AKA7G_MOUSE
ID AKA7G_MOUSE Reviewed; 314 AA.
AC Q7TN79; F8VQ58;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=A-kinase anchor protein 7 isoform gamma {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000312|EMBL:AAP55205.1};
DE Short=AKAP-7 isoform gamma {ECO:0000250|UniProtKB:Q9P0M2};
DE AltName: Full=A-kinase anchor protein 18 {ECO:0000250|UniProtKB:O55074};
DE Short=AKAP-18 {ECO:0000250|UniProtKB:O55074};
DE AltName: Full=Protein kinase A-anchoring protein 7 isoform gamma {ECO:0000250|UniProtKB:Q9P0M2};
DE Short=PRKA7 isoform gamma {ECO:0000250|UniProtKB:Q9P0M2};
GN Name=Akap7 {ECO:0000312|Ensembl:ENSMUSP00000043624,
GN ECO:0000312|MGI:MGI:1859150};
GN Synonyms=Akap18 {ECO:0000250|UniProtKB:Q9P0M2};
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] {ECO:0000305, ECO:0000312|EMBL:AAP55205.1}
RP NUCLEOTIDE SEQUENCE [MRNA], RI-ALPHA-BINDING, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF LYS-41; LYS-43; LEU-265 AND LEU-269.
RC STRAIN=C57BL/6J x SJL/J {ECO:0000312|EMBL:AAP55205.1};
RC TISSUE=Oocyte {ECO:0000269|PubMed:12804576};
RX PubMed=12804576; DOI=10.1016/s0006-291x(03)00982-3;
RA Brown R.L., August S.L., Williams C.J., Moss S.B.;
RT "AKAP7gamma is a nuclear RI-binding AKAP.";
RL Biochem. Biophys. Res. Commun. 306:394-401(2003).
RN [2] {ECO:0000312|Ensembl:ENSMUSP00000043624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000043624};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Probably targets cAMP-dependent protein kinase (PKA) to the
CC cellular membrane or cytoskeletal structures. The membrane-associated
CC form reduces epithelial sodium channel (ENaC) activity, whereas the
CC free cytoplasmic form may negatively regulate ENaC channel feedback
CC inhibition by intracellular sodium (By similarity).
CC {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000305}.
CC -!- SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with
CC PRKCA; only the cytoplasmic form is capable of interacting with PRKCA
CC (By similarity). {ECO:0000250|UniProtKB:Q9P0M2,
CC ECO:0000269|PubMed:12804576}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12804576}. Cytoplasm
CC {ECO:0000269|PubMed:12804576}. Note=In oocytes, localizes to the
CC nucleus, to germinal vesicles and throughout the cytoplasm.
CC {ECO:0000269|PubMed:12804576}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Gamma {ECO:0000269|PubMed:12804576};
CC IsoId=Q7TN79-1; Sequence=Displayed;
CC Name=Alpha {ECO:0000305};
CC IsoId=O55074-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC {ECO:0000269|PubMed:12804576}.
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DR EMBL; AY301068; AAP55205.1; -; mRNA.
DR EMBL; AC153549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23753.1; -. [Q7TN79-1]
DR RefSeq; NP_061217.3; NM_018747.4. [Q7TN79-1]
DR AlphaFoldDB; Q7TN79; -.
DR SMR; Q7TN79; -.
DR BioGRID; 240608; 1.
DR STRING; 10090.ENSMUSP00000043624; -.
DR iPTMnet; Q7TN79; -.
DR MaxQB; Q7TN79; -.
DR PaxDb; Q7TN79; -.
DR PeptideAtlas; Q7TN79; -.
DR PRIDE; Q7TN79; -.
DR ProteomicsDB; 296010; -. [Q7TN79-1]
DR Antibodypedia; 19674; 297 antibodies from 28 providers.
DR DNASU; 432442; -.
DR Ensembl; ENSMUST00000041984; ENSMUSP00000043624; ENSMUSG00000039166. [Q7TN79-1]
DR GeneID; 432442; -.
DR UCSC; uc007eri.1; mouse. [Q7TN79-1]
DR CTD; 9465; -.
DR MGI; MGI:1859150; Akap7.
DR VEuPathDB; HostDB:ENSMUSG00000039166; -.
DR eggNOG; KOG2814; Eukaryota.
DR GeneTree; ENSGT00390000012756; -.
DR HOGENOM; CLU_052186_0_0_1; -.
DR InParanoid; Q7TN79; -.
DR OMA; AEGDHMN; -.
DR OrthoDB; 606751at2759; -.
DR PhylomeDB; Q7TN79; -.
DR TreeFam; TF105406; -.
DR BioGRID-ORCS; 432442; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Akap7; mouse.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q7TN79; protein.
DR Bgee; ENSMUSG00000039166; Expressed in animal zygote and 224 other tissues.
DR ExpressionAtlas; Q7TN79; baseline and differential.
DR Genevisible; Q7TN79; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:MGI.
DR InterPro; IPR019511; AKAP7_RI-RII-bd_dom.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR019510; Kinase-A_anchor_nucl_local_sig.
DR Pfam; PF10469; AKAP7_NLS; 1.
DR Pfam; PF10470; AKAP7_RIRII_bdg; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..314
FT /note="A-kinase anchor protein 7 isoform gamma"
FT /id="PRO_0000419634"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..314
FT /note="PKA-RII-alpha subunit binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q6JP77"
FT REGION 261..285
FT /note="RI-alpha-binding"
FT /evidence="ECO:0000269|PubMed:12804576"
FT REGION 262..275
FT /note="RII-binding"
FT /evidence="ECO:0000250|UniProtKB:O43687"
FT REGION 281..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6JP77"
FT BINDING 95
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q6JP77"
FT BINDING 185..187
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6JP77"
FT BINDING 185..187
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q6JP77"
FT MUTAGEN 41
FT /note="K->E: Abolishes nuclear localization; when
FT associated with E-43."
FT /evidence="ECO:0000269|PubMed:12804576"
FT MUTAGEN 43
FT /note="K->E: Abolishes nuclear localization; when
FT associated with E-41."
FT /evidence="ECO:0000269|PubMed:12804576"
FT MUTAGEN 265
FT /note="L->P: Abolishes PKA-RI-alpha binding; when
FT associated with P-269."
FT /evidence="ECO:0000269|PubMed:12804576"
FT MUTAGEN 269
FT /note="L->P: Abolishes PKA-RI-alpha binding; when
FT associated with P-265."
FT /evidence="ECO:0000269|PubMed:12804576"
FT CONFLICT 70
FT /note="V -> S (in Ref. 1; AAP55205)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="V -> A (in Ref. 1; AAP55205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35482 MW; 67D7D6733D69936F CRC64;
MPFAAVDIQD DCGSPDVPQA NPKRSKEEEE DRGDKNDHVK KRKKAKKDYQ PNYFLSIPIT
NKKITTGIKV LQNSILQQDK RLTKAMVGDG SFHITLLVMQ LLNEDEVNIG TDALLELKPF
VEEILEGKHL ALPFQGIGTF QGQVGFVKLA DGDHVSALLE IAETAKRTFR EKGILAGESR
TFKPHLTFMK LSKAPMLRKK GVRKIEPGLY EQFIDHRFGE ELLYQIDLCS MLKKKQSNGY
YHCESSIVIG EKDRREPEDA ELVRLSKRLV ENAVLKAVQQ YLEETQNKKQ PGEGNSTKAE
EGDRNGDGSD NNRK
