ARRB1_BOVIN
ID ARRB1_BOVIN Reviewed; 418 AA.
AC P17870;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Beta-arrestin-1;
DE AltName: Full=Arrestin beta-1;
DE AltName: Full=Arrestin-2;
GN Name=ARRB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2163110; DOI=10.1126/science.2163110;
RA Lohse M.J., Benovic J.L., Codina J., Caron M.G., Lefkowitz R.J.;
RT "Beta-arrestin: a protein that regulates beta-adrenergic receptor
RT function.";
RL Science 248:1547-1550(1990).
RN [2]
RP FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION.
RX PubMed=1349018; DOI=10.1016/s0021-9258(18)42479-9;
RA Lohse M.J., Andexinger S., Pitcher J., Trukawinski S., Codina J.,
RA Faure J.P., Caron M.G., Lefkowitz R.J.;
RT "Receptor-specific desensitization with purified proteins. Kinase
RT dependence and receptor specificity of beta-arrestin and arrestin in the
RT beta 2-adrenergic receptor and rhodopsin systems.";
RL J. Biol. Chem. 267:8558-8564(1992).
RN [3]
RP ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=8340388; DOI=10.1016/s0021-9258(18)82304-3;
RA Sterne-Marr R., Gurevich V.V., Goldsmith P., Bodine R.C., Sanders C.,
RA Donoso L.A., Benovic J.L.;
RT "Polypeptide variants of beta-arrestin and arrestin3.";
RL J. Biol. Chem. 268:15640-15648(1993).
RN [4]
RP INTERACTION WITH ADRB2 AND CHRM2.
RX PubMed=7822302; DOI=10.1074/jbc.270.2.720;
RA Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M.,
RA Sterne-Marr R., Hosey M.M., Benovic J.L.;
RT "Arrestin interactions with G protein-coupled receptors. Direct binding
RT studies of wild type and mutant arrestins with rhodopsin, beta 2-
RT adrenergic, and m2 muscarinic cholinergic receptors.";
RL J. Biol. Chem. 270:720-731(1995).
RN [5]
RP PHOSPHOINOSITIDE-BINDING.
RX PubMed=10022830; DOI=10.1093/emboj/18.4.871;
RA Gaidarov I., Krupnick J.G., Falck J.R., Benovic J.L., Keen J.H.;
RT "Arrestin function in G protein-coupled receptor endocytosis requires
RT phosphoinositide binding.";
RL EMBO J. 18:871-881(1999).
RN [6]
RP FUNCTION IN DESENSITIZATION OF LHCGR.
RX PubMed=9892661; DOI=10.1073/pnas.96.2.493;
RA Mukherjee S., Palczewski K., Gurevich V.V., Benovic J.L., Banga J.P.,
RA Hunzicker-Dunn M.;
RT "A direct role for arrestins in desensitization of the luteinizing
RT hormone/choriogonadotropin receptor in porcine ovarian follicular
RT membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:493-498(1999).
RN [7]
RP INTERACTION WITH LHCGR.
RX PubMed=11867621; DOI=10.1074/jbc.m110479200;
RA Mukherjee S., Gurevich V.V., Preninger A., Hamm H.E., Bader M.-F.,
RA Fazleabas A.T., Birnbaumer L., Hunzicker-Dunn M.;
RT "Aspartic acid 564 in the third cytoplasmic loop of the luteinizing
RT hormone/choriogonadotropin receptor is crucial for phosphorylation-
RT independent interaction with arrestin2.";
RL J. Biol. Chem. 277:17916-17927(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CYTH2 AND CASR.
RX PubMed=17623778; DOI=10.1242/jcs.03469;
RA Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M.;
RT "The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO
RT ARF6 ELMO protein network.";
RL J. Cell Sci. 120:2489-2497(2007).
RN [9]
RP FUNCTION IN INTERNALIZATION OF P2Y PURINOCEPTORS, AND SUBCELLULAR LOCATION.
