NEB2_RAT
ID NEB2_RAT Reviewed; 817 AA.
AC O35274;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Neurabin-2 {ECO:0000305};
DE AltName: Full=Neurabin-II;
DE AltName: Full=Neural tissue-specific F-actin-binding protein II;
DE AltName: Full=PP1bp134;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 9B;
DE AltName: Full=Spinophilin {ECO:0000303|PubMed:15743906};
DE AltName: Full=p130;
GN Name=Ppp1r9b {ECO:0000312|RGD:632281};
GN Synonyms=Spino {ECO:0000303|PubMed:15743906};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9275233; DOI=10.1073/pnas.94.18.9956;
RA Allen P.B., Ouimet C.C., Greengard P.;
RT "Spinophilin, a novel protein phosphatase 1 binding protein localized to
RT dendritic spines.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9956-9961(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 4-24; 164-182;
RP 199-242; 449-480; 678-689 AND 776-791.
RC TISSUE=Brain;
RX PubMed=9452470; DOI=10.1074/jbc.273.6.3470;
RA Satoh A., Nakanishi H., Obaishi H., Wada M., Takahashi K., Satoh K.,
RA Hirao K., Nishioka H., Hata Y., Mizoguchi A., Takai Y.;
RT "Neurabin-II/spinophilin. An actin filament-binding protein with one pdz
RT domain localized at cadherin-based cell-cell adhesion sites.";
RL J. Biol. Chem. 273:3470-3475(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-767, AND INTERACTION WITH D2DR.
RX PubMed=10391935; DOI=10.1074/jbc.274.28.19894;
RA Smith F.D., Oxford G.S., Milgram S.L.;
RT "Association of the D2 dopamine receptor third cytoplasmic loop with
RT spinophilin, a protein phosphatase-1-interacting protein.";
RL J. Biol. Chem. 274:19894-19900(1999).
RN [4]
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10585469; DOI=10.1074/jbc.274.50.35845;
RA MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S.,
RA Wadzinski B.E., Colbran R.J.;
RT "Brain actin-associated protein phosphatase 1 holoenzymes containing
RT spinophilin, neurabin, and selected catalytic subunit isoforms.";
RL J. Biol. Chem. 274:35845-35854(1999).
RN [5]
RP INTERACTION WITH TGN38.
RX PubMed=10514494; DOI=10.1074/jbc.274.42.30080;
RA Stephens D.J., Banting G.;
RT "Direct interaction of the trans-Golgi network membrane protein, TGN38,
RT with the F-actin binding protein, neurabin.";
RL J. Biol. Chem. 274:30080-30086(1999).
RN [6]
RP CHARACTERIZATION, INTERACTION WITH PP1, AND MUTAGENESIS.
RX PubMed=10194355; DOI=10.1021/bi982900m;
RA Hsieh-Wilson L.C., Allen P.B., Watanabe T., Nairn A.C., Greengard P.;
RT "Characterization of the neuronal targeting protein spinophilin and its
RT interactions with protein phosphatase-1.";
RL Biochemistry 38:4365-4373(1999).
RN [7]
RP INTERACTION WITH ADRA2A; ADRA2B AND ADRA2C.
RX PubMed=11154706; DOI=10.1074/jbc.m011679200;
RA Richman J.G., Brady A.E., Wang Q., Hensel J.L., Colbran R.J., Limbird L.E.;
RT "Agonist-regulated Interaction between alpha2-adrenergic receptors and
RT spinophilin.";
RL J. Biol. Chem. 276:15003-15008(2001).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH ACTIN AND PPP1CA, PHOSPHORYLATION AT
RP SER-94; SER-100 AND SER-177, AND MUTAGENESIS OF SER-17; SER-59; SER-87;
RP SER-94; SER-99; SER-100; SER-122; SER-126 AND SER-177.
RX PubMed=12417592; DOI=10.1074/jbc.m205754200;
RA Hsieh-Wilson L.C., Benfenati F., Snyder G.L., Allen P.B., Nairn A.C.,
RA Greengard P.;
RT "Phosphorylation of spinophilin modulates its interaction with actin
RT filaments.";
RL J. Biol. Chem. 278:1186-1194(2003).
RN [9]
RP INTERACTION WITH TIAM1 AND RASGRF1.
RX PubMed=12531897; DOI=10.1074/jbc.m207876200;
RA Buchsbaum R.J., Connolly B.A., Feig L.A.;
RT "Regulation of p70 S6 kinase by complex formation between the Rac guanine
RT nucleotide exchange factor (Rac-GEF) Tiam1 and the scaffold spinophilin.";
RL J. Biol. Chem. 278:18833-18841(2003).
RN [10]
RP INTERACTION WITH ACTIN.
