AKAP5_BOVIN
ID AKAP5_BOVIN Reviewed; 428 AA.
AC P24275;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=A-kinase anchor protein 5;
DE Short=AKAP-5;
DE AltName: Full=A-kinase anchor protein 75 kDa;
DE Short=AKAP 75;
DE Short=P75;
DE AltName: Full=cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein;
GN Name=AKAP5; Synonyms=AKAP75;
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 [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1733921; DOI=10.1016/s0021-9258(18)45852-8;
RA Hirsch A.H., Glantz S.B., Li Y., You Y., Rubin C.S.;
RT "Cloning and expression of an intron-less gene for AKAP 75, an anchor
RT protein for the regulatory subunit of cAMP-dependent protein kinase II
RT beta.";
RL J. Biol. Chem. 267:2131-2134(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-428.
RC TISSUE=Brain;
RX PubMed=2016323; DOI=10.1016/s0021-9258(20)89631-8;
RA Bregman D.B., Hirsch A.H., Rubin C.S.;
RT "Molecular characterization of bovine brain p75, a high affinity binding
RT protein for the regulatory subunit of cAMP-dependent protein kinase II
RT beta.";
RL J. Biol. Chem. 266:7207-7213(1991).
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 -!- TISSUE SPECIFICITY: Predominantly in brain, and to a lesser extent in
CC adrenal medulla, lung and anterior pituitary.
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-129 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M82914; AAA30366.1; -; Genomic_DNA.
DR EMBL; M60292; AAA30682.1; -; mRNA.
DR PIR; A42311; A42311.
DR RefSeq; NP_776661.1; NM_174236.1.
DR AlphaFoldDB; P24275; -.
DR DIP; DIP-172N; -.
DR STRING; 9913.ENSBTAP00000012705; -.
DR PaxDb; P24275; -.
DR PRIDE; P24275; -.
DR GeneID; 281612; -.
DR KEGG; bta:281612; -.
DR CTD; 9495; -.
DR eggNOG; ENOG502S1NI; Eukaryota.
DR InParanoid; P24275; -.
DR OrthoDB; 1260618at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0008179; F:adenylate cyclase binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:InterPro.
DR InterPro; IPR042375; AKAP5.
DR InterPro; IPR001573; AKAP_WSK.
DR PANTHER; PTHR15182; PTHR15182; 1.
DR Pfam; PF03832; WSK; 1.
DR PROSITE; PS51893; AKAP_CAM_BD; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Endosome; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..428
FT /note="A-kinase anchor protein 5"
FT /id="PRO_0000064528"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..170
FT /note="Essential to the intracellular anchoring function"
FT REGION 237..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..410
FT /note="RII-beta subunit binding domain"
FT MOTIF 76..96
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 7..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 92
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 94
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT LIPID 36
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 129
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 225
FT /note="R -> T (in Ref. 2; AAA30682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47878 MW; 427E8E980D3B173E CRC64;
MEITVSEIQV ESKDETRSAE VRPQDERQEE KASMLCFKRR KKAAKAMKPK ASSKAADAAK
KCPPEARASD QPQRPGGAWD SIKRLVTRRK RSESSKQQKP FKAKLQSEIN AEDANPSKKK
AKSRLKIPCI KFSKGEKRSN HSKIIEDSDR SVKVQEAENL VTKTQTQSDD QATKSKSPQD
VREDVSQKGD DEVCESNVNN SITSPGEKVI SVELELDMGH SAIQRGTLIL EKDTEMLEEK
QSIQPQHVSP LEASDTEQEL PVGSEVPPSS AVPDQQILEE ARNGVLESGP DWKEHESREI
VVEESKPKDT ELSQELDFQE NEITAEKPKP EESKRMEPIA IIITDTEISE FDVKKSKNVP
KPFLISIENE QVGVFANDSG FEGRTSEQYE TLLIETASSL VKNAIQLSIE QLVNEMASDD
NTINNRLQ