RX PubMed=18703513; DOI=10.1074/jbc.m801472200;
RA Hoffmann C., Ziegler N., Reiner S., Krasel C., Lohse M.J.;
RT "Agonist-selective, receptor-specific interaction of human P2Y receptors
RT with beta-arrestin-1 and -2.";
RL J. Biol. Chem. 283:30933-30941(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-393, AND INTERACTION WITH CHRM2.
RX PubMed=11566136; DOI=10.1016/s0969-2126(01)00644-x;
RA Han M., Gurevich V.V., Vishnivetskiy S.A., Sigler P.B., Schubert C.;
RT "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of
RT receptor binding and membrane translocation.";
RL Structure 9:869-880(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), INTERACTION WITH AP2B1 AND CLTC, AND
RP MUTAGENESIS OF PHE-391; ARG-395 AND LEU-396.
RX PubMed=11876640; DOI=10.1021/bi015905j;
RA Milano S.K., Pace H.C., Kim Y.-M., Brenner C., Benovic J.L.;
RT "Scaffolding functions of arrestin-2 revealed by crystal structure and
RT mutagenesis.";
RL Biochemistry 41:3321-3328(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT, INSP6-BINDING, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-157; LYS-160; ARG-161; LYS-232; ARG-236;
RP LYS-250; LYS-324 AND LYS-326.
RX PubMed=16439357; DOI=10.1074/jbc.m512703200;
RA Milano S.K., Kim Y.-M., Stefano F.P., Benovic J.L., Brenner C.;
RT "Nonvisual arrestin oligomerization and cellular localization are regulated
RT by inositol hexakisphosphate binding.";
RL J. Biol. Chem. 281:9812-9823(2006).
CC -!- FUNCTION: Functions in regulating agonist-mediated G-protein coupled
CC receptor (GPCR) signaling by mediating both receptor desensitization
CC and resensitization processes. During homologous desensitization, beta-
CC arrestins bind to the GPRK-phosphorylated receptor and sterically
CC preclude its coupling to the cognate G-protein; the binding appears to
CC require additional receptor determinants exposed only in the active
CC receptor conformation. The beta-arrestins target many receptors for
CC internalization by acting as endocytic adapters (CLASPs, clathrin-
CC associated sorting proteins) and recruiting the GPRCs to the adapter
CC protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the
CC extent of beta-arrestin involvement appears to vary significantly
CC depending on the receptor, agonist and cell type. Internalized
CC arrestin-receptor complexes traffic to intracellular endosomes, where
CC they remain uncoupled from G-proteins. Two different modes of arrestin-
CC mediated internalization occur. Class A receptors, like ADRB2, OPRM1,
CC ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the
CC plasma membrane and undergo rapid recycling. Class B receptors, like
CC AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with
CC arrestin and traffic with it to endosomal vesicles, presumably as
CC desensitized receptors, for extended periods of time. Receptor
CC resensitization then requires that receptor-bound arrestin is removed
CC so that the receptor can be dephosphorylated and returned to the plasma
CC membrane. Involved in internalization of P2RY4 and UTP-stimulated
CC internalization of P2RY2. Involved in phosphorylation-dependent
CC internalization of OPRD1 ands subsequent recycling. Involved in the
CC degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-
CC activated receptors. Beta-arrestins function as multivalent adapter
CC proteins that can switch the GPCR from a G-protein signaling mode that
CC transmits short-lived signals from the plasma membrane via small
CC molecule second messengers and ion channels to a beta-arrestin
CC signaling mode that transmits a distinct set of signals that are
CC initiated as the receptor internalizes and transits the intracellular
CC compartment. Acts as signaling scaffold for MAPK pathways such as
CC MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is
CC largely excluded from the nucleus and confined to cytoplasmic locations
CC such as endocytic vesicles, also called beta-arrestin signalosomes.