RX PubMed=15135218; DOI=10.1016/j.molbrainres.2003.12.020;
RA Barnes A.P., Smith F.D. III, VanDongen H.M., VanDongen A.M., Milgram S.L.;
RT "The identification of a second actin-binding region in
RT spinophilin/neurabin II.";
RL Brain Res. Mol. Brain Res. 124:105-113(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15514983; DOI=10.1002/cne.20313;
RA Ouimet C.C., Katona I., Allen P., Freund T.F., Greengard P.;
RT "Cellular and subcellular distribution of spinophilin, a PP1 regulatory
RT protein that bundles F-actin in dendritic spines.";
RL J. Comp. Neurol. 479:374-388(2004).
RN [12]
RP PHOSPHORYLATION BY CAMK2, PHOSPHORYLATION AT SER-100 AND SER-116, AND
RP MUTAGENESIS OF SER-100 AND SER-116.
RX PubMed=15228588; DOI=10.1111/j.1471-4159.2004.02491.x;
RA Grossman S.D., Futter M., Snyder G.L., Allen P.B., Nairn A.C.,
RA Greengard P., Hsieh-Wilson L.C.;
RT "Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase
RT II resulting in regulation of its binding to F-actin.";
RL J. Neurochem. 90:317-324(2004).
RN [13]
RP FUNCTION IN DENDRITIC SPINE MORPHOGENESIS, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PPP1R2.
RX PubMed=15743906; DOI=10.1091/mbc.e04-12-1054;
RA Terry-Lorenzo R.T., Roadcap D.W., Otsuka T., Blanpied T.A., Zamorano P.L.,
RA Garner C.C., Shenolikar S., Ehlers M.D.;
RT "Neurabin/protein phosphatase-1 complex regulates dendritic spine
RT morphogenesis and maturation.";
RL Mol. Biol. Cell 16:2349-2362(2005).
RN [14]
RP FUNCTION, AND INTERACTION WITH RGS1; RGS2; RGS4; RGS19; ADRA1B.
RX PubMed=15793568; DOI=10.1038/ncb1237;
RA Wang X., Zeng W., Soyombo A.A., Tang W., Ross E.M., Barnes A.P.,
RA Milgram S.L., Penninger J.M., Allen P.B., Greengard P., Muallem S.;
RT "Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of
RT RGS2 and the third intracellular loop of G-protein-coupled receptors.";
RL Nat. Cell Biol. 7:405-411(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 417-583 IN COMPLEX WITH HUMAN
RP PP1CA.
RX PubMed=20305656; DOI=10.1038/nsmb.1786;
RA Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.;
RT "Spinophilin directs protein phosphatase 1 specificity by blocking
RT substrate binding sites.";
RL Nat. Struct. Mol. Biol. 17:459-464(2010).
CC -!- FUNCTION: Seems to act as a scaffold protein in multiple signaling
CC pathways. Modulates excitatory synaptic transmission and dendritic
CC spine morphology. Binds to actin filaments (F-actin) and shows cross-
CC linking activity. Binds along the sides of the F-actin. May play an
CC important role in linking the actin cytoskeleton to the plasma membrane
CC at the synaptic junction. Believed to target protein phosphatase 1/PP1
CC to dendritic spines, which are rich in F-actin, and regulates its
CC specificity toward ion channels and other substrates, such as AMPA-type
CC and NMDA-type glutamate receptors. Plays a role in regulation of G-
CC protein coupled receptor signaling, including dopamine D2 receptors and
CC alpha-adrenergic receptors. May establish a signaling complex for
CC dopaminergic neurotransmission through D2 receptors by linking
CC receptors downstream signaling molecules and the actin cytoskeleton.
CC Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling.
CC May confer to Rac signaling specificity by binding to both, RacGEFs and
CC Rac effector proteins. Probably regulates p70 S6 kinase activity by
CC forming a complex with TIAM1. Required for hepatocyte growth factor
CC (HGF)-induced cell migration (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15743906, ECO:0000269|PubMed:15793568}.
CC -!- SUBUNIT: Interacts with DCLK2 (By similarity). Possibly exists as a
CC homodimer, homotrimer or a homotetramer. Interacts with F-actin,
CC PPP1CA, neurabin-1, TGN38 and D(2) dopamine receptor. Interacts with
CC RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A,
CC PPP1R2, RASGFR1 and TIAM1. Interacts (via C-terminus) with SPATA13 (via
CC C-terminal tail) (By similarity). Interacts with ADRA2B (By
CC similarity). {ECO:0000250|UniProtKB:Q6R891,
CC ECO:0000250|UniProtKB:Q96SB3}.
