Full text data of AKAP7
AKAP7
(AKAP18)
[Confidence: low (only semi-automatic identification from reviews)]
A-kinase anchor protein 7 isoform gamma; AKAP-7 isoform gamma (A-kinase anchor protein 18 kDa; AKAP 18; Protein kinase A-anchoring protein 7 isoform gamma; PRKA7 isoform gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
A-kinase anchor protein 7 isoform gamma; AKAP-7 isoform gamma (A-kinase anchor protein 18 kDa; AKAP 18; Protein kinase A-anchoring protein 7 isoform gamma; PRKA7 isoform gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9P0M2
ID AKA7G_HUMAN Reviewed; 348 AA.
AC Q9P0M2; B4DUC3; Q9HCZ8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-NOV-2011, sequence version 2.
DT 22-JAN-2014, entry version 98.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
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.,
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 [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.,
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-348, FUNCTION, RII-BINDING,
RP SUBCELLULAR 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-
RT kinase 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
RT the epithelial Na+ channel.";
RL FASEB J. 21:1189-1201(2007).
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.
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: Nucleus (By similarity). Cytoplasm.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28106.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAI19003.1; Type=Erroneous gene model prediction;
CC Sequence=CAI19788.1; Type=Erroneous gene model prediction;
CC Sequence=CAI21509.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK300587; BAG62285.1; -; mRNA.
DR EMBL; AL137063; CAI19003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136110; CAI19003.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI19003.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI19788.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136110; CAI19788.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19788.1; JOINED; Genomic_DNA.
DR EMBL; AL136110; CAI21509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137063; CAI21509.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI21509.1; JOINED; Genomic_DNA.
DR EMBL; AF152929; AAF28106.1; ALT_INIT; mRNA.
DR RefSeq; NP_057461.2; NM_016377.3.
DR UniGene; Hs.486483; -.
DR UniGene; Hs.732515; -.
DR ProteinModelPortal; Q9P0M2; -.
DR SMR; Q9P0M2; 83-287.
DR IntAct; Q9P0M2; 3.
DR PhosphoSite; Q9P0M2; -.
DR DMDM; 25089623; -.
DR PRIDE; Q9P0M2; -.
DR Ensembl; ENST00000368123; ENSP00000357105; ENSG00000118507.
DR Ensembl; ENST00000431975; ENSP00000405252; ENSG00000118507.
DR GeneID; 9465; -.
DR KEGG; hsa:9465; -.
DR UCSC; uc003qck.4; human.
DR CTD; 9465; -.
DR GeneCards; GC06P131508; -.
DR H-InvDB; HIX0032781; -.
DR HGNC; HGNC:377; AKAP7.
DR HPA; HPA027172; -.
DR HPA; HPA028327; -.
DR MIM; 604693; gene.
DR neXtProt; NX_Q9P0M2; -.
DR PharmGKB; PA24671; -.
DR HOGENOM; HOG000294077; -.
DR HOVERGEN; HBG050475; -.
DR InParanoid; Q9P0M2; -.
DR KO; K16524; -.
DR OMA; HRIDLCS; -.
DR GenomeRNAi; 9465; -.
DR NextBio; 35464; -.
DR ArrayExpress; Q9P0M2; -.
DR Bgee; Q9P0M2; -.
DR CleanEx; HS_AKAP7; -.
DR Genevestigator; Q9P0M2; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0016208; F:AMP binding; IEA:Ensembl.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR GO; GO:0010738; P:regulation of protein kinase A signaling cascade; IEA:Ensembl.
DR Gene3D; 3.90.1140.10; -; 1.
DR InterPro; IPR019510; Kinase-A_anchor_nucl_local_sig.
DR InterPro; IPR019511; Kinase-A_anchor_RI-RII-bd_dom.
DR InterPro; IPR009097; RNA_ligase/cNuc_Pdiesterase.
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; Polymorphism; Reference proteome.
FT CHAIN 1 348 A-kinase anchor protein 7 isoform gamma.
FT /FTId=PRO_0000064523.
FT NP_BIND 219 221 AMP (By similarity).
FT NP_BIND 219 221 CMP (By similarity).
FT REGION 294 348 PKA-RII-alpha subunit binding domain (By
FT similarity).
FT REGION 295 319 RI-alpha-binding (By similarity).
FT REGION 296 309 RII-binding.
FT BINDING 129 129 AMP (By similarity).
FT BINDING 129 129 CMP (By similarity).