CC Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for
CC which the beta-arrestin-mediated signaling relies on both ARRB1 and
CC ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some
CC GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or
CC ARRB2 and is inhibited by the other respective beta-arrestin form
CC (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-
CC mediated activation (reciprocal regulation). Is required for SP-
CC stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized
CC NK1R resulting in ERK1/2 activation, which is required for the
CC antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-
CC mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway.
CC Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in
CC IGF1-stimulated AKT1 signaling leading to increased protection from
CC apoptosis. Involved in activation of the p38 MAPK signaling pathway and
CC in actin bundle formation. Involved in F2RL1-mediated cytoskeletal
CC rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber
CC formation by acting together with GNAQ to activate RHOA. Appears to
CC function as signaling scaffold involved in regulation of MIP-1-beta-
CC stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-
CC kappa-B-dependent transcription in response to GPCR or cytokine
CC stimulation by interacting with and stabilizing CHUK. May serve as
CC nuclear messenger for GPCRs. Involved in OPRD1-stimulated
CC transcriptional regulation by translocating to CDKN1B and FOS promoter
CC regions and recruiting EP300 resulting in acetylation of histone H4.
CC Involved in regulation of LEF1 transcriptional activity via interaction
CC with DVL1 and/or DVL2 Also involved in regulation of receptors other
CC than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling
CC through the interaction with TRAF6 which prevents TRAF6
CC autoubiquitination and oligomerization required for activation of NF-
CC kappa-B and JUN. Involved in IL8-mediated granule release in
CC neutrophils. Binds phosphoinositides. Binds inositol hexakisphosphate
CC (InsP6) (By similarity). Required for atypical chemokine receptor
CC ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin
CC (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to
CC cell membrane, increasing its efficiency in chemokine uptake and
CC degradation. Involved in the internalization of the atypical chemokine
CC receptor ACKR3 (By similarity). Negatively regulates the NOTCH
CC signaling pathway by mediating the ubiquitination and degradation of
CC NOTCH1 by ITCH. Participates in the recruitment of the ubiquitin-
CC protein ligase to the receptor (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P49407, ECO:0000269|PubMed:1349018,
CC ECO:0000269|PubMed:18703513, ECO:0000269|PubMed:2163110,
CC ECO:0000269|PubMed:9892661}.
CC -!- SUBUNIT: Monomer. Homodimer. Homooligomer; the self-association is
CC mediated by InsP6-binding. Heterooligomer with ARRB2; the association
CC is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated).
CC Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts
CC with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated at 'Tyr-
CC 737'); phosphorylation of AP2B1 at 'Tyr-737' disrupts the interaction.
CC Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2
CC and GRK2. Interacts with CRR5. Interacts with PTAFR (phosphorylated on
CC serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1.
CC Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with
CC C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and
CC the protein kinase domain); the interaction is independent of the
CC phosphorylation state of SRC C-terminus. Interacts with TACR1.
CC Interacts with RAF1. Interacts with CHUK, IKBKB and MAP3K14. Interacts
CC with DVL1; the interaction is enhanced by phosphorylation of DVL1.
CC Interacts with DVL2; the interaction is enhanced by phosphorylation of
CC DVL2. Interacts with IGF1R. Associates with MAP kinase p38. Part of a
CC MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1
CC (activated) and MAPK3 (activated). Part of a MAPK signaling complex
CC consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3
CC (activated). Interacts with GPR143 (By similarity). Interacts with
CC MAP2K4/MKK4. Interacts with HCK and CXCR1 (phosphorylated) (By
CC similarity). Interacts ACKR3 and ACKR4 (By similarity). Interacts with
CC ARRDC1; the interaction is direct. Interacts with GPR61, GPR62 and
CC GPR135 (By similarity). {ECO:0000250|UniProtKB:P49407}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Membrane,
CC clathrin-coated pit {ECO:0000305}. Cell projection, pseudopodium
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to
CC the plasma membrane and colocalizes with antagonist-stimulated GPCRs.
