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A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 150 kDa) (AKAP 150) (P150) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein)

 AKAP5_RAT               Reviewed;         714 AA.
P24587; P70593;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
05-DEC-2018, entry version 119.
RecName: Full=A-kinase anchor protein 5;
Short=AKAP-5;
AltName: Full=A-kinase anchor protein 150 kDa;
Short=AKAP 150;
Short=P150;
AltName: Full=cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein;
Name=Akap5; Synonyms=Akap150;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Takai Y., Irie M., Toyada A., Hata Y.;
"Characterization of rat AKAP150.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 251-714.
TISSUE=Brain;
PubMed=2538452;
Bregman D.B., Bhattacharyya N., Rubin C.S.;
"High affinity binding protein for the regulatory subunit of cAMP-
dependent protein kinase II-B. Cloning, characterization, and
expression of cDNAs for rat brain P150.";
J. Biol. Chem. 264:4648-4656(1989).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: May anchor the PKA kinase to cytoskeletal and/or
organelle-associated proteins, targeting the signal carried by
cAMP to specific intracellular effectors.
-!- SUBUNIT: Interacts with ADCY8, and enhances its phosphorylation at
lipid rafts (By similarity). Binds dimer of the RII-beta
regulatory subunit of cAMP-dependent protein kinase.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}. Note=Associates with lipid rafts. {ECO:0000250}.
-!- DOMAIN: The N-terminal region, which is highly basic, is required
for interaction with calmodulin. {ECO:0000250}.
-!- PTM: Palmitoylation at Cys-36 and Cys-123 plays a key role in
targeting to lipid rafts. {ECO:0000250}.
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EMBL; U67136; AAB07887.1; -; mRNA.
EMBL; J04597; AAA50420.1; -; mRNA.
PIR; A32461; A32461.
UniGene; Rn.122003; -.
UniGene; Rn.215609; -.
SMR; P24587; -.
CORUM; P24587; -.
IntAct; P24587; 1.
MINT; P24587; -.
STRING; 10116.ENSRNOP00000008416; -.
iPTMnet; P24587; -.
PhosphoSitePlus; P24587; -.
SwissPalm; P24587; -.
PaxDb; P24587; -.
PRIDE; P24587; -.
UCSC; RGD:620829; rat.
RGD; 620829; Akap5.
eggNOG; ENOG410IIWH; Eukaryota.
eggNOG; ENOG4111833; LUCA.
InParanoid; P24587; -.
PhylomeDB; P24587; -.
PRO; PR:P24587; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:SynGO-UCL.
GO; GO:0032590; C:dendrite membrane; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0032591; C:dendritic spine membrane; IDA:RGD.
GO; GO:0060076; C:excitatory synapse; IDA:SynGO-UCL.
GO; GO:0031527; C:filopodium membrane; IDA:RGD.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0003779; F:actin binding; IDA:RGD.
GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL.
GO; GO:0045296; F:cadherin binding; IPI:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0001664; F:G protein-coupled receptor binding; IPI:RGD.
GO; GO:0050811; F:GABA receptor binding; IDA:RGD.
GO; GO:0035254; F:glutamate receptor binding; IPI:SynGO-UCL.
GO; GO:0019900; F:kinase binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IDA:RGD.
GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:SynGO-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:SynGO-UCL.
GO; GO:0043624; P:cellular protein complex disassembly; IDA:RGD.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0043271; P:negative regulation of ion transport; IMP:RGD.
GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:RGD.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:RGD.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:RGD.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0006605; P:protein targeting; IEA:InterPro.
GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0014850; P:response to muscle activity; IEP:RGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
InterPro; IPR001573; Pkinase-A_anch_WSK-motif.
Pfam; PF03832; WSK; 1.
1: Evidence at protein level;
Calmodulin-binding; Complete proteome; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 714 A-kinase anchor protein 5.
/FTId=PRO_0000064516.
DOMAIN 72 101 AKAP.
REPEAT 305 312 1; approximate.
REPEAT 322 329 2; approximate.
REPEAT 330 337 3; approximate.
REPEAT 350 357 4; approximate.
REPEAT 358 365 5; approximate.
REPEAT 366 373 6; approximate.
REPEAT 398 405 7; approximate.
REPEAT 414 421 8; approximate.
REPEAT 430 437 9.
REPEAT 438 445 10.
REPEAT 446 453 11.
REPEAT 454 461 12.
REPEAT 462 469 13.
REPEAT 470 477 14; approximate.
REPEAT 486 493 15; approximate.
REPEAT 494 501 16.
REPEAT 502 509 17.
REPEAT 510 517 18.
REPEAT 518 525 19.
REPEAT 526 533 20; approximate.
REPEAT 534 541 21.
REPEAT 542 549 22; approximate.
REPEAT 550 557 23; approximate.
REPEAT 558 565 24; approximate.
REPEAT 566 573 25.
REPEAT 574 581 26; approximate.
REPEAT 582 589 27; approximate.
REPEAT 590 597 28; approximate.
REGION 1 164 Essential to the intracellular anchoring
function. {ECO:0000250}.
REGION 305 597 28 X 8 AA repeats of V-G-Q-A-E-E-A-T.
REGION 675 696 RII-beta subunit binding domain.
{ECO:0000250}.
COMPBIAS 326 595 Glu-rich.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:D3YVF0}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 36 36 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 123 123 S-palmitoyl cysteine. {ECO:0000250}.
CONFLICT 251 251 S -> G (in Ref. 2; AAA50420).
{ECO:0000305}.
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


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