ID   ADRB2_MOUSE             Reviewed;         418 AA.
AC   P18762; Q8BH38;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Beta-2 adrenergic receptor;
DE   AltName: Full=Beta-2 adrenoreceptor;
DE            Short=Beta-2 adrenoceptor;
GN   Name=Adrb2; Synonyms=Adrb2r;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=2834198; DOI=10.1002/j.1460-2075.1988.tb02792.x;
RA   Allen J.M., Baetge E.E., Abrass I.B., Palmiter R.D.;
RT   "Isoproterenol response following transfection of the mouse beta 2-
RT   adrenergic receptor gene into Y1 cells.";
RL   EMBO J. 7:133-138(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2549959; DOI=10.1042/bj2600053;
RA   Nakada M.T., Haskell K.M., Ecker D.J., Stadel J.M., Crooke S.T.;
RT   "Genetic regulation of beta 2-adrenergic receptors in 3T3-L1 fibroblasts.";
RL   Biochem. J. 260:53-59(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
CC   -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC       activation of adenylate cyclase through the action of G proteins. The
CC       beta-2-adrenergic receptor binds epinephrine with an approximately 30-
CC       fold greater affinity than it does norepinephrine.
CC       {ECO:0000269|PubMed:2834198}.
CC   -!- SUBUNIT: Binds NHERF1 and GPRASP1. Interacts with ARRB1 and ARRB2.
CC       Interacts with SRC (By similarity). Interacts with USP20 and USP33 (By
CC       similarity). Interacts with VHL; the interaction, which is increased on
CC       hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation.
CC       Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating
CC       VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding
CC       motif) with SNX27 (via PDZ domain); the interaction is required when
CC       endocytosed to prevent degradation in lysosomes and promote recycling
CC       to the plasma membrane. Interacts with CNIH4. Interacts with ARRDC3.
CC       Interacts with NEDD4 (By similarity). Interacts with MARCHF2 (By
CC       similarity). {ECO:0000250|UniProtKB:P07550}.
CC   -!- INTERACTION:
CC       P18762; P34971: Adrb1; NbExp=2; IntAct=EBI-491143, EBI-7764182;
CC       P18762; P51637: Cav3; NbExp=2; IntAct=EBI-491143, EBI-298576;
CC       P18762; P70424: Erbb2; NbExp=3; IntAct=EBI-491143, EBI-2945468;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2834198};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early
CC       endosome {ECO:0000250|UniProtKB:P07550}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL at the cell
CC       membrane. Activated receptors are internalized into endosomes prior to
CC       their degradation in lysosomes. Activated receptors are also detected
CC       within the Golgi apparatus. {ECO:0000250|UniProtKB:P07550}.
CC   -!- PTM: Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by
CC       anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes
CC       depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which
CC       mediates homologous desensitization of the receptor. PKA-mediated
CC       phosphorylation seems to facilitate phosphorylation by BARK.
CC   -!- PTM: Phosphorylation of Tyr-141 is induced by insulin and leads to
CC       supersensitization of the receptor. {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated. Agonist-induced ubiquitination leads to sort
CC       internalized receptors to the lysosomes for degradation.
CC       Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and
CC       resensitization after prolonged agonist stimulation. USP20 and USP33
CC       are constitutively associated and are dissociated immediately after
CC       agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is
CC       oxygen-dependent (By similarity). {ECO:0000250}.
CC   -!- PTM: Hydroxylation by EGLN3 occurs only under normoxia and increases
CC       the interaction with VHL and the subsequent ubiquitination and
CC       degradation of ADRB2. {ECO:0000250}.
CC   -!- PTM: Palmitoylated. Mainly palmitoylated at Cys-341. Palmitoylation may
CC       reduce accessibility of phosphorylation sites by anchoring the receptor
CC       to the plasma membrane. Agonist stimulation promotes depalmitoylation
CC       and further allows Ser-345 and Ser-346 phosphorylation. Also undergoes
CC       transient, ligand-induced palmitoylation at Cys-265 probably by ZDHHC9,
CC       ZDHHC14 and ZDHHC18 within the Golgi. Palmitoylation at Cys-265
CC       requires phosphorylation by PKA and receptor internalization and
CC       stabilizes the receptor. Could be depalmitoylated by LYPLA1 at the
CC       plasma membrane. {ECO:0000250|UniProtKB:P07550}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB2 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X15643; CAA33664.1; -; Genomic_DNA.
DR   EMBL; AK080241; BAC37856.1; -; mRNA.
DR   EMBL; CH466528; EDL09746.1; -; Genomic_DNA.
DR   EMBL; BC032883; AAH32883.1; -; mRNA.
DR   CCDS; CCDS29289.1; -.
DR   PIR; S00260; S00260.
DR   RefSeq; NP_031446.2; NM_007420.3.
DR   AlphaFoldDB; P18762; -.
DR   SMR; P18762; -.
DR   CORUM; P18762; -.
DR   DIP; DIP-59568N; -.
DR   IntAct; P18762; 9.
DR   MINT; P18762; -.
DR   STRING; 10090.ENSMUSP00000062256; -.
DR   BindingDB; P18762; -.
DR   ChEMBL; CHEMBL3707; -.
DR   DrugCentral; P18762; -.
DR   GlyCosmos; P18762; 2 sites, No reported glycans.
DR   GlyGen; P18762; 2 sites.
DR   iPTMnet; P18762; -.
DR   PhosphoSitePlus; P18762; -.
DR   SwissPalm; P18762; -.
