AKAP6_RAT
ID AKAP6_RAT Reviewed; 2314 AA.
AC Q9WVC7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=A-kinase anchor protein 6;
DE Short=AKAP-6;
DE AltName: Full=Protein kinase A-anchoring protein 6;
DE Short=PRKA6;
DE AltName: Full=mAKAP;
GN Name=Akap6;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=10413680; DOI=10.1242/jcs.112.16.2725;
RA Kapiloff M.S., Shillace R.V., Westphal A.M., Scott J.D.;
RT "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of
RT differentiated myocytes.";
RL J. Cell Sci. 112:2725-2736(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1072; SER-1568 AND SER-1593,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them to the nuclear membrane or sarcoplasmic reticulum.
CC May act as an adapter for assembling multiprotein complexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RII subunit of PKA, phosphatase 2B
CC (calcineurin) and AKAP79. Interacts with SYNPO2. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13023}.
CC -!- INTERACTION:
CC Q9WVC7; P20651: Ppp3cb; NbExp=2; IntAct=EBI-7559840, EBI-7400670;
CC Q9WVC7; P48453: Ppp3cb; Xeno; NbExp=2; IntAct=EBI-7559840, EBI-642618;
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum. Nucleus membrane. Note=In
CC heart muscle. Participation of multiple targeting signals allow correct
CC intracellular targeting. These may be repeated motifs rich in basic and
CC hydrophobic amino acids, palmitoylated/myristoylated motifs or
CC alternatively splice targeting sequences.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
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DR EMBL; AF139518; AAD39150.1; -; mRNA.
DR RefSeq; NP_072140.1; NM_022618.1.
DR AlphaFoldDB; Q9WVC7; -.
DR BioGRID; 249134; 4.
DR CORUM; Q9WVC7; -.
DR IntAct; Q9WVC7; 3.
DR MINT; Q9WVC7; -.
DR STRING; 10116.ENSRNOP00000006562; -.
DR iPTMnet; Q9WVC7; -.
DR PhosphoSitePlus; Q9WVC7; -.
DR PaxDb; Q9WVC7; -.
DR PRIDE; Q9WVC7; -.
DR GeneID; 64553; -.
DR KEGG; rno:64553; -.
DR UCSC; RGD:69412; rat.
DR CTD; 9472; -.
DR RGD; 69412; Akap6.
DR eggNOG; ENOG502QSMH; Eukaryota.
DR InParanoid; Q9WVC7; -.
DR OrthoDB; 90793at2759; -.
DR PRO; PR:Q9WVC7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0051018; F:protein kinase A binding; IDA:BHF-UCL.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:BHF-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:BHF-UCL.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:BHF-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IMP:RGD.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IMP:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IDA: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:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:BHF-UCL.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IDA:BHF-UCL.
DR GO; GO:1901897; P:regulation of relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IC:BHF-UCL.
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 1: Evidence at protein level;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum.
FT CHAIN 1..2314
FT /note="A-kinase anchor protein 6"
FT /id="PRO_0000064531"
