AKAP5_MOUSE
ID AKAP5_MOUSE Reviewed; 745 AA.
AC D3YVF0; D3Z5C9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=A-kinase anchor protein 5;
DE Short=AKAP-5;
DE AltName: Full=A-kinase anchor protein 150 kDa;
DE Short=AKAP 150;
DE Short=P150;
DE AltName: Full=cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein;
GN Name=Akap5; Synonyms=Akap150;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Multivalent scaffold protein that anchors the cAMP-dependent
CC protein kinase/PKA to cytoskeletal and/or organelle-associated
CC proteins, targeting the signal carried by cAMP to specific
CC intracellular effectors. Association with the beta2-adrenergic receptor
CC (beta2-AR) not only regulates beta2-AR signaling pathway, but also the
CC activation by PKA by switching off the beta2-AR signaling cascade.
CC Plays a role in long term synaptic potentiation by regulating protein
CC trafficking from the dendritic recycling endosomes to the plasma
CC membrane and controlling both structural and functional plasticity at
CC excitatory synapses. {ECO:0000250|UniProtKB:P24588}.
CC -!- SUBUNIT: Interacts with ADCY8, and enhances its phosphorylation at
CC lipid rafts. Binds dimer of the RII-beta regulatory subunit of cAMP-
CC dependent protein kinase (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC D3YVF0; P97438: Kcnk2; NbExp=4; IntAct=EBI-7091108, EBI-7091062;
CC D3YVF0; P48453: Ppp3cb; NbExp=3; IntAct=EBI-7091108, EBI-642618;
CC D3YVF0; P12367: Prkar2a; NbExp=2; IntAct=EBI-7091108, EBI-645747;
CC -!- SUBCELLULAR LOCATION: Postsynaptic recycling endosome membrane
CC {ECO:0000250|UniProtKB:P24588}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P24588}. Note=Associates with lipid rafts.
CC {ECO:0000250|UniProtKB:P24588}.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000250|UniProtKB:P24588}.
CC -!- DOMAIN: The N-terminal region, which is highly basic, is required for
CC interaction with calmodulin. {ECO:0000250|UniProtKB:P24588}.
CC -!- PTM: Palmitoylated. Palmitoylation at Cys-36 and Cys-123 play a key
CC role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2
CC is required for AKAP5 function in LTP-stimulated recycling endosome
CC exocytosis. {ECO:0000250|UniProtKB:P24588}.
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DR EMBL; AC120002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49092.1; -.
DR RefSeq; NP_001094941.1; NM_001101471.1.
DR AlphaFoldDB; D3YVF0; -.
DR BioGRID; 231964; 7.
DR ComplexPortal; CPX-1006; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
DR ComplexPortal; CPX-1113; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR ComplexPortal; CPX-1115; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
DR ComplexPortal; CPX-1117; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
DR ComplexPortal; CPX-1119; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR ComplexPortal; CPX-881; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DR IntAct; D3YVF0; 4.
DR MINT; D3YVF0; -.
DR STRING; 10090.ENSMUSP00000093270; -.
DR iPTMnet; D3YVF0; -.
DR PhosphoSitePlus; D3YVF0; -.
DR SwissPalm; D3YVF0; -.
DR MaxQB; D3YVF0; -.
DR PaxDb; D3YVF0; -.
DR PeptideAtlas; D3YVF0; -.
DR PRIDE; D3YVF0; -.
DR ProteomicsDB; 282059; -.
DR Antibodypedia; 3806; 261 antibodies from 31 providers.
DR DNASU; 238276; -.
DR Ensembl; ENSMUST00000154078; ENSMUSP00000114495; ENSMUSG00000021057.
DR GeneID; 238276; -.
DR KEGG; mmu:238276; -.
DR UCSC; uc007nya.2; mouse.
DR CTD; 9495; -.
DR MGI; MGI:2685104; Akap5.
DR VEuPathDB; HostDB:ENSMUSG00000021057; -.
DR eggNOG; ENOG502S1NI; Eukaryota.
DR GeneTree; ENSGT00390000019941; -.
DR HOGENOM; CLU_372953_0_0_1; -.
DR InParanoid; D3YVF0; -.
DR OMA; VHQEDDV; -.
DR PhylomeDB; D3YVF0; -.
DR BioGRID-ORCS; 238276; 1 hit in 72 CRISPR screens.
DR PRO; PR:D3YVF0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; D3YVF0; protein.
DR Bgee; ENSMUSG00000021057; Expressed in left lung lobe and 176 other tissues.
DR ExpressionAtlas; D3YVF0; baseline and differential.
