AK200_DROME
ID AK200_DROME Reviewed; 753 AA.
AC Q9VLL3; Q8IPF5; Q9U7E7;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=A-kinase anchor protein 200 {ECO:0000303|PubMed:10480936, ECO:0000312|FlyBase:FBgn0027932};
GN Name=Akap200 {ECO:0000303|PubMed:10480936,
GN ECO:0000312|FlyBase:FBgn0027932};
GN Synonyms=MESR2 {ECO:0000312|FlyBase:FBgn0027932};
GN ORFNames=CG13388 {ECO:0000312|FlyBase:FBgn0027932};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAD47200.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, INTERACTION WITH
RP PKA-R2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD47200.1};
RX PubMed=10480936; DOI=10.1074/jbc.274.38.27191;
RA Li Z., Rossi E.A., Hoheisel J.D., Kalderon D., Rubin C.S.;
RT "Generation of a novel A kinase anchor protein and a myristoylated alanine-
RT rich C kinase substrate-like analog from a single gene.";
RL J. Biol. Chem. 274:27191-27200(1999).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAQ23606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23606.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAQ23606.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PKA-R2; F-ACTIN AND CAM, SUBCELLULAR LOCATION,
RP MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-132; SER-135 AND SER-137,
RP AND MUTAGENESIS OF 1-MET--LYS-7; SER-132; SER-135; SER-137; ALA-515;
RP 518-ILE-VAL-519 AND THR-523.
RX PubMed=10480937; DOI=10.1074/jbc.274.38.27201;
RA Rossi E.A., Li Z., Feng H., Rubin C.S.;
RT "Characterization of the targeting, binding, and phosphorylation site
RT domains of an A kinase anchor protein and a myristoylated alanine-rich C
RT kinase substrate-like analog that are encoded by a single gene.";
RL J. Biol. Chem. 274:27201-27210(1999).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12223401; DOI=10.1242/dev.129.19.4423;
RA Jackson S.M., Berg C.A.;
RT "An A-kinase anchoring protein is required for protein kinase A regulatory
RT subunit localization and morphology of actin structures during oogenesis in
RT Drosophila.";
RL Development 129:4423-4433(2002).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23929551; DOI=10.1177/0748730413497179;
RA Duvall L.B., Taghert P.H.;
RT "E and M circadian pacemaker neurons use different PDF receptor signalosome
RT components in drosophila.";
RL J. Biol. Rhythms 28:239-248(2013).
RN [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ETHANOL, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 1-MET--LYS-7; SER-132; SER-135 AND SER-137.
RX PubMed=29444420; DOI=10.1016/j.celrep.2018.01.049;
RA Parkhurst S.J., Adhikari P., Navarrete J.S., Legendre A., Manansala M.,
RA Wolf F.W.;
RT "Perineurial Barrier Glia Physically Respond to Alcohol in an Akap200-
RT Dependent Manner to Promote Tolerance.";
RL Cell Rep. 22:1647-1656(2018).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH N, AND DISRUPTION PHENOTYPE.
RX PubMed=29309414; DOI=10.1371/journal.pgen.1007153;
RA Bala Tannan N., Collu G., Humphries A.C., Serysheva E., Weber U.,
RA Mlodzik M.;
RT "AKAP200 promotes Notch stability by protecting it from Cbl/lysosome-
RT mediated degradation in Drosophila melanogaster.";
RL PLoS Genet. 14:E1007153-E1007153(2018).
CC -!- FUNCTION: Scaffolding protein involved in the regulation of PKA
CC signaling and anchoring to the actin cytoskeleton integrating signals
CC propagated by cAMP, diacylglycerol and calcium (PubMed:10480936,
CC PubMed:10480937, PubMed:12223401). Contributes to the maintenance and
CC regulation of cytoskeletal structures in germline via PKA-mediated
CC signaling (PubMed:12223401). As part of ethanol response in the glia,
CC mediates ethanol-induced structural remodeling of actin cytoskeleton
CC and perineurial membrane topology by anchoring PKA to the membrane of
CC perineurial glia (PubMed:29444420). In specific tissues such as eye and
CC thorax, promotes N/Notch protein stability by inhibiting Cbl-mediated
CC ubiquitination and lysosomal degradation pathway of N/Notch in a PKA-
CC independent way (PubMed:29309414). In the circadian brain neurons
CC evening cells (E-cells), might have a role in circadian pacemaker
CC synchronization by playing a redundant role in signaling downstream of
CC the G protein-couple receptor Pdfr (PubMed:23929551).
