ID A0A2K6CNB5_MACNE Unreviewed; 2830 AA.
AC A0A2K6CNB5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=A-kinase anchoring protein 13 {ECO:0000313|Ensembl:ENSMNEP00000025148.1};
GN Name=AKAP13 {ECO:0000313|Ensembl:ENSMNEP00000025148.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000025148.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000025148.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 9545.ENSMNEP00000025148; -.
DR Ensembl; ENSMNET00000049423.1; ENSMNEP00000025148.1; ENSMNEG00000035804.1.
DR GeneTree; ENSGT00940000154146; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000035804; Expressed in heart and 12 other cell types or tissues.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR CDD; cd20878; C1_AKAP13; 1.
DR CDD; cd13392; PH_AKAP13; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018459; RII-bd_1.
DR PANTHER; PTHR13944:SF18; A-KINASE ANCHOR PROTEIN 13; 1.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF10522; RII_binding_1; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1809..1856
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2010..2207
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2247..2349
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 359..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2479..2522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2682..2830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2363..2394
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 359..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2495..2518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2682..2706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2761..2790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2830 AA; 310666 MW; 3F9AE7013B94884C CRC64;
MKLNPQQAPL YGDCVVTVLL AEEDKVEDDV VFYLVFSGST LRHCTSTRKV SSDTLETIAP
GHDCCETVKV QLCASKEGLP VFVVAEEDFH FIQDEAYDAA QFLATSAGNQ QALNFTRFLD
QSGPPSGDVN SLDKKVVLAF RHLKLPAEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
DCSVRHHREL DIYTLTSESE SHEHPFPGDS CTGHIFRLMN IQQQLMKTNL KQMDNLMPLM
VTAQDPSSAP ETDGQFLPCA PEPTDPQRLS SSEEIESTHC CPGIPVAQTE SPCDLSSIVE
EENTDHSCRK KNKGVERKGE EVEPAPIVDS GTVSDQDSCL QRLPDCGVKG MEGVSSCGNR
SEETGTKSSR MPTDQDSLSS GDAVLQRDLV MEPGTAQYSS GGELGGISTT NVSTPETAGE
MEHGLMNPDA TVQKNVLEVG ESTKERFENS NIGTAGASDV HVVISKPVDK VSVPNCAPAA
SSLDGDKPAE SSLAFSNEET SIEKTAETET SQSREESADA PVDQNSVVIP AATEDKISDG
LEPYTLLAAV IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS PICSTTGDDK