DR Genevisible; D3YVF0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:MGI.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; IPI:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0050811; F:GABA receptor binding; ISO:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0036394; P:amylase secretion; IMP:MGI.
DR GO; GO:0070073; P:clustering of voltage-gated calcium channels; IMP:CACAO.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IDA:CACAO.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0043271; P:negative regulation of ion transport; ISO:MGI.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISO:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; ISO:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0032984; P:protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; IDA:CACAO.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:MGI.
DR InterPro; IPR042375; AKAP5.
DR InterPro; IPR001573; AKAP_WSK.
DR PANTHER; PTHR15182; PTHR15182; 2.
DR Pfam; PF03832; WSK; 1.
DR PROSITE; PS51893; AKAP_CAM_BD; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Endosome; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..745
FT /note="A-kinase anchor protein 5"
FT /id="PRO_0000414750"
FT REPEAT 304..312
FT /note="1; approximate"
FT REPEAT 320..327
FT /note="2; approximate"
FT REPEAT 328..335
FT /note="3; approximate"
FT REPEAT 348..355
FT /note="4; approximate"
FT REPEAT 356..363
FT /note="5; approximate"
FT REPEAT 364..395
FT /note="6; approximate"
FT REPEAT 420..436
FT /note="7; approximate"
FT REPEAT 445..452
FT /note="8; approximate"
FT REPEAT 461..468
FT /note="9"
FT REPEAT 469..476
FT /note="10"
FT REPEAT 477..484
FT /note="11"
FT REPEAT 485..492
FT /note="12"
FT REPEAT 493..500
FT /note="13"
FT REPEAT 501..508
FT /note="14; approximate"
FT REPEAT 517..524
FT /note="15; approximate"
FT REPEAT 525..532
FT /note="16"
FT REPEAT 533..540
FT /note="17"
FT REPEAT 541..548
FT /note="18"
FT REPEAT 549..556
FT /note="19"
FT REPEAT 557..564
FT /note="20; approximate"
FT REPEAT 565..572
FT /note="21"
FT REPEAT 573..580
FT /note="22; approximate"
FT REPEAT 581..588
FT /note="23; approximate"
FT REPEAT 589..596
FT /note="24; approximate"
FT REPEAT 597..604
FT /note="25"
FT REPEAT 605..612
FT /note="26; approximate"
FT REPEAT 613..620
FT /note="27; approximate"
FT REPEAT 621..628
FT /note="28; approximate"
FT REGION 1..164
FT /note="Essential to the intracellular anchoring function"
FT /evidence="ECO:0000250"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..628
FT /note="28 X 8 AA repeats of V-G-Q-A-E-E-A-T"
FT REGION 466..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="RII-beta subunit binding domain"
FT /evidence="ECO:0000250"
FT MOTIF 74..94
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 7..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 123
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 745 AA; 79397 MW; B0A2949CC0F52569 CRC64;
METSVSEIQV ETKDEKGPVA ASPQKERQER KTATLCFKRR KKANKTKPKA GSRTAEETKK
HTPEAGGSGQ RQPAGAWASI KGLVTHRKRS EPAKKQKPPE AEVQPEDGAL PKKKAKSRLK
FPCLRFSRGA KRSRHSKLTE DSGYVRVQGE ADDLEIKAQT QPDDQAIQAG STQGLQEGVL
VRDGKKSQES HISNSVTSGE NVIAIELELE NKSSAIQMGT PELEKETKVI TEKPSVQTQR
ASLLESSAAG SPRSVTSAAP PSPATTHQHS LEEPSNGIRE SAPSGKDDRR KTAAEEKKSG
ETALGQAEEA AVGQADKRAL SQAGEATAGH PEEATVIQAE SQAKEGKLSQ AEETTVAQAK
ETVLSQAKEG ELSQAKKATV GQAEEATIDH TEKVTVDQAE ETTVGQAEEA TVGQAGEAIL
SQAKEATVVG QAEEATVDRA EEATVGQAEE ATVGHTEKVT VDQAEEATVG QAEEATVGQA
EEATVDWAEK PTVGQAEEAT VGQAEEATVG HTEKVTVDQA EEATVGQAEE ATVGHTEKVT
VDHAEEATVG QAEEATVGQA EKVTVDHAEE ATVGQAEEAT VGQAEKVTVD HAEEATVGQA
EEATVGQAEK VTVDQAEEPT VDQAEEAISS HAPDLKENGI DTEKPRSEES KRMEPIAIII
TDTEISEFDV KKSKNVPKQF LISMENEQVG VFANDSDFEG RTSEQYETLL IETASSLVKN
AIELSVEQLV NEMVSEDNQI NTLFQ
