67; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-2875665, EBI-7353612;
CC Q96B67; P51668: UBE2D1; NbExp=5; IntAct=EBI-2875665, EBI-743540;
CC Q96B67; P62837: UBE2D2; NbExp=5; IntAct=EBI-2875665, EBI-347677;
CC Q96B67; Q96LR5: UBE2E2; NbExp=8; IntAct=EBI-2875665, EBI-2129763;
CC Q96B67; Q969T4: UBE2E3; NbExp=7; IntAct=EBI-2875665, EBI-348496;
CC Q96B67; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2875665, EBI-947187;
CC Q96B67; Q9NZC7-5: WWOX; NbExp=8; IntAct=EBI-2875665, EBI-12040603;
CC Q96B67; Q9H0M0: WWP1; NbExp=3; IntAct=EBI-2875665, EBI-742157;
CC Q96B67; O00308: WWP2; NbExp=5; IntAct=EBI-2875665, EBI-743923;
CC Q96B67; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2875665, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16269462,
CC ECO:0000269|PubMed:23208550}. Cell membrane
CC {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325,
CC ECO:0000269|PubMed:23208550}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325}; Cytoplasmic
CC side {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325}.
CC Lysosome {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}.
CC Endosome {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:23208550}.
CC Early endosome {ECO:0000269|PubMed:20559325,
CC ECO:0000269|PubMed:23208550}. Note=Associated with plasma membrane, as
CC well as with endosomes and lysosomes during endocytosis
CC (PubMed:16269462, PubMed:23208550, PubMed:20559325).
CC {ECO:0000269|PubMed:16269462, ECO:0000269|PubMed:20559325,
CC ECO:0000269|PubMed:23208550}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, placenta,
CC kidney, lung, liver, blood, adrenal gland, lymph node, mammary gland,
CC thyroid, and trachea (PubMed:16269462, PubMed:21982743). Very low
CC levels in colon, thymus, spleen, small intestine, bladder and bone
CC marrow (PubMed:16269462). Strong expression in differentiated
CC adipocytes compared to preadipocytes (PubMed:16269462). Detected in
CC omental fat and subcutaneous fat tissue (PubMed:21982743).
CC {ECO:0000269|PubMed:16269462}.
CC -!- INDUCTION: By troglitazone and pioglitazone (selective PPARG agonists),
CC by prostaglandin J2 (PGJ2) and by L165,041 (a PPARD ligand), by vitamin
CC D3 and, to a lesser extent, by phorbol myristate acetate (PMA) in the
CC promyelocytic leukemia HL-60 cells. No induction by retinoic acid, nor
CC by clofibrate (a specific PPARA agonist) (PubMed:16269462). Up-
CC regulated by fasting (PubMed:21982743). {ECO:0000269|PubMed:16269462,
CC ECO:0000269|PubMed:21982743}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037797; BAA92614.1; ALT_INIT; mRNA.
DR EMBL; AK291753; BAF84442.1; -; mRNA.
DR EMBL; BC015928; AAH15928.1; -; mRNA.
DR EMBL; BC053619; AAH53619.1; -; mRNA.
DR CCDS; CCDS34202.1; -.
DR RefSeq; NP_065852.1; NM_020801.3.
DR PDB; 4N7H; X-ray; 1.70 A; B=342-354.
DR PDB; 4R7V; X-ray; 1.73 A; A=1-165.
DR PDB; 4R7X; X-ray; 2.61 A; A/B=1-180.
DR PDBsum; 4N7H; -.
DR PDBsum; 4R7V; -.
DR PDBsum; 4R7X; -.
DR AlphaFoldDB; Q96B67; -.
DR SMR; Q96B67; -.
DR BioGRID; 121616; 75.
DR IntAct; Q96B67; 59.
DR MINT; Q96B67; -.
DR STRING; 9606.ENSP00000265138; -.
DR TCDB; 8.A.136.1.11; the beta-arrestin (arrb) family.
DR iPTMnet; Q96B67; -.
DR PhosphoSitePlus; Q96B67; -.
DR BioMuta; ARRDC3; -.
DR DMDM; 74731205; -.
DR EPD; Q96B67; -.
DR jPOST; Q96B67; -.
DR MassIVE; Q96B67; -.
DR MaxQB; Q96B67; -.
DR PaxDb; Q96B67; -.
DR PeptideAtlas; Q96B67; -.
