Full text data of AKAP7
AKAP7
(AKAP15, AKAP18)
[Confidence: low (only semi-automatic identification from reviews)]
A-kinase anchor protein 7 isoforms alpha and beta; AKAP-7 isoforms alpha and beta (A-kinase anchor protein 18 kDa; AKAP 18; Protein kinase A-anchoring protein 7 isoforms alpha/beta; PRKA7 isoforms alpha/beta)
A-kinase anchor protein 7 isoforms alpha and beta; AKAP-7 isoforms alpha and beta (A-kinase anchor protein 18 kDa; AKAP 18; Protein kinase A-anchoring protein 7 isoforms alpha/beta; PRKA7 isoforms alpha/beta)
UniProt
O43687
ID AKA7A_HUMAN Reviewed; 104 AA.
AC O43687; A8K2K6; Q5TBR9; Q5TBS0; Q9HCZ8; Q9P0G4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=A-kinase anchor protein 7 isoforms alpha and beta;
DE Short=AKAP-7 isoforms alpha and beta;
DE AltName: Full=A-kinase anchor protein 18 kDa;
DE Short=AKAP 18;
DE AltName: Full=Protein kinase A-anchoring protein 7 isoforms alpha/beta;
DE Short=PRKA7 isoforms alpha/beta;
GN Name=AKAP7; Synonyms=AKAP15, AKAP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, AND
RP PALMITOYLATION AT CYS-5 AND CYS-6.
RC TISSUE=Brain;
RX PubMed=9545239; DOI=10.1093/emboj/17.8.2261;
RA Fraser I.D.C., Tavalin S.J., Lester L.B., Langeberg L.K.,
RA Westphal A.M., Dean R.A., Marrion N.V., Scott J.D.;
RT "A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-
RT responsive membrane events.";
RL EMBO J. 17:2261-2272(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, AND SUBCELLULAR
RP LOCATION.
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-
RT kinase anchoring protein 18 isoforms.";
RL J. Cell Biol. 147:1481-1492(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Adrenal cortex, Hippocampus, and Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH PRKCA, AND MUTAGENESIS OF 2-GLY--CYS-6.
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
RT the epithelial Na+ channel.";
RL FASEB J. 21:1189-1201(2007).
CC -!- FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the
CC plasma membrane, and permits functional coupling to the L-type
CC calcium channel. The membrane-associated form reduces epithelial
CC sodium channel (ENaC) activity, whereas the free cytoplasmic form
CC may negatively regulate ENaC channel feedback inhibition by
CC intracellular sodium.
CC -!- SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with
CC PRKCA; only the cytoplasmic form is capable of interacting with
CC PRKCA.
CC -!- SUBCELLULAR LOCATION: Isoform Alpha: Lateral cell membrane; Lipid-
CC anchor. Note=Targeted predominantly to the lateral membrane.
CC -!- SUBCELLULAR LOCATION: Isoform Beta: Apical cell membrane; Lipid-
CC anchor. Note=Targeted predominantly to the apical membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=Beta;
CC IsoId=O43687-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=O43687-2; Sequence=VSP_004101;
CC Name=Gamma;
CC IsoId=Q9P0M2-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, pancreas and
CC skeletal muscle.
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DR EMBL; AF047715; AAC39715.1; -; mRNA.
DR EMBL; AF161075; AAF26676.1; -; mRNA.
DR EMBL; AK290271; BAF82960.1; -; mRNA.
DR EMBL; AL136110; CAI21507.1; -; Genomic_DNA.
DR EMBL; AL137063; CAI21507.1; JOINED; Genomic_DNA.
DR EMBL; AL136110; CAI21508.1; -; Genomic_DNA.
DR EMBL; AL137063; CAI21508.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19001.1; -; Genomic_DNA.
DR EMBL; AL136110; CAI19001.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19002.1; -; Genomic_DNA.
DR EMBL; AL136110; CAI19002.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW48057.1; -; Genomic_DNA.
DR EMBL; BC016927; AAH16927.1; -; mRNA.
DR EMBL; BC073847; AAH73847.1; -; mRNA.
DR EMBL; BC094732; AAH94732.1; -; mRNA.
DR RefSeq; NP_004833.1; NM_004842.3.
DR RefSeq; NP_619539.1; NM_138633.2.
DR UniGene; Hs.486483; -.
DR UniGene; Hs.732515; -.
DR ProteinModelPortal; O43687; -.
DR MINT; MINT-5000796; -.
DR STRING; 9606.ENSP00000357105; -.
DR PaxDb; O43687; -.