CC -!- INTERACTION:
CC O35274; P61169: Drd2; NbExp=2; IntAct=EBI-80022, EBI-80012;
CC O35274; P63088: Ppp1cc; NbExp=3; IntAct=EBI-80022, EBI-80049;
CC O35274; P62136: PPP1CA; Xeno; NbExp=8; IntAct=EBI-80022, EBI-357253;
CC O35274; P29350: PTPN6; Xeno; NbExp=2; IntAct=EBI-80022, EBI-78260;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus {ECO:0000250}.
CC Postsynaptic density {ECO:0000269|PubMed:15514983}. Cell junction,
CC adherens junction. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:15514983}. Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
CC projection, filopodium {ECO:0000250}. Cell projection, ruffle membrane
CC {ECO:0000250}. Note=Enriched at synapse and cadherin-based cell-cell
CC adhesion sites. In neurons, both cytosolic and membrane-associated, and
CC highly enriched in the postsynaptic density apposed to exitatory
CC synapses (PubMed:15514983). Colocalizes with PPP1R2 at actin-rich
CC adherens junctions in epithelial cells and in dendritic spines.
CC Accumulates in the lamellipodium, filopodium and ruffle membrane in
CC response to hepatocyte growth factor (HGF) treatment (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15514983}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Abundantly expressed in the brain.
CC Expressed at highest levels in hippocampus and at lower levels in the
CC cortex, cerebellum and brainstem. Localizes to the dendritic spines of
CC neurons. Also localizes to aspiny neurons, such as GABAergic
CC interneurons.
CC -!- DEVELOPMENTAL STAGE: Expression is low during embryogenesis and
CC increases around postnatal day 21.
CC -!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
CC binding, it acquires structure, blocks a substrate-binding site, and
CC restricts PP1 phosphatase specificity to a subset of substrates.
CC -!- PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94
CC and Ser-177 phosphorylation. Dephosphorylation of these residues is
CC mediated by PP1 and possibly PP2A. Spinophilin unphosphorylated or
CC phosphorylated at Ser-94 is concentrated in the postsynaptic density,
CC whereas spinophilin phosphorylated at Ser-177 is absent from the
CC postsynaptic density and enriched in the cytosol. Phosphorylation of
CC spinophilin disrupts its association with F-actin, but does not affect
CC its binding to PP1. {ECO:0000269|PubMed:12417592,
CC ECO:0000269|PubMed:15228588}.
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DR EMBL; AF016252; AAB72005.1; -; mRNA.
DR EMBL; AF027181; AAC05183.1; -; Genomic_DNA.
DR PIR; T03852; T03852.
DR RefSeq; NP_445926.1; NM_053474.1.
DR PDB; 2G5M; NMR; -; B=493-602.
DR PDB; 3EGG; X-ray; 1.85 A; C/D=417-583.
DR PDB; 3EGH; X-ray; 2.00 A; C/D=417-583.
DR PDBsum; 2G5M; -.
DR PDBsum; 3EGG; -.
DR PDBsum; 3EGH; -.
DR AlphaFoldDB; O35274; -.
DR BMRB; O35274; -.
DR SMR; O35274; -.
DR BioGRID; 250040; 29.
DR CORUM; O35274; -.
DR DIP; DIP-30882N; -.
DR IntAct; O35274; 8.
DR MINT; O35274; -.
DR STRING; 10116.ENSRNOP00000005498; -.
DR iPTMnet; O35274; -.
DR PhosphoSitePlus; O35274; -.
DR jPOST; O35274; -.
DR PaxDb; O35274; -.
DR PRIDE; O35274; -.
DR Ensembl; ENSRNOT00000089497; ENSRNOP00000074026; ENSRNOG00000052113.
DR GeneID; 84686; -.
DR KEGG; rno:84686; -.
DR UCSC; RGD:632281; rat.
DR CTD; 84687; -.
DR RGD; 632281; Ppp1r9b.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000158833; -.
DR HOGENOM; CLU_007401_1_0_1; -.
DR InParanoid; O35274; -.
DR OMA; AHKEEVD; -.
DR OrthoDB; 128743at2759; -.
DR PhylomeDB; O35274; -.
DR EvolutionaryTrace; O35274; -.
DR PRO; PR:O35274; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000052113; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; O35274; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:1990780; C:cytoplasmic side of dendritic spine plasma membrane; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:RGD.
DR GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0030042; P:actin filament depolymerization; IEP:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0071315; P:cellular response to morphine; ISS:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0003006; P:developmental process involved in reproduction; IEP:RGD.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0007612; P:learning; IEP:RGD.
DR GO; GO:0060179; P:male mating behavior; IEP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:RGD.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1903829; P:positive regulation of protein localization; IDA:RGD.
