AKA7G_HUMAN
ID AKA7G_HUMAN Reviewed; 348 AA.
AC Q9P0M2; B4DUC3; Q9HCZ8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=A-kinase anchor protein 7 isoform gamma;
DE Short=AKAP-7 isoform gamma;
DE AltName: Full=A-kinase anchor protein 18 kDa;
DE Short=AKAP 18;
DE AltName: Full=Protein kinase A-anchoring protein 7 isoform gamma;
DE Short=PRKA7 isoform gamma;
GN Name=AKAP7; Synonyms=AKAP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF28106.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-348, FUNCTION, RII-BINDING, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=10613906; DOI=10.1083/jcb.147.7.1481;
RA Trotter K.W., Fraser I.D.C., Scott G.K., Stutts M.J., Scott J.D.,
RA Milgram S.L.;
RT "Alternative splicing regulates the subcellular localization of A-kinase
RT anchoring protein 18 isoforms.";
RL J. Cell Biol. 147:1481-1492(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH PRKCA.
RX PubMed=17244820; DOI=10.1096/fj.06-6046com;
RA Bengrine A., Li J., Awayda M.S.;
RT "The A-kinase anchoring protein 15 regulates feedback inhibition of the
RT epithelial Na+ channel.";
RL FASEB J. 21:1189-1201(2007).
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. {ECO:0000269|PubMed:10613906,
CC ECO:0000269|PubMed:17244820}.
CC -!- SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with
CC PRKCA; only the cytoplasmic form is capable of interacting with PRKCA.
CC {ECO:0000269|PubMed:17244820}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:10613906}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=Gamma;
CC IsoId=Q9P0M2-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=O43687-2; Sequence=External;
CC Name=Beta;
CC IsoId=O43687-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, pancreas and
CC placenta. {ECO:0000269|PubMed:10613906}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK300587; BAG62285.1; -; mRNA.
DR EMBL; AL136110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF152929; AAF28106.1; ALT_INIT; mRNA.
DR CCDS; CCDS5142.2; -. [Q9P0M2-1]
DR RefSeq; NP_057461.2; NM_016377.3. [Q9P0M2-1]
DR PDB; 4ZP3; X-ray; 2.63 A; M/N/O/P/Q/R=287-326.
DR PDB; 5JJ2; X-ray; 1.25 A; A=76-286.
DR PDBsum; 4ZP3; -.
DR PDBsum; 5JJ2; -.
DR AlphaFoldDB; Q9P0M2; -.
DR SMR; Q9P0M2; -.
DR BioGRID; 114851; 42.
DR IntAct; Q9P0M2; 20.
DR STRING; 9606.ENSP00000405252; -.
DR BindingDB; Q9P0M2; -.
DR iPTMnet; Q9P0M2; -.
DR PhosphoSitePlus; Q9P0M2; -.
DR BioMuta; AKAP7; -.
DR DMDM; 357528766; -.
DR EPD; Q9P0M2; -.
DR jPOST; Q9P0M2; -.
DR MassIVE; Q9P0M2; -.
DR MaxQB; Q9P0M2; -.
DR PaxDb; Q9P0M2; -.
DR PeptideAtlas; Q9P0M2; -.
DR PRIDE; Q9P0M2; -.
DR ProteomicsDB; 83578; -. [Q9P0M2-1]
DR Antibodypedia; 19674; 297 antibodies from 28 providers.
DR DNASU; 9465; -.
DR Ensembl; ENST00000431975.7; ENSP00000405252.2; ENSG00000118507.18. [Q9P0M2-1]
DR GeneID; 9465; -.
DR KEGG; hsa:9465; -.
DR MANE-Select; ENST00000431975.7; ENSP00000405252.2; NM_016377.4; NP_057461.2.
DR UCSC; uc003qck.5; human. [Q9P0M2-1]
DR CTD; 9465; -.
DR DisGeNET; 9465; -.
DR GeneCards; AKAP7; -.
DR HGNC; HGNC:377; AKAP7.
DR HPA; ENSG00000118507; Tissue enhanced (adrenal).
DR MIM; 604693; gene.
DR neXtProt; NX_Q9P0M2; -.
DR OpenTargets; ENSG00000118507; -.
DR PharmGKB; PA24671; -.
DR VEuPathDB; HostDB:ENSG00000118507; -.
DR eggNOG; KOG2814; Eukaryota.
DR GeneTree; ENSGT00390000012756; -.
DR HOGENOM; CLU_052186_0_0_1; -.
DR InParanoid; Q9P0M2; -.
DR OMA; AEGDHMN; -.
DR OrthoDB; 606751at2759; -.
DR TreeFam; TF105406; -.
DR PathwayCommons; Q9P0M2; -.
DR SignaLink; Q9P0M2; -.
DR BioGRID-ORCS; 9465; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; AKAP7; human.
DR GenomeRNAi; 9465; -.
DR Pharos; Q9P0M2; Tbio.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P0M2; protein.
DR Bgee; ENSG00000118507; Expressed in adrenal tissue and 208 other tissues.
DR ExpressionAtlas; Q9P0M2; baseline and differential.
DR Genevisible; Q9P0M2; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IBA:GO_Central.
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 3D-structure; Alternative splicing; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..348
FT /note="A-kinase anchor protein 7 isoform gamma"
FT /id="PRO_0000064523"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..348
FT /note="PKA-RII-alpha subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 295..319
FT /note="RI-alpha-binding"
FT /evidence="ECO:0000250"
FT REGION 296..309
FT /note="RII-binding"
FT REGION 316..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 219..221
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 219..221
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT VARIANT 26
FT /note="E -> K (in dbSNP:rs7771473)"
FT /id="VAR_024246"
FT VARIANT 215
FT /note="S -> N (in dbSNP:rs1190788)"
FT /id="VAR_024247"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 138..159
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:5JJ2"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:5JJ2"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:5JJ2"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:5JJ2"
FT HELIX 294..319
FT /evidence="ECO:0007829|PDB:4ZP3"
SQ SEQUENCE 348 AA; 39518 MW; 642221A7CA8730CA CRC64;
MERPEAGGIN SNECENVSRK KKMSEEFEAN TMDSLVDMPF ATVDIQDDCG ITDEPQINLK
RSQENEWVKS DQVKKRKKKR KDYQPNYFLS IPITNKEIIK GIKILQNAII QQDERLAKAM
VSDGSFHITL LVMQLLNEDE VNIGIDALLE LKPFIEELLQ GKHLTLPFQG IGTFGNQVGF
VKLAEGDHVN SLLEIAETAN RTFQEKGILV GESRSFKPHL TFMKLSKSPW LRKNGVKKID
PDLYEKFISH RFGEEILYRI DLCSMLKKKQ SNGYYHCESS IVIGEKNGGE PDDAELVRLS
KRLVENAVLK AVQQYLEETQ NKNKPGEGSS VKTEAADQNG NDNENNRK