DR PRIDE; O43687; -.
DR DNASU; 9465; -.
DR Ensembl; ENST00000342266; ENSP00000345149; ENSG00000118507.
DR Ensembl; ENST00000474850; ENSP00000418208; ENSG00000118507.
DR GeneID; 9465; -.
DR KEGG; hsa:9465; -.
DR UCSC; uc003qcm.2; human.
DR CTD; 9465; -.
DR GeneCards; GC06P131508; -.
DR HGNC; HGNC:377; AKAP7.
DR MIM; 604693; gene.
DR neXtProt; NX_O43687; -.
DR PharmGKB; PA24671; -.
DR eggNOG; NOG266143; -.
DR HOGENOM; HOG000013043; -.
DR HOVERGEN; HBG050474; -.
DR KO; K16524; -.
DR OrthoDB; EOG773XG9; -.
DR GeneWiki; AKAP7; -.
DR GenomeRNAi; 9465; -.
DR NextBio; 35464; -.
DR ArrayExpress; O43687; -.
DR Bgee; O43687; -.
DR CleanEx; HS_AKAP7; -.
DR Genevestigator; O43687; -.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
DR GO; GO:0006811; P:ion transport; TAS:ProtInc.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IC:UniProtKB.
DR GO; GO:0001508; P:regulation of action potential; IC:BHF-UCL.
DR GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR InterPro; IPR019511; Kinase-A_anchor_RI-RII-bd_dom.
DR Pfam; PF10470; AKAP7_RIRII_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Lipoprotein;
KW Membrane; Myristate; Palmitate; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 104 A-kinase anchor protein 7 isoforms alpha
FT and beta.
FT /FTId=PRO_0000064522.
FT REGION 2 11 Required for membrane localization.
FT REGION 18 40 Required for apical membrane
FT localization.
FT REGION 52 65 RII-binding.
FT LIPID 2 2 N-myristoyl glycine.
FT LIPID 5 5 S-palmitoyl cysteine.
FT LIPID 6 6 S-palmitoyl cysteine.
FT VAR_SEQ 18 40 Missing (in isoform Alpha).
FT /FTId=VSP_004101.
FT MUTAGEN 2 6 GQLCC->AQLAA: Abolishes membrane
FT localization and affects its ability to
FT inhibit ENaC activity in a sodium-
FT dependent manner.
SQ SEQUENCE 104 AA; 11465 MW; 6F84ED8E032AF954 CRC64;
MGQLCCFPFS RDEGKISELE SSSSAVLQRY SKDIPSWSSG EKNGGEPDDA ELVRLSKRLV
ENAVLKAVQQ YLEETQNKNK PGEGSSVKTE AADQNGNDNE NNRK
//
ID AKA7A_HUMAN Reviewed; 104 AA.
AC O43687; A8K2K6; Q5TBR9; Q5TBS0; Q9HCZ8; Q9P0G4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=A-kinase anchor protein 7 isoforms alpha and beta;
DE Short=AKAP-7 isoforms alpha and beta;
DE AltName: Full=A-kinase anchor protein 18 kDa;
DE Short=AKAP 18;
DE AltName: Full=Protein kinase A-anchoring protein 7 isoforms alpha/beta;
DE Short=PRKA7 isoforms alpha/beta;
GN Name=AKAP7; Synonyms=AKAP15, AKAP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, AND
RP PALMITOYLATION AT CYS-5 AND CYS-6.
RC TISSUE=Brain;
RX PubMed=9545239; DOI=10.1093/emboj/17.8.2261;
RA Fraser I.D.C., Tavalin S.J., Lester L.B., Langeberg L.K.,
RA Westphal A.M., Dean R.A., Marrion N.V., Scott J.D.;
RT "A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-
RT responsive membrane events.";
RL EMBO J. 17:2261-2272(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, AND SUBCELLULAR
RP LOCATION.
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-
RT kinase anchoring protein 18 isoforms.";
RL J. Cell Biol. 147:1481-1492(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Colon;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Adrenal cortex, Hippocampus, and Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH PRKCA, AND MUTAGENESIS OF 2-GLY--CYS-6.
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
RT the epithelial Na+ channel.";
RL FASEB J. 21:1189-1201(2007).
CC -!- FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the
CC plasma membrane, and permits functional coupling to the L-type
CC calcium channel. The membrane-associated form reduces epithelial
CC sodium channel (ENaC) activity, whereas the free cytoplasmic form
CC may negatively regulate ENaC channel feedback inhibition by
CC intracellular sodium.