CC The monomeric form is predominantly located in the nucleus. The
CC oligomeric form is located in the cytoplasm. Translocates to the
CC nucleus upon stimulation of OPRD1 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1A;
CC IsoId=P17870-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=P17870-2; Sequence=VSP_000321;
CC -!- TISSUE SPECIFICITY: Beta-arrestin 1A is found in cortex, cerebellum,
CC striatum, pineal gland, retina and heart. Beta-arrestin 1B is found in
CC spleen, lung, pituitary and kidney.
CC -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction
CC the AP-2 complex subunit AP2B1. Binding to phosphorylated GPCRs induces
CC a conformationanl change that exposes the motif to the surface (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminus binds InsP6 with low affinity.
CC -!- DOMAIN: The C-terminus binds InsP6 with high affinity.
CC -!- PTM: Constitutively phosphorylated at Ser-412 in the cytoplasm. At the
CC plasma membrane, is rapidly dephosphorylated, a process that is
CC required for clathrin binding and ADRB2 endocytosis but not for ADRB2
CC binding and desensitization. Once internalized, is rephosphorylated.
CC -!- PTM: The ubiquitination status appears to regulate the formation and
CC trafficking of beta-arrestin-GPCR complexes and signaling.
CC Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2;
CC the ubiquitination is required for rapid internalization of ADRB2.
CC Deubiquitinated by USP33; the deubiquitination leads to a dissociation
CC of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such
CC as ADRB2, induces transient ubiquitination and subsequently promotes
CC association with USP33 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; M33601; AAA30387.1; -; mRNA.
DR PIR; A34851; A34851.
DR RefSeq; NP_776668.1; NM_174243.3. [P17870-1]
DR PDB; 1G4M; X-ray; 1.90 A; A/B=1-393.
DR PDB; 1G4R; X-ray; 2.20 A; A=1-393.
DR PDB; 1JSY; X-ray; 2.90 A; A=1-418.
DR PDB; 1ZSH; X-ray; 2.90 A; A=1-418.
DR PDB; 2WTR; X-ray; 2.90 A; A/B=1-418.
DR PDB; 3GC3; X-ray; 2.20 A; A=1-393.
DR PDB; 3GD1; X-ray; 3.50 A; C/E=1-393.
DR PDB; 6NI2; EM; 4.00 A; B=1-393.
DR PDB; 7DF9; X-ray; 3.17 A; A=1-418.
DR PDB; 7DFA; X-ray; 2.54 A; A=1-418.
DR PDB; 7DFB; X-ray; 3.28 A; A=1-418.
DR PDB; 7DFC; X-ray; 2.49 A; A=1-418.
DR PDBsum; 1G4M; -.
DR PDBsum; 1G4R; -.
DR PDBsum; 1JSY; -.
DR PDBsum; 1ZSH; -.
DR PDBsum; 2WTR; -.
DR PDBsum; 3GC3; -.
DR PDBsum; 3GD1; -.
DR PDBsum; 6NI2; -.
DR PDBsum; 7DF9; -.
DR PDBsum; 7DFA; -.
DR PDBsum; 7DFB; -.
DR PDBsum; 7DFC; -.
DR AlphaFoldDB; P17870; -.
DR SMR; P17870; -.
DR DIP; DIP-61028N; -.
DR ELM; P17870; -.
DR IntAct; P17870; 1.
DR STRING; 9913.ENSBTAP00000027296; -.
DR BindingDB; P17870; -.
DR PaxDb; P17870; -.
DR PeptideAtlas; P17870; -.
DR PRIDE; P17870; -.
DR Ensembl; ENSBTAT00000045006; ENSBTAP00000042435; ENSBTAG00000020485. [P17870-1]
DR GeneID; 281637; -.
DR KEGG; bta:281637; -.
DR CTD; 408; -.
DR VEuPathDB; HostDB:ENSBTAG00000020485; -.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_1_1_1; -.
DR InParanoid; P17870; -.
