ID Q2VEB4_MOUSE Unreviewed; 2308 AA. AC Q2VEB4; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 14-DEC-2022, entry version 75. DE SubName: Full=A-kinase anchoring protein alpha {ECO:0000313|EMBL:ABB60211.1}; GN Name=Akap6 {ECO:0000313|MGI:MGI:3050566}; GN Synonyms=Akapalpha {ECO:0000313|EMBL:ABB60211.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ABB60211.1}; RN [1] {ECO:0000313|EMBL:ABB60211.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Black Swiss {ECO:0000313|EMBL:ABB60211.1}; RX PubMed=16337591; DOI=10.1016/j.molcel.2005.10.013; RA Carlisle Michel J.J., Townley I.K., Dodge-Kafka K.L., Zhang F., RA Kapiloff M.S., Scott J.D.; RT "Spatial restriction of PDK1 activation cascades by anchoring to RT mAKAPalpha."; RL Mol. Cell 20:661-672(2005). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ233645; ABB60211.1; -; mRNA. DR AGR; MGI:3050566; -. DR MGI; MGI:3050566; Akap6. DR ChiTaRS; Akap6; mouse. DR GO; GO:0034704; C:calcium channel complex; ISO:MGI. DR GO; GO:0005901; C:caveola; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0014704; C:intercalated disc; ISO:MGI. DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISO:MGI. DR GO; GO:0005635; C:nuclear envelope; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; ISO:MGI. DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI. DR GO; GO:0030315; C:T-tubule; ISO:MGI. DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0051018; F:protein kinase A binding; ISO:MGI. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI. DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI. DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI. DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI. DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:MGI. DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI. DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI. 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:0001934; P:positive regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI. DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI. DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI. DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI. DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; 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:1901897; P:regulation of relaxation of cardiac muscle; ISO:MGI. DR CDD; cd00176; SPEC; 1. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR Pfam; PF00435; Spectrin; 1. DR SMART; SM00150; SPEC; 3. PE 2: Evidence at transcript level; KW Kinase {ECO:0000313|EMBL:ABB60211.1}; KW Transferase {ECO:0000313|EMBL:ABB60211.1}. FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 303..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 399..431 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 488..