CC -!- SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with
CC PRKCA; only the cytoplasmic form is capable of interacting with
CC PRKCA.
CC -!- SUBCELLULAR LOCATION: Isoform Alpha: Lateral cell membrane; Lipid-
CC anchor. Note=Targeted predominantly to the lateral membrane.
CC -!- SUBCELLULAR LOCATION: Isoform Beta: Apical cell membrane; Lipid-
CC anchor. Note=Targeted predominantly to the apical membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=Beta;
CC IsoId=O43687-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=O43687-2; Sequence=VSP_004101;
CC Name=Gamma;
CC IsoId=Q9P0M2-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, pancreas and
CC skeletal muscle.
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DR EMBL; AF047715; AAC39715.1; -; mRNA.
DR EMBL; AF161075; AAF26676.1; -; mRNA.
DR EMBL; AK290271; BAF82960.1; -; mRNA.
DR EMBL; AL136110; CAI21507.1; -; Genomic_DNA.
DR EMBL; AL137063; CAI21507.1; JOINED; Genomic_DNA.
DR EMBL; AL136110; CAI21508.1; -; Genomic_DNA.
DR EMBL; AL137063; CAI21508.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19001.1; -; Genomic_DNA.
DR EMBL; AL136110; CAI19001.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19002.1; -; Genomic_DNA.
DR EMBL; AL136110; CAI19002.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW48057.1; -; Genomic_DNA.
DR EMBL; BC016927; AAH16927.1; -; mRNA.
DR EMBL; BC073847; AAH73847.1; -; mRNA.
DR EMBL; BC094732; AAH94732.1; -; mRNA.
DR RefSeq; NP_004833.1; NM_004842.3.
DR RefSeq; NP_619539.1; NM_138633.2.
DR UniGene; Hs.486483; -.
DR UniGene; Hs.732515; -.
DR ProteinModelPortal; O43687; -.
DR MINT; MINT-5000796; -.
DR STRING; 9606.ENSP00000357105; -.
DR PaxDb; O43687; -.
DR PRIDE; O43687; -.
DR DNASU; 9465; -.
DR Ensembl; ENST00000342266; ENSP00000345149; ENSG00000118507.
DR Ensembl; ENST00000474850; ENSP00000418208; ENSG00000118507.
DR GeneID; 9465; -.
DR KEGG; hsa:9465; -.
DR UCSC; uc003qcm.2; human.
DR CTD; 9465; -.
DR GeneCards; GC06P131508; -.
DR HGNC; HGNC:377; AKAP7.
DR MIM; 604693; gene.
DR neXtProt; NX_O43687; -.
DR PharmGKB; PA24671; -.
DR eggNOG; NOG266143; -.
DR HOGENOM; HOG000013043; -.
DR HOVERGEN; HBG050474; -.
DR KO; K16524; -.
DR OrthoDB; EOG773XG9; -.
DR GeneWiki; AKAP7; -.
DR GenomeRNAi; 9465; -.
DR NextBio; 35464; -.
DR ArrayExpress; O43687; -.
DR Bgee; O43687; -.
DR CleanEx; HS_AKAP7; -.
DR Genevestigator; O43687; -.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
DR GO; GO:0006811; P:ion transport; TAS:ProtInc.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IC:UniProtKB.
DR GO; GO:0001508; P:regulation of action potential; IC:BHF-UCL.
DR GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR InterPro; IPR019511; Kinase-A_anchor_RI-RII-bd_dom.
DR Pfam; PF10470; AKAP7_RIRII_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Lipoprotein;
KW Membrane; Myristate; Palmitate; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 104 A-kinase anchor protein 7 isoforms alpha
FT and beta.
FT /FTId=PRO_0000064522.
FT REGION 2 11 Required for membrane localization.
FT REGION 18 40 Required for apical membrane
FT localization.
FT REGION 52 65 RII-binding.
FT LIPID 2 2 N-myristoyl glycine.
FT LIPID 5 5 S-palmitoyl cysteine.
FT LIPID 6 6 S-palmitoyl cysteine.
FT VAR_SEQ 18 40 Missing (in isoform Alpha).
FT /FTId=VSP_004101.
FT MUTAGEN 2 6 GQLCC->AQLAA: Abolishes membrane
FT localization and affects its ability to
FT inhibit ENaC activity in a sodium-
FT dependent manner.
