ID G3QER7_GORGO Unreviewed; 2817 AA.
AC G3QER7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=A-kinase anchoring protein 13 {ECO:0000313|Ensembl:ENSGGOP00000000766.3};
GN Name=AKAP13 {ECO:0000313|Ensembl:ENSGGOP00000000766.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000766.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000000766.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000000766.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000000766.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CABD030097664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030097673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000000766; -.
DR Ensembl; ENSGGOT00000000782.3; ENSGGOP00000000766.3; ENSGGOG00000000774.3.
DR GeneTree; ENSGT00940000154146; -.
DR HOGENOM; CLU_000597_0_0_1; -.
DR InParanoid; G3QER7; -.
DR OMA; NDESMSN; -.
DR Proteomes; UP000001519; Chromosome 15.
DR Bgee; ENSGGOG00000000774; Expressed in heart and 6 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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
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:UP000001519};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1795..1842
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1998..2195
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2235..2337
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 304..400
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 458..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2470..2508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2672..2817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2355..2382
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 326..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2672..2693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2717..2736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2748..2778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2817 AA; 307486 MW; 4FBEA34A6CCCE78C CRC64;
MKLNPQQAPL YGDCVVTVLL AEEDKVEDDV VFYLVFLGSA LRHCTSTQKV SSDTLETIAP
GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD
QSGPPSGDVN SLDKKLVLAF RHLKLPAEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
DCSVRHHREL DIYTLTSESD SHHEHPFPGD SCTGPIFKLM NIQQQLMKTN LKQMDNLMPL
MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT ESPCDLSSIV
EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC LQSLPDCGVK GTEGLSSCGN
RDEETGTKSS AMPTDRESLS SGDAVLQRDL VMEPGTAQYS SGGELGGIST TNVSTPDTAG
EMEHGLMNPD ATVRKNVLQG GESTKERFEN SNIGTAGASD VHVTNKPVDK VSVPNCAPAA
SSLDGNKPAE SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG
LEPYTLLAAG IGEAMSLSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS PICSTTGDNK
LCADCACQQN TVTSSGDLVA KLCDNIVSEP ESTTARQPSS QDPPNASHCE DPQAHTVASD
PVRDTQEHVD FCPFKVVDNK GQRKDVKLDK PLTNMLEVVS RPHPVVPKME KELVPDQAVI
SDSTFSLANS PGSESVTKDD ALSFVPSQKE KGTATPELHT ATDCRDGPDG DSNEPDTLPL
EDRAAGLSTS STAAELQHGM GNTSLTGLGG EHEGPAPPAT PEALNIEGNT DSSLQSVGKA
TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE QRTPPPGQDT
LQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETERNKE VAPQVSLLTQ GGAAQSLVPP
GASLATESRQ EALGAEHNSS ALLPCLLPDG SDGSDALNCS QPSPLDVGVK NTQSQGKTSA
CEVSGNVTVD VIGVNALQGT AEPRRENISH NTQDILIPNV LLSQEKNAIL GLPVALQDKA
VTDPQGVGTP EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VPKELPTDME
LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCTVSAEDAP LPKGADLIEE AASRIVDAVI
EQVKAAGALL TEGEACHMSL SSPELGPLTK GLGNAFTEKV STFPPGESLP MGSTPEEATG
SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD VKAEDEVDFR ASSISEEVAV GSIAATLKMK
QGPMTQAINR ENWCTIEPCP DAASLLASKQ SPECENFMDV GLGRECTSKQ GVLKRESGSD
SDLFHSPSDD MDSIIFPKPE EEQLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN
RSRDQQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV LRSSMRSLSP
FRRHSWGPGK NAASDAEMNH RSMSWCPSGV QYSAGLSADF NYRSFSLEGL TGGAGVGNKP
SSSLEVSSAN AEELRHPFSG EERVDSLVSL SEEDLELGQR EHRMFDQQIC HRSKQQGFNY
CTSAISSPLT KSISLMTISH PGLDNSRPFH STFHNTSANL TESITEENYN FLPHSPSKKD
SEWKSGTKVS RTFSYIKNKM SSSKKSKEKE KEKDKIKEKE KDSKDKEKDK KTVNGHTFSS
IPVVGPISCS QCMKSFTNKD AYTCANCSAF VHKGCRESLA SCAKVKMKQP KGSLQAHDTS
SLPTVIMRNK PSQPKERPRS AVLLVDETTT TPIFANRRSQ QSVSLSKSVS IQNITGVGND
ENMSNTWKFL SHSTDSLNKI SKVNESTESL TDEGVGTDMN EGQLLGDFEI ESKQLEAESW
SRIIDSKFLK QQKKDVVKRQ EVIYELMQTE FHHVRTLKIM SGVYSQGMMA DLLFEQQMVE
KLFPCLDELI SIHSQFFQRI LERKKESLVD KSEKNFLIKR IGDVLVNQFS GENAERLKKT
YGKFCGQHNQ SVNYFKDLYA KDKRFQAFVK KKMSSSVVRR LGIPECILLV TQRITKYPVL
FQRILQCTKD NEVEQEDLAQ SLSLVKDVIG AVDSKVASYE KKVRLNEIYT KTDSKSIMRM
KSGQMFAKED LKRKKLVRDG SVFLKNAAGR LKEVQAVLLT DILVFLQEKD QKYIFASLDQ
KSTVISLKKL IVREVAHEEK GLFLISMGMT DPEMVEVHAS SKEERNSWIQ IIQDTINTLN
RDEDEGIPSE NEEEKKMLDA RARELKEQLQ QKDQKILLLL EEKEMIFRDM AECSTPLPED
CSPTHSPRVL FRSNTEEALK GGPLMKSAIN EVEILQGLVS GNLGGTLGPT VSSPIEQGVV
GPVSLPRRAE TFGGFDSHQM NASKGGEKEE GDDGQDLRRT ESDSGLKKGG NANLVFMLKR
NSEQVVQSVV HLHELLSALQ GVVLQQDSYI EDQKLVLSER ALTRSLSRPS SLIEQEKQRS
LEKQRQDLAN LQKQQAQYLE EKRRREREWE ARERELRERE ALLAQREEKV QQGQQDLEKE
REELQQKKGT YQCDLERLRA AQKQLEREQE QLRREAERLS QRQTERDLCQ VSHPHTKLMR
IPSFFPSPEE PPSPSAPSIA KSGSLDSELS VSPKRNSISR THKDKGPFHI LSSTSQTNKG
PEGQSLAPAS TSASTRLFGL TKPKEKKEKK KKNKTSRSQP GDGPASEVSA EGEEIFC
//