CC {ECO:0000269|PubMed:10480936, ECO:0000269|PubMed:10480937,
CC ECO:0000269|PubMed:12223401, ECO:0000269|PubMed:23929551,
CC ECO:0000269|PubMed:29309414, ECO:0000269|PubMed:29444420}.
CC -!- SUBUNIT: Homodimer (PubMed:10480937). Interacts with Cam; interaction
CC is calcium-dependent and is inhibited by PKC-mediated phosphorylation
CC of Akap200 (PubMed:10480937). Interacts with N/Notch; the interaction
CC stabilizes N/Notch protein levels by preventing Cbl-mediated
CC ubiquitination and subsequent lysosomal degradation of N/Notch
CC (PubMed:29309414). Interacts with Pka-R2 (PubMed:10480936,
CC PubMed:10480937). Binds to F-actin; interaction is independent of
CC myristoylation, but is inhibited by Akap200 phosphorylation and Cam
CC binding (PubMed:10480937). Isoform B: Does not bind to Pka-R2
CC (PubMed:10480936). {ECO:0000269|PubMed:10480936,
CC ECO:0000269|PubMed:10480937, ECO:0000269|PubMed:29309414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10480936,
CC ECO:0000269|PubMed:10480937, ECO:0000269|PubMed:12223401}. Cell
CC membrane {ECO:0000269|PubMed:10480937, ECO:0000269|PubMed:12223401};
CC Lipid-anchor {ECO:0000269|PubMed:10480937,
CC ECO:0000269|PubMed:12223401}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:10480937}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0027932}; Synonyms=C
CC {ECO:0000312|FlyBase:FBgn0027932}, F {ECO:0000312|FlyBase:FBgn0027932},
CC Akap200L {ECO:0000269|PubMed:29444420};
CC IsoId=Q9VLL3-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0027932}; Synonyms=E
CC {ECO:0000312|FlyBase:FBgn0027932}, Akap200S
CC {ECO:0000269|PubMed:29444420};
CC IsoId=Q9VLL3-2; Sequence=VSP_059969;
CC -!- TISSUE SPECIFICITY: Detected in the brain in both neurons and glia
CC (including perineurial glia); specifically in the neuronal nuclei in
CC the cortex and synaptic neuropil (at protein level) (PubMed:29444420).
CC Detected in germline cells, somatic follicle cells and outer rim of the
CC ring canals during oogenesis (at protein level) (PubMed:12223401).
CC Isoform A: Detected in the adult (at protein level) (PubMed:10480936).
CC Isoform B: Detected in the adult with higher levels in the head (at
CC protein level) (PubMed:10480936). {ECO:0000269|PubMed:10480936,
CC ECO:0000269|PubMed:12223401, ECO:0000269|PubMed:29444420}.
CC -!- DEVELOPMENTAL STAGE: Isoform A: Detected in all stages of development,
CC with higher levels in the pupae (at protein level) (PubMed:10480936).
CC Isoform B: Detected in all stages of development (at protein level)
CC (PubMed:10480936). {ECO:0000269|PubMed:10480936}.
CC -!- INDUCTION: By ethanol. {ECO:0000269|PubMed:29444420}.
CC -!- PTM: Myristoylated; myristoylation promotes accumulation at the cell
CC periphery. {ECO:0000269|PubMed:10480937}.
CC -!- PTM: Phosphorylated; phosphorylation prevents binding to F-actin and
CC Cam. {ECO:0000269|PubMed:10480937}.
CC -!- DISRUPTION PHENOTYPE: Viable (PubMed:12223401, PubMed:29309414).
CC Results in extra notal macrochaetae often accompanied by a socket cell
CC (PubMed:12223401). In the eye, results in decreased N/Notch protein
CC levels and ommatidia defects (PubMed:29309414). In all imaginal disks
CC at early larval stages, results in supernumerary scutellar bristles and
CC loss or mispositioned microchaetae (PubMed:29309414). In the wings,
CC results in a blistered phenotype (PubMed:29309414). Females have egg
CC chambers with multinucleate cells with ring canal remnants
CC (PubMed:12223401). RNAi-mediated knockdown in glia or perineurial glia
CC reduces ethanol tolerance and locomotor sensitization possibly by
CC limiting ethanol-induced membrane topology changes; does not affect
CC perineurial morphology; does not affect glia-mediated blood-brain
CC barrier permeability (PubMed:29444420). RNAi-mediated knockdown in
CC neurons does not alter ethanol sedation sensitivity or tolerance
CC (PubMed:29444420). RNAi-mediated knockdown in the pacemaker dorsal
CC lateral neurons (LNDs) results in reduced pigment-dispersing factor
CC receptor (Pdfr)-mediated response in the circadian brain neuron evening
CC cells (E-cells) (PubMed:23929551). {ECO:0000269|PubMed:12223401,
CC ECO:0000269|PubMed:23929551, ECO:0000269|PubMed:29309414,
CC ECO:0000269|PubMed:29444420}.