SQ SEQUENCE 104 AA; 11465 MW; 6F84ED8E032AF954 CRC64;
MGQLCCFPFS RDEGKISELE SSSSAVLQRY SKDIPSWSSG EKNGGEPDDA ELVRLSKRLV
ENAVLKAVQQ YLEETQNKNK PGEGSSVKTE AADQNGNDNE NNRK
//
MIM
604693
*RECORD*
*FIELD* NO
604693
*FIELD* TI
*604693 A-KINASE ANCHOR PROTEIN 7; AKAP7
;;A-KINASE ANCHOR PROTEIN, 18-KD; AKAP18
*FIELD* TX
read moreA-kinase anchor proteins (AKAPs; see 602449) direct the activity of
protein kinase A (PKA; see 176911) by tethering the enzyme near its
physiologic substrates.
By screening a fetal brain cDNA library with regulatory type II (RII)
PKA as a probe, Fraser et al. (1998) obtained a cDNA encoding a novel
AKAP protein, AKAP7, which the authors designated AKAP18. AKAP7 contains
81 amino acids. Northern blot analysis demonstrated the expression of a
major 2.9-kb transcript in pancreas, brain, and heart as well as a minor
band of 4.3 kb in cardiac and skeletal muscle. Helical wheel analysis
showed that the RII-binding amphipathic helix domain comprises residues
29 to 42. Sequence analysis identified a myristoylation signal at the
N-terminal glycine residue and 2 palmitoylation sites at cys4 and cys5.
Immunoprecipitation and immunofluorescence confocal microscopy analyses
of wildtype and mutant AKAP18 showed that the lipids are required for
attachment of AKAP18 to the cytoplasmic face of the plasma membrane.
Expression of AKAP18 in cells expressing cardiac L-type calcium channels
promoted an increase in cAMP-responsive calcium currents, suggesting
that membrane anchoring of PKA participates in physiologically relevant
events involving ion channel activation.
The International Radiation Hybrid Mapping Corsortium mapped the AKAP7
gene to chromosome 6 (TMAP stSG41406).
*FIELD* RF
1. Fraser, I. D. C.; Tavalin, S. J.; Lester, L. B.; Langeberg, L.
K.; Westphal, A. M.; Dean, R. A.; Marrion, N. V.; Scott, J. D.: A
novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive
membrane events. EMBO J. 17: 2261-2272, 1998.
*FIELD* CD
Paul J. Converse: 3/17/2000
*FIELD* ED
carol: 04/04/2000
carol: 3/30/2000
carol: 3/20/2000
carol: 3/17/2000
*RECORD*
*FIELD* NO
604693
*FIELD* TI
*604693 A-KINASE ANCHOR PROTEIN 7; AKAP7
;;A-KINASE ANCHOR PROTEIN, 18-KD; AKAP18
*FIELD* TX
read moreA-kinase anchor proteins (AKAPs; see 602449) direct the activity of
protein kinase A (PKA; see 176911) by tethering the enzyme near its
physiologic substrates.
By screening a fetal brain cDNA library with regulatory type II (RII)
PKA as a probe, Fraser et al. (1998) obtained a cDNA encoding a novel
AKAP protein, AKAP7, which the authors designated AKAP18. AKAP7 contains
81 amino acids. Northern blot analysis demonstrated the expression of a
major 2.9-kb transcript in pancreas, brain, and heart as well as a minor
band of 4.3 kb in cardiac and skeletal muscle. Helical wheel analysis
showed that the RII-binding amphipathic helix domain comprises residues
29 to 42. Sequence analysis identified a myristoylation signal at the
N-terminal glycine residue and 2 palmitoylation sites at cys4 and cys5.
Immunoprecipitation and immunofluorescence confocal microscopy analyses
of wildtype and mutant AKAP18 showed that the lipids are required for
attachment of AKAP18 to the cytoplasmic face of the plasma membrane.
Expression of AKAP18 in cells expressing cardiac L-type calcium channels
promoted an increase in cAMP-responsive calcium currents, suggesting
that membrane anchoring of PKA participates in physiologically relevant
events involving ion channel activation.
The International Radiation Hybrid Mapping Corsortium mapped the AKAP7
gene to chromosome 6 (TMAP stSG41406).
*FIELD* RF
1. Fraser, I. D. C.; Tavalin, S. J.; Lester, L. B.; Langeberg, L.
K.; Westphal, A. M.; Dean, R. A.; Marrion, N. V.; Scott, J. D.: A
novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive
membrane events. EMBO J. 17: 2261-2272, 1998.
*FIELD* CD
Paul J. Converse: 3/17/2000
*FIELD* ED
carol: 04/04/2000
carol: 3/30/2000
carol: 3/20/2000
carol: 3/17/2000