AKA7G_RAT
ID AKA7G_RAT Reviewed; 353 AA.
AC Q6JP77; D3ZMQ5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=A-kinase anchor protein 7 isoforms delta and gamma;
DE Short=AKAP-7 isoforms delta and gamma;
DE AltName: Full=A-kinase anchor protein 18 {ECO:0000250|UniProtKB:F8VQ58};
DE AltName: Full=AKAP-18 {ECO:0000250|UniProtKB:F8VQ58};
DE AltName: Full=Protein kinase A-anchoring protein 7 isoforms delta and gamma;
DE Short=PRKA7 isoforms delta and gamma;
GN Name=Akap7 {ECO:0000312|RGD:1303071};
GN Synonyms=Akap18 {ECO:0000303|PubMed:15037626};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR06859.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), PKA-RII-ALPHA SUBUNIT BINDING,
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, MUTAGENESIS
RP OF LEU-308, AND FUNCTION.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAR06859.1};
RX PubMed=15037626; DOI=10.1074/jbc.m312835200;
RA Henn V., Edemir B., Stefan E., Wiesner B., Lorenz D., Theilig F.,
RA Schmitt R., Vossebein L., Tamma G., Beyermann M., Krause E., Herberg F.W.,
RA Valenti G., Bachmann S., Rosenthal W., Klussmann E.;
RT "Identification of a novel A-kinase anchoring protein 18 isoform and
RT evidence for its role in the vasopressin-induced aquaporin-2 shuttle in
RT renal principal cells.";
RL J. Biol. Chem. 279:26654-26665(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000312|EMBL:AAH98632.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH98632.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 88-292 IN COMPLEX WITH AMP AND
RP CMP.
RX PubMed=18082768; DOI=10.1016/j.jmb.2007.11.037;
RA Gold M.G., Smith F.D., Scott J.D., Barford D.;
RT "AKAP18 contains a phosphoesterase domain that binds AMP.";
RL J. Mol. Biol. 375:1329-1343(2008).
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). Isoform Delta may
CC be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane.
CC {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000269|PubMed:15037626,
CC 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 {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000269|PubMed:15037626,
CC ECO:0000269|PubMed:18082768}.
CC -!- INTERACTION:
CC Q6JP77; P61016: Pln; NbExp=6; IntAct=EBI-6096191, EBI-7620725;
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus
CC {ECO:0000250|UniProtKB:F8VQ58, ECO:0000250|UniProtKB:Q9P0M2}. Cytoplasm
CC {ECO:0000250|UniProtKB:F8VQ58, ECO:0000250|UniProtKB:Q9P0M2}.
CC -!- SUBCELLULAR LOCATION: [Isoform Delta]: Nucleus
CC {ECO:0000269|PubMed:15037626}. Cell membrane
CC {ECO:0000269|PubMed:15037626}. Note=Cotranslocates with AQP2 to the
CC plasma membrane in response to arginine-vasopressin (AVP) stimulation
CC in inner medullary collecting duct (IMCD) cells.
CC {ECO:0000269|PubMed:15037626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Delta {ECO:0000303|PubMed:15037626};
CC IsoId=Q6JP77-1; Sequence=Displayed;
CC Name=Gamma {ECO:0000269|PubMed:15057822};
CC IsoId=Q6JP77-2; Sequence=VSP_044297;
CC -!- TISSUE SPECIFICITY: Expressed highly in the heart, and moderately in
CC brain, lung, liver, kidney and testis. Hardly detectable in spleen and
CC skeletal muscle. In kidney, isoform Delta is expressed in the principal
CC cells of the IMCD. {ECO:0000269|PubMed:15037626}.
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DR EMBL; AY350741; AAR06859.1; -; mRNA.
DR EMBL; BC098632; AAH98632.1; -; mRNA.
DR RefSeq; NP_001001801.1; NM_001001801.3. [Q6JP77-1]
DR PDB; 2VFK; X-ray; 1.50 A; A=88-292.
DR PDB; 2VFL; X-ray; 2.25 A; A=88-292.
DR PDB; 2VFY; X-ray; 1.80 A; A=88-292.
DR PDB; 3J4Q; EM; 35.00 A; A=1-353.
DR PDB; 3J4R; EM; 35.00 A; A=1-353.
DR PDBsum; 2VFK; -.
DR PDBsum; 2VFL; -.
DR PDBsum; 2VFY; -.
DR PDBsum; 3J4Q; -.
DR PDBsum; 3J4R; -.
DR AlphaFoldDB; Q6JP77; -.
DR SMR; Q6JP77; -.
DR BioGRID; 262695; 1.
DR IntAct; Q6JP77; 1.
DR MINT; Q6JP77; -.
DR STRING; 10116.ENSRNOP00000017617; -.
DR PaxDb; Q6JP77; -.
DR PRIDE; Q6JP77; -.
DR GeneID; 361458; -.
DR KEGG; rno:361458; -.
DR CTD; 9465; -.
DR RGD; 1303071; Akap7.
DR eggNOG; KOG2814; Eukaryota.
DR InParanoid; Q6JP77; -.
DR OrthoDB; 606751at2759; -.
DR PhylomeDB; Q6JP77; -.
DR TreeFam; TF105406; -.
DR PRO; PR:Q6JP77; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0070382; C:exocytic vesicle; IDA:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0016208; F:AMP binding; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISO:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0008104; P:protein localization; TAS:RGD.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:RGD.
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; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Reference proteome.
FT CHAIN 1..353
FT /note="A-kinase anchor protein 7 isoforms delta and gamma"
FT /id="PRO_0000419635"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..353
FT /note="PKA-RII-alpha subunit binding domain"
FT /evidence="ECO:0000269|PubMed:15037626"
FT REGION 300..324
FT /note="RI-alpha-binding"
FT /evidence="ECO:0000250|UniProtKB:F8VQ58"
FT REGION 301..314
FT /note="RII-binding"
FT /evidence="ECO:0000250|UniProtKB:O43687"
FT REGION 321..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:18082768"
FT BINDING 134
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000269|PubMed:18082768"
FT BINDING 224..226
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:18082768"
FT BINDING 224..226
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000269|PubMed:18082768"
FT VAR_SEQ 56..60
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:15057822"
FT /id="VSP_044297"
FT MUTAGEN 308
FT /note="L->P: Reduces PKA-RII-alpha binding."
FT /evidence="ECO:0000269|PubMed:15037626"
SQ SEQUENCE 353 AA; 39418 MW; 5C1712A9B04E6CF3 CRC64;
MERPAAGEID ANKCDHLSRG EEGTGDLETS PVGSLADLPF AAVDIQDDCG LPDVPQGNVP
QGNPKRSKEN RGDRNDHVKK RKKAKKDYQP NYFLSIPITN KKITAGIKVL QNSILRQDNR
LTKAMVGDGS FHITLLVMQL LNEDEVNIGT DALLELKPFV EEILEGKHLT LPFHGIGTFQ
GQVGFVKLAD GDHVSALLEI AETAKRTFQE KGILAGESRT FKPHLTFMKL SKAPMLWKKG
VRKIEPGLYE QFIDHRFGEE ILYQIDLCSM LKKKQSNGYY HCESSIVIGE KDRKEPEDAE
LVRLSKRLVE NAVLKAVQQY LEETQNKKQP GEGNSVKAEE GDRNGDGSDN NRK