DR   jPOST; P18762; -.
DR   PaxDb; 10090-ENSMUSP00000062256; -.
DR   ProteomicsDB; 296071; -.
DR   Antibodypedia; 15959; 1320 antibodies from 44 providers.
DR   DNASU; 11555; -.
DR   Ensembl; ENSMUST00000053640.5; ENSMUSP00000062256.4; ENSMUSG00000045730.5.
DR   GeneID; 11555; -.
DR   KEGG; mmu:11555; -.
DR   UCSC; uc008fcy.2; mouse.
DR   AGR; MGI:87938; -.
DR   CTD; 154; -.
DR   MGI; MGI:87938; Adrb2.
DR   VEuPathDB; HostDB:ENSMUSG00000045730; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000159538; -.
DR   HOGENOM; CLU_009579_11_0_1; -.
DR   InParanoid; P18762; -.
DR   OMA; HNVTQER; -.
DR   OrthoDB; 2900736at2759; -.
DR   PhylomeDB; P18762; -.
DR   TreeFam; TF316350; -.
DR   Reactome; R-MMU-390696; Adrenoceptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 11555; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Adrb2; mouse.
DR   PRO; PR:P18762; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P18762; Protein.
DR   Bgee; ENSMUSG00000045730; Expressed in granulocyte and 139 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0043235; C:receptor complex; ISS:HGNC-UCL.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0008179; F:adenylate cyclase binding; IDA:BHF-UCL.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0031713; F:B2 bradykinin receptor binding; ISO:MGI.
DR   GO; GO:0004941; F:beta2-adrenergic receptor activity; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0051380; F:norepinephrine binding; ISS:HGNC-UCL.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0090722; F:receptor-receptor interaction; ISO:MGI.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:HGNC-UCL.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0071875; P:adrenergic receptor signaling pathway; ISO:MGI.
DR   GO; GO:0008306; P:associative learning; ISO:MGI.
DR   GO; GO:0045453; P:bone resorption; IMP:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IGI:MGI.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0002032; P:desensitization of G protein-coupled receptor signaling pathway by arrestin; ISS:HGNC-UCL.
DR   GO; GO:0002086; P:diaphragm contraction; ISO:MGI.
DR   GO; GO:0002024; P:diet induced thermogenesis; IGI:MGI.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0031649; P:heat generation; IGI:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; IGI:MGI.
DR   GO; GO:0035811; P:negative regulation of urine volume; ISO:MGI.
DR   GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:GO_Central.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR   GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR   GO; GO:1904504; P:positive regulation of lipophagy; ISS:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
DR   GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; IGI:ARUK-UCL.
DR   GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR   GO; GO:0010739; P:positive regulation of protein kinase A signaling; IGI:ARUK-UCL.
DR   GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISO:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0003059; P:positive regulation of the force of heart contraction by epinephrine; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC-UCL.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
DR   GO; GO:0001993; P:regulation of systemic arterial blood pressure by norepinephrine-epinephrine; IMP:MGI.
DR   GO; GO:0071869; P:response to catecholamine; ISO:MGI.
DR   GO; GO:0009409; P:response to cold; IGI:MGI.
DR   GO; GO:0006939; P:smooth muscle contraction; IGI:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0042311; P:vasodilation; ISO:MGI.
DR   CDD; cd15957; 7tmA_Beta2_AR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000332; ADRB2_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF21; BETA-2 ADRENERGIC RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00562; ADRENRGCB2AR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P18762; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW   Glycoprotein; Golgi apparatus; Hydroxylation; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..418
FT                   /note="Beta-2 adrenergic receptor"
FT                   /id="PRO_0000069134"
FT   TOPO_DOM        1..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        35..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        59..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        72..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        96..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        107..129
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        130..150
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        151..174
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        175..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        197..220
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        221..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        275..298
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        299..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        306..329
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        330..418
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           415..418
FT                   /note="PDZ-binding"
FT   MOD_RES         141
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   MOD_RES         261
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         262
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         345
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   MOD_RES         346
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   MOD_RES         355
FT                   /note="Phosphoserine; by BARK"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         356
FT                   /note="Phosphoserine; by BARK"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         387
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         400
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   LIPID           265
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   LIPID           341
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P07550"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        106..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        184..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        21
FT                   /note="D -> H (in Ref. 2; CAA33664)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94..95
FT                   /note="IL -> TS (in Ref. 2; CAA33664)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="S -> T (in Ref. 2; CAA33664)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347..348
FT                   /note="SK -> FE (in Ref. 2; CAA33664)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  46998 MW;  51D1EC73D7619D58 CRC64;
     MGPHGNDSDF LLAPNGSRAP DHDVTQERDE AWVVGMAILM SVIVLAIVFG NVLVITAIAK
     FERLQTVTNY FIISLACADL VMGLAVVPFG ASHILMKMWN FGNFWCEFWT SIDVLCVTAS
     IETLCVIAVD RYVAITSPFK YQSLLTKNKA RVVILMVWIV SGLTSFLPIQ MHWYRATHKK
     AIDCYTEETC CDFFTNQAYA IASSIVSFYV PLVVMVFVYS RVFQVAKRQL QKIDKSEGRF
     HAQNLSQVEQ DGRSGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIRD
     NLIPKEVYIL LNWLGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSSKTY GNGYSSNSNG
     RTDYTGEPNT CQLGQEREQE LLCEDPPGME GFVNCQGTVP SLSVDSQGRN CSTNDSPL
//