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DR EMBL; AF132884; AAD47200.1; -; mRNA.
DR EMBL; AE014134; AAF52674.3; -; Genomic_DNA.
DR EMBL; AE014134; AAN10668.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10667.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54265.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54266.1; -; Genomic_DNA.
DR EMBL; BT010288; AAQ23606.1; -; mRNA.
DR RefSeq; NP_001285751.1; NM_001298822.1. [Q9VLL3-1]
DR RefSeq; NP_001285752.1; NM_001298823.1. [Q9VLL3-2]
DR RefSeq; NP_477459.1; NM_058111.4. [Q9VLL3-2]
DR RefSeq; NP_477460.1; NM_058112.4. [Q9VLL3-1]
DR RefSeq; NP_723395.1; NM_164820.2. [Q9VLL3-2]
DR AlphaFoldDB; Q9VLL3; -.
DR IntAct; Q9VLL3; 2.
DR STRING; 7227.FBpp0079282; -.
DR iPTMnet; Q9VLL3; -.
DR PRIDE; Q9VLL3; -.
DR DNASU; 34170; -.
DR EnsemblMetazoa; FBtr0079664; FBpp0079279; FBgn0027932. [Q9VLL3-1]
DR EnsemblMetazoa; FBtr0079665; FBpp0079280; FBgn0027932. [Q9VLL3-2]
DR EnsemblMetazoa; FBtr0079666; FBpp0079281; FBgn0027932. [Q9VLL3-2]
DR EnsemblMetazoa; FBtr0340239; FBpp0309213; FBgn0027932. [Q9VLL3-1]
DR EnsemblMetazoa; FBtr0340240; FBpp0309214; FBgn0027932. [Q9VLL3-2]
DR GeneID; 34170; -.
DR KEGG; dme:Dmel_CG13388; -.
DR UCSC; CG13388-RA; d. melanogaster. [Q9VLL3-1]
DR UCSC; CG13388-RB; d. melanogaster.
DR CTD; 34170; -.
DR FlyBase; FBgn0027932; Akap200.
DR VEuPathDB; VectorBase:FBgn0027932; -.
DR HOGENOM; CLU_333523_0_0_1; -.
DR PhylomeDB; Q9VLL3; -.
DR SignaLink; Q9VLL3; -.
DR BioGRID-ORCS; 34170; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Akap200; fly.
DR GenomeRNAi; 34170; -.
DR PRO; PR:Q9VLL3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027932; Expressed in wing disc and 33 other tissues.
DR ExpressionAtlas; Q9VLL3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0071361; P:cellular response to ethanol; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10480937"
FT CHAIN 2..753
FT /note="A-kinase anchor protein 200"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445798"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..148
FT /note="F-actin binding"
FT /evidence="ECO:0000269|PubMed:10480937"
FT REGION 345..725
FT /note="Interaction with PKA-R2"
FT /evidence="ECO:0000269|PubMed:10480936,
FT ECO:0000269|PubMed:10480937"
FT REGION 462..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10480937"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10480937"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10480937"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10480937"
FT VAR_SEQ 345..725
FT /note="Missing (in isoform B)"
FT /id="VSP_059969"
FT MUTAGEN 1..7
FT /note="Missing: Loss of myristoylation. Overexpression in
FT perineurial glia, leads to decreased ethanol sensitivity
FT upon initial exposure and has no effect on ethanol
FT tolerance following repeated exposure in contrast to
FT overexpression of the wild-type form, possibly by
FT delocalizing the protein from the membrane."
FT /evidence="ECO:0000269|PubMed:10480937,
FT ECO:0000269|PubMed:29444420"
FT MUTAGEN 132
FT /note="S->A: Loss of phosphorylation by PKC. Overexpression
FT in perineurial glia, results in reduced locomotor
FT sensitization when first exposed to ethanol and ethanol
FT tolerance following repeated exposure; when associated with
FT A-135 and A-137."