DR PRIDE; Q96B67; -.
DR ProteomicsDB; 76051; -.
DR Antibodypedia; 57571; 150 antibodies from 27 providers.
DR DNASU; 57561; -.
DR Ensembl; ENST00000265138.4; ENSP00000265138.3; ENSG00000113369.9.
DR GeneID; 57561; -.
DR KEGG; hsa:57561; -.
DR MANE-Select; ENST00000265138.4; ENSP00000265138.3; NM_020801.4; NP_065852.1.
DR UCSC; uc003kjz.3; human.
DR CTD; 57561; -.
DR DisGeNET; 57561; -.
DR GeneCards; ARRDC3; -.
DR HGNC; HGNC:29263; ARRDC3.
DR HPA; ENSG00000113369; Low tissue specificity.
DR MIM; 612464; gene.
DR neXtProt; NX_Q96B67; -.
DR OpenTargets; ENSG00000113369; -.
DR PharmGKB; PA134925765; -.
DR VEuPathDB; HostDB:ENSG00000113369; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000155411; -.
DR HOGENOM; CLU_039221_1_1_1; -.
DR InParanoid; Q96B67; -.
DR OMA; WFLPVKL; -.
DR OrthoDB; 817924at2759; -.
DR PhylomeDB; Q96B67; -.
DR TreeFam; TF313650; -.
DR PathwayCommons; Q96B67; -.
DR SignaLink; Q96B67; -.
DR BioGRID-ORCS; 57561; 27 hits in 1085 CRISPR screens.
DR ChiTaRS; ARRDC3; human.
DR GenomeRNAi; 57561; -.
DR Pharos; Q96B67; Tbio.
DR PRO; PR:Q96B67; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96B67; protein.
DR Bgee; ENSG00000113369; Expressed in adrenal tissue and 186 other tissues.
DR Genevisible; Q96B67; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031699; F:beta-3 adrenergic receptor binding; IDA:MGI.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0031649; P:heat generation; IEA:Ensembl.
DR GO; GO:0071878; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0031651; P:negative regulation of heat generation; IEA:Ensembl.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IPI:MGI.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
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 3D-structure; Cell membrane; Cytoplasm; Endosome; Lysosome; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..414
FT /note="Arrestin domain-containing protein 3"
FT /id="PRO_0000244349"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 346..349
FT /note="PPxY motif 1"
FT /evidence="ECO:0000305"
FT MOTIF 391..394
FT /note="PPxY motif 2"
FT /evidence="ECO:0000305"
FT MUTAGEN 48
FT /note="K->E: Abolishes interaction with ADRB2; when
FT associated with E-52; E-85 and E-139."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 52
FT /note="R->E: Abolishes interaction with ADRB2; when
FT associated with E-48; E-85 and E-139."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 56
FT /note="K->E: Nearly abolishes interaction with ADRB2; when
FT associated with E-58; E-135 and E-153."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 58
FT /note="R->E: Nearly abolishes interaction with ADRB2; when
FT associated with E-56; E-135 and E-153."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 85
FT /note="K->E: Abolishes interaction with ADRB2; when
FT associated with E-48; E-52 and E-139."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 135
FT /note="R->E: Nearly abolishes interaction with ADRB2; when
FT associated with E-56; E-58 and E-153."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 139
FT /note="K->E: Abolishes interaction with ADRB2; when
FT associated with E-48; E-52 and E-85."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 153
FT /note="K->E: Nearly abolishes interaction with ADRB2; when
FT associated with E-56; E-58 and E-135."
FT /evidence="ECO:0000269|PubMed:25220262"
FT MUTAGEN 346..349
FT /note="PPSY->AASA: Strongly reduces interaction with NEDD4.
FT Abolishes interaction with NEDD4; when associated with 391-
FT A--A-394. Abolishes interaction with HGS; when associated
FT with 391-A--A-394."
FT /evidence="ECO:0000269|PubMed:20559325,
FT ECO:0000269|PubMed:23208550"
FT MUTAGEN 391..394
FT /note="PPLY->AALA: Abolishes interaction with NEDD4; when
FT associated with 346-A--A-349."
FT /evidence="ECO:0000269|PubMed:20559325"
FT CONFLICT 12
FT /note="S -> G (in Ref. 2; BAF84442)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 42..61
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 73..90
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:4R7V"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4R7V"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4N7H"
SQ 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
