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Database: UniProt
Entry: AKA7G_MOUSE
LinkDB: AKA7G_MOUSE
Original site: 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   07-NOV-2018, entry version 100.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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,
RP   TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-41; LYS-43; LEU-265 AND
RP   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Probably targets cAMP-dependent protein kinase (PKA) to
CC       the cellular membrane or cytoskeletal structures. The membrane-
CC       associated form reduces epithelial sodium channel (ENaC) activity,
CC       whereas the free cytoplasmic form may negatively regulate ENaC
CC       channel feedback inhibition by intracellular sodium (By
CC       similarity). {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
CC       PRKCA (By similarity). {ECO:0000250|UniProtKB:Q9P0M2,
CC       ECO:0000269|PubMed:12804576}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12804576}.
CC       Cytoplasm {ECO:0000269|PubMed:12804576}. Note=In oocytes,
CC       localizes to the nucleus, to germinal vesicles and throughout the
CC       cytoplasm. {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}.
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   UniGene; Mm.485937; -.
DR   UniGene; Mm.487103; -.
DR   ProteinModelPortal; 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   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   eggNOG; KOG2814; Eukaryota.
DR   eggNOG; ENOG4111FMP; LUCA.
DR   GeneTree; ENSGT00390000012756; -.
DR   HOGENOM; HOG000294077; -.
DR   HOVERGEN; HBG050475; -.
DR   InParanoid; Q7TN79; -.
DR   OMA; KLSKAPW; -.
DR   OrthoDB; EOG091G0771; -.
DR   TreeFam; TF105406; -.
DR   ChiTaRS; Akap7; mouse.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000039166; Expressed in 234 organ(s), highest expression level in cerebral cortex.
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:0032947; F:protein-containing complex scaffold activity; ISO: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; cNuc_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; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    314       A-kinase anchor protein 7 isoform gamma.
FT                                /FTId=PRO_0000419634.
FT   NP_BIND     185    187       AMP. {ECO:0000250|UniProtKB:Q6JP77}.
FT   NP_BIND     185    187       CMP. {ECO:0000250|UniProtKB:Q6JP77}.
FT   REGION      260    314       PKA-RII-alpha subunit binding domain.
FT                                {ECO:0000250|UniProtKB:Q6JP77}.
FT   REGION      261    285       RI-alpha-binding.
FT                                {ECO:0000269|PubMed:12804576}.
FT   REGION      262    275       RII-binding.
FT                                {ECO:0000250|UniProtKB:O43687}.
FT   BINDING      95     95       AMP. {ECO:0000250|UniProtKB:Q6JP77}.
FT   BINDING      95     95       CMP. {ECO:0000250|UniProtKB:Q6JP77}.
FT   MUTAGEN      41     41       K->E: Abolishes nuclear localization;
FT                                when associated with E-43.
FT                                {ECO:0000269|PubMed:12804576}.
FT   MUTAGEN      43     43       K->E: Abolishes nuclear localization;
FT                                when associated with E-41.
FT                                {ECO:0000269|PubMed:12804576}.
FT   MUTAGEN     265    265       L->P: Abolishes PKA-RI-alpha binding;
FT                                when associated with P-269.
FT                                {ECO:0000269|PubMed:12804576}.
FT   MUTAGEN     269    269       L->P: Abolishes PKA-RI-alpha binding;
FT                                when associated with P-265.
FT                                {ECO:0000269|PubMed:12804576}.
FT   CONFLICT     70     70       V -> S (in Ref. 1; AAP55205).
FT                                {ECO:0000305}.
FT   CONFLICT    278    278       V -> A (in Ref. 1; AAP55205).
FT                                {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
//
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