FT /evidence="ECO:0000269|PubMed:10480937,
FT ECO:0000269|PubMed:29444420"
FT MUTAGEN 132
FT /note="S->D: Overexpression in perineurial glia, leads to
FT decreased ethanol sensitivity upon initial exposure and has
FT no effect on ethanol tolerance following repeated exposure
FT in contrast to overexpression of the wild-type form,
FT possibly by delocalizing the protein from the membrane;
FT when associated with D-135 and D-137."
FT /evidence="ECO:0000269|PubMed:29444420"
FT MUTAGEN 135
FT /note="S->A: Partial loss of phosphorylation by PKC; when
FT associated with A-137. Overexpression in perineurial glia,
FT results in reduced locomotor sensitization when first
FT exposed to ethanol and ethanol tolerance following repeated
FT exposure; when associated with A-132 and A-137."
FT /evidence="ECO:0000269|PubMed:10480937,
FT ECO:0000269|PubMed:29444420"
FT MUTAGEN 135
FT /note="S->D: Overexpression in perineurial glia, leads to
FT decreased ethanol sensitivity upon initial exposure and has
FT no effect on ethanol tolerance following repeated exposure
FT in contrast to overexpression of the wild-type form,
FT possibly by delocalizing the protein from the membrane;
FT when associated with D-132 and D-137."
FT /evidence="ECO:0000269|PubMed:29444420"
FT MUTAGEN 137
FT /note="S->A: Partial loss of phosphorylation by PKC; when
FT associated with A-13A. Overexpression in perineurial glia,
FT results in reduced locomotor sensitization when first
FT exposed to ethanol and ethanol tolerance following repeated
FT exposure; when associated with A-132 and A-135."
FT /evidence="ECO:0000269|PubMed:10480937,
FT ECO:0000269|PubMed:29444420"
FT MUTAGEN 137
FT /note="S->D: Overexpression in perineurial glia, leads to
FT decreased ethanol sensitivity upon initial exposure and has
FT no effect on ethanol tolerance following repeated exposure
FT in contrast to overexpression of the wild-type form,
FT possibly by delocalizing the protein from the membrane;
FT when associated with D-132 and D-135."
FT /evidence="ECO:0000269|PubMed:29444420"
FT MUTAGEN 515
FT /note="A->S: Partial loss of binding to PKA-R2."
FT /evidence="ECO:0000269|PubMed:10480937"
FT MUTAGEN 518..519
FT /note="IV->AA: Loss of binding to PKA-R2."
FT /evidence="ECO:0000269|PubMed:10480937"
FT MUTAGEN 523
FT /note="T->A: Partial loss of binding to PKA-R2."
FT /evidence="ECO:0000269|PubMed:10480937"
FT CONFLICT 87
FT /note="G -> D (in Ref. 1; AAD47200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 79029 MW; 27163DE6B7187DD3 CRC64;
MGKAQSKRSI DITTDPKKVG EGDEVAGKVE KIDVDQKTDA PAVNGDAATP KEGGDEAAAV
EKKETEEHSE NDKDLTTEKS AAVAEGGDAV AETAKGEEGS PKEAAAGEDI TPLADESIKS
KSKKDKVKKK WSFRSISFGK KDKQKPAKSE EATSPTSGTT SPTTAEAEAA PAGDAAVAEP
SVATNGEAEK PAETATATSE PASKDEKPAE NGSATEQEKQ ANGETEKAAP APSTVEEAAK
PKPAEEPATV TATESNTTAT EEVPVKESQP EPEVVTNGHG AGEALTNGSS NGLAESPVTE
TAPVADNIPS NVDDEPPHQN GTNGTTTPPP TPVATEIEKG QQIEASSEVI ETVTPSQAEE
EVVAAIIKAV SSEPEAETET ETEAEGFVLV APVSTEVEVP VSISPIEPVA EVSQVKIEPL
VEIPEVEAKS VADVSEADTE SVPKVSELKT EVSEIEFESV IVETRSSSPP PPLPKSPPPS
RVSAFVLSED VIEEQVTPNV PEVNDVKPDE IEQQAISIVA EITEQAAEIV TEQEKQQEEA
KVDSVPETIE ESSSTVVVEE VLPVQNDEVT APSPTPDDVQ KPIEDQDTPD EKESYPVPDP
IDPAAVNDEV AVTEAVDCEV EKETGSISSN VAESSSVSDE QAAIENQVEI LEEQTVAVEE
TTEQETSDQQ VISEEAHSDN DKENEIDLVE NIISDLDAPI TKAGGDLLVE LDARSAEQEG
ESNNKVDLAK DLKEKNAAAA DVTTQEQLPV TCE