DR GO; GO:1904372; P:positive regulation of protein localization to actin cortical patch; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:RGD.
DR GO; GO:1903119; P:protein localization to actin cytoskeleton; IMP:RGD.
DR GO; GO:1990778; P:protein localization to cell periphery; IMP:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0061458; P:reproductive system development; IEP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0097338; P:response to clozapine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:1904373; P:response to kainic acid; IEP:RGD.
DR GO; GO:1904386; P:response to L-phenylalanine derivative; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0034695; P:response to prostaglandin E; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR DisProt; DP00943; -.
DR Gene3D; 2.30.42.10; -; 1.
DR IDEAL; IID50058; -.
DR InterPro; IPR029921; NEB2.
DR InterPro; IPR040645; Neurabin-1/2_PDZ.
DR InterPro; IPR043446; Neurabin-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16154; PTHR16154; 1.
DR PANTHER; PTHR16154:SF24; PTHR16154:SF24; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17817; PDZ_5; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Direct protein sequencing; Membrane; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..817
FT /note="Neurabin-2"
FT /id="PRO_0000071509"
FT DOMAIN 496..584
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..154
FT /note="Actin-binding"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..371
FT /note="Interaction with D(2) dopamine receptor"
FT REGION 117..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..282
FT /note="Actin-binding"
FT REGION 169..255
FT /note="Interaction with ADRA2A, ADRA2B and ADRA2C"
FT /evidence="ECO:0000269|PubMed:11154706"
FT REGION 216..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..494
FT /note="Interaction with protein phosphatase 1"
FT REGION 480..525
FT /note="Interaction with RGS2"
FT /evidence="ECO:0000269|PubMed:15793568"
FT REGION 595..816
FT /note="Interaction with TGN38"
FT /evidence="ECO:0000269|PubMed:10514494"
FT COILED 595..616
FT /evidence="ECO:0000255"
FT COILED 665..816
FT /evidence="ECO:0000255"
FT MOTIF 447..451
FT /note="PP1-binding motif"
FT /evidence="ECO:0000269|PubMed:20305656"
FT COMPBIAS 286..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R891"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R891"
FT MOD_RES 94
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:12417592"
FT MOD_RES 100
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:12417592,
FT ECO:0000269|PubMed:15228588, ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:15228588"
FT MOD_RES 177
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:12417592"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MUTAGEN 17
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 59
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 87
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 94
FT /note="S->A: Diminishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 99
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 100
FT /note="S->A: Diminishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592,
FT ECO:0000269|PubMed:15228588"
FT MUTAGEN 116
FT /note="S->A: Diminishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:15228588"
FT MUTAGEN 122
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 126
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 177
FT /note="S->A: Diminishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:12417592"
FT MUTAGEN 447..451
FT /note="Missing: Abolishes protein phosphatase 1 binding."
FT /evidence="ECO:0000269|PubMed:10194355"
FT MUTAGEN 451
FT /note="F->A: Abolishes protein phosphatase 1 binding."
FT /evidence="ECO:0000269|PubMed:10194355"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:3EGG"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:3EGG"
FT HELIX 476..489
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 505..513
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 521..531
FT /evidence="ECO:0007829|PDB:3EGG"
FT HELIX 536..540
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:3EGG"
FT HELIX 562..571
FT /evidence="ECO:0007829|PDB:3EGG"
FT STRAND 574..582
FT /evidence="ECO:0007829|PDB:3EGG"
SQ SEQUENCE 817 AA; 89646 MW; D31D3E94EE2FFB6A CRC64;
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY GSNVHRIKSM
FLQMGTTTGP PGEAGGASGM AEAPRASDRG VRLSLPRASS LNENVDHSAL LKLGTSVSER
VSRFDSKPAP SAQPAPPPHP PSRLQETRKL FERSVPAASG GDKEAVARRL LRQERASLQD
RKLDVVVRFN GSTEALDKLD ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN
SKLVTKRSRV FQPPPPPPAP SGDAATEKDR GPGGQQPPQH RVAPARPPPK PREVRKIKPV
EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTTATTASP APEEPKAEAV PEEEASSSVA
TLERGVDNGR APDMAPEEVD ESKKEDFSEA DLVDVSAYSG LGEDSGGSAL EEDDEEDEED
GEPPYEPESG CVEIPGLSEE EDPAPSRKIH FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS
AEYELEKRVE RLELFPVELE KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD
GRIQVNDLLV EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL AENEDALSPV
EMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG RWRVEKAQLE QSVEENKERM
EKLEGYWGEA QSLCQAVDEH LRETQAQYQA LERKYSKAKR LIKDYQQKEI EFLKKETAQR
RVLEESELAR KEEMDKLLDK ISELEGNLQT LRNSNST