FT VARIANT 26 26 E -> K (in dbSNP:rs7771473).
FT /FTId=VAR_024246.
FT VARIANT 215 215 S -> N (in dbSNP:rs1190788).
FT /FTId=VAR_024247.
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
//
ID AKA7G_HUMAN Reviewed; 348 AA.
AC Q9P0M2; B4DUC3; Q9HCZ8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-NOV-2011, sequence version 2.
DT 22-JAN-2014, entry version 98.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
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.,
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 [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.,
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-348, FUNCTION, RII-BINDING,
RP SUBCELLULAR 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-
RT kinase 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
RT the epithelial Na+ channel.";
RL FASEB J. 21:1189-1201(2007).
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.
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: Nucleus (By similarity). Cytoplasm.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28106.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAI19003.1; Type=Erroneous gene model prediction;
CC Sequence=CAI19788.1; Type=Erroneous gene model prediction;
CC Sequence=CAI21509.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK300587; BAG62285.1; -; mRNA.
DR EMBL; AL137063; CAI19003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136110; CAI19003.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI19003.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI19788.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136110; CAI19788.1; JOINED; Genomic_DNA.
DR EMBL; AL137063; CAI19788.1; JOINED; Genomic_DNA.
DR EMBL; AL136110; CAI21509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137063; CAI21509.1; JOINED; Genomic_DNA.
DR EMBL; AL137222; CAI21509.1; JOINED; Genomic_DNA.
DR EMBL; AF152929; AAF28106.1; ALT_INIT; mRNA.
DR RefSeq; NP_057461.2; NM_016377.3.
DR UniGene; Hs.486483; -.
DR UniGene; Hs.732515; -.
DR ProteinModelPortal; Q9P0M2; -.
DR SMR; Q9P0M2; 83-287.
DR IntAct; Q9P0M2; 3.
DR PhosphoSite; Q9P0M2; -.
DR DMDM; 25089623; -.
DR PRIDE; Q9P0M2; -.
DR Ensembl; ENST00000368123; ENSP00000357105; ENSG00000118507.
DR Ensembl; ENST00000431975; ENSP00000405252; ENSG00000118507.
DR GeneID; 9465; -.
DR KEGG; hsa:9465; -.
DR UCSC; uc003qck.4; human.
DR CTD; 9465; -.
DR GeneCards; GC06P131508; -.
DR H-InvDB; HIX0032781; -.
DR HGNC; HGNC:377; AKAP7.
DR HPA; HPA027172; -.
DR HPA; HPA028327; -.
DR MIM; 604693; gene.
DR neXtProt; NX_Q9P0M2; -.
DR PharmGKB; PA24671; -.
DR HOGENOM; HOG000294077; -.
DR HOVERGEN; HBG050475; -.
DR InParanoid; Q9P0M2; -.
DR KO; K16524; -.
DR OMA; HRIDLCS; -.
DR GenomeRNAi; 9465; -.
DR NextBio; 35464; -.
DR ArrayExpress; Q9P0M2; -.
DR Bgee; Q9P0M2; -.
DR CleanEx; HS_AKAP7; -.
DR Genevestigator; Q9P0M2; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0016208; F:AMP binding; IEA:Ensembl.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR GO; GO:0010738; P:regulation of protein kinase A signaling cascade; IEA:Ensembl.
DR Gene3D; 3.90.1140.10; -; 1.
DR InterPro; IPR019510; Kinase-A_anchor_nucl_local_sig.
DR InterPro; IPR019511; Kinase-A_anchor_RI-RII-bd_dom.
DR InterPro; IPR009097; RNA_ligase/cNuc_Pdiesterase.
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; Polymorphism; Reference proteome.
FT CHAIN 1 348 A-kinase anchor protein 7 isoform gamma.
FT /FTId=PRO_0000064523.
FT NP_BIND 219 221 AMP (By similarity).
FT NP_BIND 219 221 CMP (By similarity).
FT REGION 294 348 PKA-RII-alpha subunit binding domain (By
FT similarity).
FT REGION 295 319 RI-alpha-binding (By similarity).
FT REGION 296 309 RII-binding.
FT BINDING 129 129 AMP (By similarity).
FT BINDING 129 129 CMP (By similarity).
FT VARIANT 26 26 E -> K (in dbSNP:rs7771473).
FT /FTId=VAR_024246.
FT VARIANT 215 215 S -> N (in dbSNP:rs1190788).
FT /FTId=VAR_024247.
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
//
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