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 732..753 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1347..1375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1810..1836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1854..1919 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1935..1975 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1982..2001 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2158..2285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..357 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..502 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 515..530 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 543..558 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 565..611 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 732..747 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1810..1828 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1867..1910 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2183..2204 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2308 AA; 254423 MW; C0BAF1766CA8001C CRC64; MLTMSVTLSP LRSQDPDPMA TDASPMAINM TPTVEQEEGE GEEAVEDVGA EQQYGKPPPL HTAADWKIVL HLPEIETWLR MTSERVRDLT YSVQQDADSK HVDVHLVQLK DICEDISDHV EQIHALLETE FSLKLLSYSV NVIVDIHAVQ LLWHQLRVSV LVLRERILQG LQDANGNYTR QTDILQAFSE ETTEGRLDSL TEVDDSGQLT IKCSQNYLSL DCGITAFELS DYSPSEDLLG GLGDMTTSQA KTKSFDSWSY SEMEKEFPEL IRSVGLLTVA TEPVPSSCGA ANEDSSQVIL SEDHRGGHEE DGALEPGEQL GSTLETSSLG DTLTNAAEHP PETANQDSTS SPQLGAKKSQ PGPCEMMTPK RSIRDCFNYN EDSPTQPTLP KRGLFLKETL KNERRGSDGK GRVVDLKPEL SRSTPSLVEP PDRSKLCLVL QSSYPSSPSA ASQSYECLHK VGIGNLENIV RSHIKEISSS LGRLTDCHKE KPRLKKPHKT LAEVSLCKIP KRGTGSGKQS ENTRSSVVPT MVSPGAPKAT ARPATDSAST TSGDTCHQRN RGGKLPAQSK ASSSSPCSHS SESSLGSDNI KSPLPLLSKS QKGSPPAPCH ATQNGQVVEA WYGSDEYLAL PSHLKQTEVL ALKLENLTKL LPQKPRGETI QDIDDWELSE MNSDSEIYPT YHIKKKHTRL GTVSPSSSSD IASSLGESIE SGPLSDILSD EDLCMPLSGM KKFTDEKSER PSSSEKNESH SATKSALIQK LMKDIQHQDN YEAIWERIEV GFVNKLDEFI QWLNEAMETT ENWTPPKAET DSLRLYLETH LSFKLNVDSH CALKEAVEEE GHQLLELIAS HKAGLKDMLK MIASQWKELQ RQIKRQHSWI LRALDTIKAE ILATDVSVED EEGTGSPKAE AQLCYLEAQR DAVEQMSLKL YSEQYTSGSK RKEEFADMSK AHSVGSNGLL DFDSEYQELW DWLIDMESLV MDSHDLMMSE EQQQHLYKRY SVEMSIRHLK KTELLSKVEA LKKGGLSLPN DILEKVDSIN EKWELLGKTL REKIQDTMAG HSGSGPRDLL SPESGSLVRQ LEVRIKELKR WLRDTELFIF NSCLRQEKEG TSAEKQLQYF KSLCHEIKQR RRGVASILRL CQHLLDDRDT CNLNADHQPM QLIIVNLERR WEAIVMQAVQ WQTRLRKKMG KESETLNVID PGLMDLNGMS EDALEWDETD ISNKLISVHE ESNDLDQDLE PMVPTVKLEE THHKDSGYEE EAGDCGGSQY TSNITAPSSP HIYQVYSLHN VEFHEDSHTQ FLKSSPKFTG TVQPTVLTKS LSKDSSFSST KSLPDLLGGS SLVRPYSCQS GDLSQNSGSE SGIVSEGDNE MPTNSDMSLF SMVDGSPSNP ETQHLDPQMG DAANVLEQKF KDEGECIKLS SVSQASVSPV GCVNGKAGDL NSITKHTTDC LGDELQGKHE VFTFYDYSYL QGSKLKFPMI MKQPQSEKAH LEDPLLRGFY FDKKSCKPKH QTSESQPDAP LHEKILASAP HEMGRSSYKS SDIEKALTGI QNARQLSLLS RSSSVESLSP GGDLFGLGIF KNGSDSLQRS TSLESWLTSY KSNEDLFSCH SSGDISVSSG SVGELSKRTL DLLNRLENIQ SPSEQKIKRS VSDITLQSSS QKMSFSGQMS LDVASSINED SPASLTELSS SDELSLCSED IVLHKNKVPE SNASFRKRLN RSVADESDVN VSMIVNVSCT SACTDDEDDS DLLSSSTLTL TEEELCLKDE DDDSSIATDD EIYEESNLMS GLDYIKNELQ TWIRPKLSLS REKKRPSVTD EIKVNKDGGS TERANPSDTL DIEALLNCSI KRLSENNGNG KNPPRTHDLG TKGENKKNTY DVTKDPHVAD MENGNVESTP EREKEKPEIP EASANLASNV KKISESKHDE YEALMDGSDD SSVTGKEFGP PNDRHPPQIG ADPQHPERGD CTSVQNSCSG LLLETGGGSR QDSDGLKSLS NDAPSVARNA AGCCLLEQNE TEESASISSS TSCCNCKPDV FHQKDDEDCS VHDFVKEIID MASTALKSKS QPESEVAAPT SLTQIKEKVL EHSHRPIHLR KGDFYSYLSL SSHDSDCGEV TNYIDEKSNT PLPPDTVDSG LDDKEDVDCF FEACVEDEPA DEEARLSSAL PNESEVQDEA AKPEQMTASS SVFRDETDTV PLSGLSPQKG ADDAKEGDGA SHTSQGCVES AEPTTPPGKA KREGSSRKQS VSGTPEENAA SAKPKIQAFS LNAKQPKGKA ALYPSPQTLT CKEKLVSFHE DRHSNMHR //