LCADSACQQN TVTSSGDLVA KRCDNIVSQP ESTTARQPSS QDPPNATHCE DPQANTVTSD
PVRDTRERVD FCPLKVVDNK GQRKDVKLDK PLTNMLEVVS HPHPVVPKME KELVPDQAVI
SDSTFSLANN PGSESVTKDD ALSFVPSQKE KGTATPELHM ATDCRDGPDG DSNEPDTQPL
EDRAADLSTP STAAELQRGM GNTSLTGLGG EREGPAPPAI PEALNIKGDT DSSLQSVGML
QEEQRTPPPR QETLQFHEKS VLVDGAKDKA LQLSNSPGAP SACLKAETEH NKEVAPQVSL
LIQGGAAQSL VPPGASLATD LRQEALGAEH NSSTLLPCLL PDGSDGSEAL NCSQPSPLDV
GVKNPQSQGK TSACEVNGSV TVDVTQVNAL QGMAVPRRKN VSHNTQDILI PDVLLNQEKN
VILGLPVALR DKAVTDPQGV GTPEMVPLDW EKGKLEGADH SCTRGDAEEA QIDTEAHPVL
LQPAAKELPT DMGLSSHDDE APAGAREVLQ ALPSGGERST PSLPCMVSAQ ATPLPKGADL
IEEAASRIVD AVIEQVKAAG ALLTEGEACQ MSLSRPKLLG PLTEGLENAF TEKVSTFPPG
ESLPMGSTPE EATGSLAGCF AEREEPEKII LPVQGPEPAT EMPDVKAEDE VDFRASSVSE
EVAVGSIAAT LKMKQGPMTQ AINRENWCTI EPCPDAASLL ASKQSPECEN FLDVGLGREC
TSKQGVLKRE PGSDSDLFHS PSDDMDSIIF PKPEEEQLTC DITGSSSSTD DTASLDQHSS
HGSDVSLSQI LKPNRSRDRQ SLDGFYSHGM GAEGRESESE PADPGDVEEE EMDSITEVPA
NCSVLRSSMR SLSPFRRHSW GPGKNAASDA EMNHRSSMRA LGDVVRRPPI HRRSMSWCPS
GVQYSAGLSA DLNYRSFSLE GLTGGAGVGN KPSSSLEVSS ANAKELRHPF GDEERVDSLV
SLSEEDLESG QREHRMFDQQ ICHRSKQQGF NYCTSAISSP LTKSISLMTI SHPGLDTQQQ
MRPARRISIS ISPLLLKSKT LFSLGSSYSS DEEEELHNTR PFHSTFHNTS ANQTESITEE
NYNFPPQSLF KKDSEWKSAT KVSRTFSYIK NKMSSSKKSK QEKEKEKDKI KEKEKDSKDK
EKDKKTVNGH TFSSIPVVGP ISCSQCMKPF TNKDAYTCAN CSAFVHKGCR ESLASCAKVK
MKQPKGSLQA HDTSSLPTVI MRNKPAQPKE RPRSAVLLVD ETTTTPIFAS RRSQQSVSLS
KSVSIQNITG VGNDENMSNT WKFLSHSTDS LNKISKVNES TESLTDEGTD MNEGQLLGDF
EIDSKQLEAE SWSRIIDSKF LKQQKKDVVK RQEVIYELMQ TELHHVRTLK IMSDVYSRGM
MTDLLFEQQM VEKLFPCLDE LISIHSQFFQ RILERKEESL VDKSEKNFLI KRIGDVLVNQ
FSGENAERLK KTYGKFCGQH NQSVNYFKDL YAKDKRFQAF VKKKMSSSVV RRLGIPECIL
LVTQRITKYP VLFQRILQCT KDNEVEQEDL AQSLSLVKDV IGAVDSKVAS YEKKVRLNEI
YTKTDSKSIM RMKSGQMFAK EDLKRKKLVR DGSVFLKNAA GRLKEVQAVL LTDILVFLQE
KDQKYIFASL DQKSTVISLK KLIVREVAHE ERGLFLISMG MKDPEMVEVH ASSKEERNSW
IQIIQDTINT LNRDEDEGIP SENEEEKKML DTKARELKEQ LQQKDQQILL LLEEKEMIFR
DMAECSTPLP EDCSPTHSPR VLFRSNTEDA LKGGPLMKSA INEVEILQGL VSGNLGGTLG
PTVSSPIEQE GAVGPVSLPR RAETFGGFDS HQMNASKGGE KEEGDDGQDL RRTESDSGLK
KGGNANLVFM LKRNSEQVVQ SIVHLHELLS TLQGVVLQQD SYIEDQKLVL SERALTRTLS
RPSSLIEQEK QRSLEKQRQD LANLQKQQAQ YLEEKRRRER EWEARERELR EREALLAQRE
EKVQQGQQDL EKEREELQQK KGTYQYDLER LRAAQKQLER EQEQLRREAE RLSQRQTERD
LCQVSHPHSK LMRIPSFFPS PEEPPSPSAP LIAKSGSLDS DLSVSPKRNS ISRTHKDKGP
FHILSSTSQT NKGPEGQSQA PVSTSASTRL FGLAKPKEKK EKKKKNKTSR SQPGDGPTSE
VSAEGEEIFC
//
