AKAP5_RAT
ID AKAP5_RAT Reviewed; 714 AA.
AC P24587; P70593;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
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 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].
RA Takai Y., Irie M., Toyada A., Hata Y.;
RT "Characterization of rat AKAP150.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 251-714.
RC TISSUE=Brain;
RX PubMed=2538452; DOI=10.1016/s0021-9258(18)83792-9;
RA Bregman D.B., Bhattacharyya N., Rubin C.S.;
RT "High affinity binding protein for the regulatory subunit of cAMP-dependent
RT protein kinase II-B. Cloning, characterization, and expression of cDNAs for
RT rat brain P150.";
RL J. Biol. Chem. 264:4648-4656(1989).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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).
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 (By similarity). Binds dimer of the RII-beta regulatory
CC subunit of cAMP-dependent protein kinase. {ECO:0000250}.
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 plays 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; U67136; AAB07887.1; -; mRNA.
DR EMBL; J04597; AAA50420.1; -; mRNA.
DR PIR; A32461; A32461.
DR AlphaFoldDB; P24587; -.
DR SMR; P24587; -.
DR CORUM; P24587; -.
DR IntAct; P24587; 1.
DR MINT; P24587; -.
DR STRING; 10116.ENSRNOP00000008416; -.
DR iPTMnet; P24587; -.
DR PhosphoSitePlus; P24587; -.
DR SwissPalm; P24587; -.
DR PaxDb; P24587; -.
DR PRIDE; P24587; -.
DR UCSC; RGD:620829; rat.
DR RGD; 620829; Akap5.
DR eggNOG; ENOG502S1NI; Eukaryota.
DR InParanoid; P24587; -.
DR PhylomeDB; P24587; -.
DR PRO; PR:P24587; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:SynGO-UCL.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:SynGO-UCL.
DR GO; GO:0031527; C:filopodium membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:RGD.
DR GO; GO:0050811; F:GABA receptor binding; IDA:RGD.
DR GO; GO:0035254; F:glutamate receptor binding; IPI:SynGO-UCL.
DR GO; GO:0019900; F:kinase binding; IDA:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:SynGO-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:SynGO-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0036394; P:amylase secretion; ISO:RGD.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
DR GO; GO:0070073; P:clustering of voltage-gated calcium channels; ISO:RGD.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0043271; P:negative regulation of ion transport; IMP:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:RGD.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0032984; P:protein-containing complex disassembly; IDA:RGD.
DR GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
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..714
FT /note="A-kinase anchor protein 5"
FT /id="PRO_0000064516"
FT REPEAT 305..312
FT /note="1; approximate"
FT REPEAT 322..329
FT /note="2; approximate"
FT REPEAT 330..337
FT /note="3; approximate"
FT REPEAT 350..357
FT /note="4; approximate"
FT REPEAT 358..365
FT /note="5; approximate"
FT REPEAT 366..373
FT /note="6; approximate"
FT REPEAT 398..405
FT /note="7; approximate"
FT REPEAT 414..421
FT /note="8; approximate"
FT REPEAT 430..437
FT /note="9"
FT REPEAT 438..445
FT /note="10"
FT REPEAT 446..453
FT /note="11"
FT REPEAT 454..461
FT /note="12"
FT REPEAT 462..469
FT /note="13"
FT REPEAT 470..477
FT /note="14; approximate"
FT REPEAT 486..493
FT /note="15; approximate"
FT REPEAT 494..501
FT /note="16"
FT REPEAT 502..509
FT /note="17"
FT REPEAT 510..517
FT /note="18"
FT REPEAT 518..525
FT /note="19"
FT REPEAT 526..533
FT /note="20; approximate"
FT REPEAT 534..541
FT /note="21"
FT REPEAT 542..549
FT /note="22; approximate"
FT REPEAT 550..557
FT /note="23; approximate"
FT REPEAT 558..565
FT /note="24; approximate"
FT REPEAT 566..573
FT /note="25"
FT REPEAT 574..581
FT /note="26; approximate"
FT REPEAT 582..589
FT /note="27; approximate"
FT REPEAT 590..597
FT /note="28; approximate"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..164
FT /note="Essential to the intracellular anchoring function"
FT /evidence="ECO:0000250"
FT REGION 243..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..597
FT /note="28 X 8 AA repeats of V-G-Q-A-E-E-A-T"
FT REGION 675..696
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 115..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3YVF0"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 123
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 251
FT /note="S -> G (in Ref. 2; AAA50420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 75962 MW; 933ED7E0CD236AEA CRC64;
METSVSEIQI ETKDEKRPEA ASPQKERQER KTATLCFKRR KKVNKKKAKA GSKTAEETEK
HAPEAGGSGQ RQPAGAWASI KRLVTHRKPS ESAEKQKPSE AEMQPEDGAL PKKKTKSKLK
IPCIRFSRGA KRSRPSKLTE DSGYVRVQGE ADDLEIKAQI QPDEQATQAK STQGLQEDVI
VRDGKEIQES HISNNVISGE HVIGIELELE KESSALRMRT PGSEKEAKVI LVKQGVQVQE
ASVLENSAAD SPQPVTSTAP LSPATTHQLG LEEPSDSIRE SAPSGKDDGR RKTAAEEKKS
GETALGQAEE ASSVSQADKS VLSQAEEATV GHTEEATVIQ AQSQAKEGKL SQAEEATVAQ
AKETVLSQAE EVKLSQIEEP AISQAKKATV GQAKEAYVSQ AEEAIVGHTE KATMGQAEEA
TVGHIEKTTV GQAEEATVGQ AEEATVGQAE EATVGQAEEA TVGQAEEATV GQAGEATVSH
IEKTTVGQAE EAIVGQAEEA TVGQAEEATV GQAEEATVGQ AEEATVDQAE EATVGQAEEA
TVGQAGEAAV GQAEEAIVAQ AEEATVGQAG EATVGQAEKA TVGQAEEPIV GQAEETVLRH
ASDLKVNGVD AEKPRSEESK RMEPIAIIIT DTEISEFDVK KSKNVPKQFL ISMENEQVGV
FANDSDFEGR TSEQYETLLI ETASSLVKNA IELSVEQLVN EMVSEDNQIN TLFQ