DR OMA; LYLAHEQ; -.
DR OrthoDB; 783081at2759; -.
DR TreeFam; TF314260; -.
DR EvolutionaryTrace; P17870; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000020485; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; P17870; baseline and differential.
DR GO; GO:0030132; C:clathrin coat of coated pit; IMP:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0033130; F:acetylcholine receptor binding; IPI:CAFA.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IMP:CAFA.
DR GO; GO:0030276; F:clathrin binding; IMP:CAFA.
DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:CAFA.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:AgBase.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:AgBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:CAFA.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; TAS:AgBase.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031623; P:receptor internalization; TAS:AgBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR DisProt; DP00390; -.
DR Gene3D; 2.60.40.640; -; 1.
DR Gene3D; 2.60.40.840; -; 1.
DR InterPro; IPR000698; Arrestin.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR017864; Arrestin_CS.
DR InterPro; IPR014753; Arrestin_N.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11792; PTHR11792; 1.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR PRINTS; PR00309; ARRESTIN.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS00295; ARRESTINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome;
KW Signal transduction inhibitor; Transcription; Transcription regulation;
KW Transport; Ubl conjugation.
FT CHAIN 1..418
FT /note="Beta-arrestin-1"
FT /id="PRO_0000205193"
FT REGION 1..163
FT /note="Interaction with SRC"
FT /evidence="ECO:0000250"
FT REGION 45..86
FT /note="Interaction with CHRM2"
FT REGION 318..418
FT /note="Interaction with TRAF6"
FT /evidence="ECO:0000250"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 385..395
FT /note="[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif"
FT COMPBIAS 353..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 255
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 324
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 326
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWG8"
FT MOD_RES 412
FT /note="Phosphoserine; by GRK5"
FT /evidence="ECO:0000250|UniProtKB:P49407"
FT VAR_SEQ 334..341
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000321"
FT MUTAGEN 157
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-160 and Q-161."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 160
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-157 and Q-161."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 161
FT /note="R->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-157 and Q-160."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 232
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-236, Q-250, Q-324 and Q-326."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 236
FT /note="R->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-232, Q-250, Q-324 and Q-326."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 250
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-232, Q-236, Q-324 and Q-326."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 324
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-232, Q-236, Q-250 and Q-326."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 326
FT /note="K->Q: Impairs InsP6-binding and oligomerization;
FT when associated with Q-232, Q-236, Q-250 and Q-324."
FT /evidence="ECO:0000269|PubMed:16439357"
FT MUTAGEN 391
FT /note="F->A: Abolishes interaction with AP2B1; no effect on
FT interaction with CLTC."
FT /evidence="ECO:0000269|PubMed:11876640"
FT MUTAGEN 395
FT /note="R->E: Abolishes interaction with AP2B1; impairs
FT interaction with CLTC."
FT /evidence="ECO:0000269|PubMed:11876640"
FT MUTAGEN 396
FT /note="L->A: Impairs interaction with AP2B1; no effect on
FT interaction with CLTC."
FT /evidence="ECO:0000269|PubMed:11876640"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2WTR"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2WTR"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 52..64
FT /evidence="ECO:0007829|PDB:1G4M"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 75..88
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1G4R"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7DF9"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2WTR"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 140..153
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:7DFC"
FT STRAND 228..241
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1G4M"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7DFC"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:7DFA"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 316..329
FT /evidence="ECO:0007829|PDB:1G4M"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7DFC"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3GD1"
FT STRAND 342..352
FT /evidence="ECO:0007829|PDB:1G4M"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2WTR"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:7DFA"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1G4M"
SQ SEQUENCE 418 AA; 47132 MW; 345302C620FA3360 CRC64;
MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVEPVDGV VLVDPEYLKE RRVYVTLTCA
FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HAYPFTFEIP
PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP
QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD
ICLFNTAQYK CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL
ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP
PHREVPEHET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKEEEEDGT GSPRLNDR