FT REPEAT 768..847
FT /note="Spectrin 1"
FT REPEAT 1033..1148
FT /note="Spectrin 2"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1854..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2062..2075
FT /note="PKA-RII subunit binding domain"
FT REGION 2166..2286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1854..1870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1871..1911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2228..2261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 2314 AA; 254352 MW; 2FB01DE0E2DDFA37 CRC64;
MLTMSVTLSP LRSQGPDPMA TDASPMAINM TPTVEQEEGE GEEAVKAIDA EQQYGKPPPL
HTAADWKIVL HLPEIETWLR MTSERVRDLT YSVQQDADSK HVDVHLVQLK DICEDISDHV
EQIHALLETE FSLKLLSYSV NVIVDIHAVQ LLWHQLRVSV LVLRERILQG LQDANGNYTR
QTDILQAFSE ETTEGRLDSL TEVDDSGQLT IKCSQDYLSL DCGITAFELS DYSPSEDLLG
GLGDMTTSQA KTKSFDSWSY SEMEKEFPEL IRSVGLLTVA TEPVPSSCGE ANEDSSQASL
SDDHKGEHGE DGAPVPGQQL DSTVGMSSLD GTLANAAEHP SETAKQDSTS SPQLGAKKTQ
PGPCEITTPK RSIRDCFNYN EDSPTQPTLP KRGLFLKETQ KNERKGSDRK GQVVDLKPEL
SRSTPSLVDP PDRSKLCLVL QSSYPSSPSA ASQSYECLHK VGLGNLENIV RSHIKEISSS
LGRLTDCHKE KLRLKKPHKT LAEVSLCRIP KQGGGSGKRS ESTGSSAGPS MVSPGAPKAT
MRPETDSAST ASGGLCHQRN RSGQLPVQSK ASSSPPCSHS SESSLGSDSI KSPVPLLSKN
KSQKSSPPAP CHATQNGQVV EAWYGSDEYL ALPSHLKQTE VLALKLESLT KLLPQKPRGE
TIQDIDDWEL SEMNSDSEIY PTYHIKKKHT RLGTVSPSSS SDIASSLGES IESGPLSDIL
SDEDLCLPLS SVKKFTDEKS ERPSSSEKNE SHSATRSALI QKLMHDIQHQ ENYEAIWERI
EGFVNKLDEF IQWLNEAMET TENWTPPKAE TDSLRLYLET HLSFKLNVDS HCALKEAVEE
EGHQLLELVV SHKAGLKDTL RMIASQWKEL QRQIKRQHSW ILRALDTIKA EILATDVSVE
DEEGTGSPKA EVQLCHLETQ RDAVEQMSLK LYSEQYTSGS KRKEEFANMS KAHAEGSNGL
LDFDSEYQEL WDWLIDMESL VMDSHDLMMS EEQQQHLYKR YSVEMSIRHL KKSELLSKVE
ALKKGGLSLP DDILEKVDSI NEKWELLGKT LREKIQDTIA GHSGSGPRDL LSPESGSLVR
QLEVRIKELK RWLRDTELFI FNSCLRQEKE GTSAEKQLQY FKSLCREIKQ RRRGVASILR
LCQHLLDDRD TCNLNADHQP MQLIIVNLER RWEAIVMQAV QWQTRLQKKM GKESETLNVI
DPGLMDLNGM SEDALEWDET DISNKLISVH EESNDLDQDP EPMLPAVKLE ETHHKDSGYE
EEAGDCGGSP YTSNITAPSS PHIYQVYSLH NVELHEDSHT PFLKSSPKFT GTTQPTVLTK
SLSKDSSFSS TKSLPDLLGG SGLVRPYSCH SGDLSQNSGS ESGIVSEGDN EMPTNSDMSL
FSMVDGSPSN PETEHPDPQM GDAANVLEQK FKDNGESIKL SSVSRASVSP VGCVNGKAGD
LNSVTKHTAD CLGEELQGKH DVFTFYDYSY LQGSKLKLPM IMKQPQSEKA HVEDPLLGGF
YFDKKSCKAK HQASESQPDA PPHERILASA PHEMGRSAYK SSDIEKTFTG IQSARQLSLL
SRSSSVESLS PGGDLFGLGI FKNGSDSLQR STSLESWLTS YKSNEDLFSC HSSGDISVSS
GSVGELSKRT LDLLNRLENI QSPSEQKIKR SVSDMTLQSS SQKMPFAGQM SLDVASSINE
DSPASLTELS SSDELSLCSE DIVLHKNKIP ESNASFRKRL NRSVADESDV NVSMIVNVSC
TSACTDDEDD SDLLSSSTLT LTEEELCLKD EDDDSSIATD DEIYEESNLM SGLDYIKNEL
QTWIRPKLSL TREKKRSGVT DEIKVNKDGG GNEKANPSDT LDIEALLNGS IRCLSENNGN
GKTPPRTHGS GTKGENKKST YDVSKDPHVA DMENGNIEST PEREREKPQG LPEVSENLAS
NVKTISESEL SEYEAVMDGS EDSSVARKEF CPPNDRHPPQ MGPKLQHPEN QSGDCKPVQN
PCPGLLSEAG VGSRQDSNGL KSLPNDAPSG ARKPAGCCLL EQNETEESAS ISSNASCCNC
KPDVFHQKDD EDCSVHDFVK EIIDMASTAL KSKSQPESEV AAPTSLTQIK EKVLEHSHRP
IHLRKGDFYS YLSLSSHDSD CGEVTNYIDE KSSTPLPPDA VDSGLDDKED MDCFFEACVE
DEPVNEEAGL PGALPNESAI EDGAEQKSEQ KTASSPVLSD KTDLVPLSGL SPQKGADDAK
EGDDVSHTSQ GCAESTEPTT PSGKANAEGR SRMQGVSATP EENAASAKPK IQAFSLNAKQ
PKGKVAMRYP SPQTLTCKEK LVNFHEDRHS NMHR
