ID A0A3Q7SB38_VULVU Unreviewed; 2877 AA.
AC A0A3Q7SB38;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=A-kinase anchor protein 13 isoform X5 {ECO:0000313|RefSeq:XP_025857169.1};
GN Name=AKAP13 {ECO:0000313|RefSeq:XP_025857169.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025857169.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025857169.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857169.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025857169.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_025857169.1; XM_026001384.1.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1777..1824
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1980..2177
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2217..2319
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 302..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2453..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2686..2791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2333..2364
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2557..2668
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 302..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2465..2488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2703..2719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2731..2756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2877 AA; 312775 MW; 81D288E18C0DAF24 CRC64;
MKLNPQQAPL YGDCVVTVLL AEEDKVEDDV VFYLVFSGST LYHCTSTRKV SADTLETIAP
GHDCCETVKV LLCASKEGLP VFVVAEEDFQ FIQDEAYDAA QFLATSAGNQ QALNFTRFLD
RSGPPSGDVN SLDEKVALAF RHLKLPAEWN VLGTDQTLHD GSPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT QENAEEPDSW SSLSYEIPYG
DCSVRHHREL DVYTLTSESK SHHEPSVPGN SCTGHIFKLM NIQQQLMKTN LKQMDNPIPL
MVTAQDPSSV PSAQDSDGQF LCCTSDPRDS QPHSYLPEDP ESSPCGQGST VGEIEGSSDF
SCVAKEENTD CSCKKETKGV EKEGEEAEPS LTVDCGTMSD LSSRSLSMPA CGGKGMGTLP
PCGIRNGETG TKSSALATDQ ESLDTGDSVL QGDGGMQPAT APTQHFSGCE LAAGIPVTPG
EMESGPVNAH AAIQKNVLEV RESTKEKLEN SNIITDGSSD VKVTNQTADK ASVPNCVSAT
SSPDGDKPAE SLLAFSNGEA SPVKTAETET SRSYEGSAGA PMDQSSLVIP AAAEDTTSDG
LELYAPLTGT SEAASPSDLT FPRPQKDAPN HKSEPESSHI QSQTSRSPIC STTRGDTPCA
AFACGQSSVT SSGMLAAEYC DGIVTQPEST TPGLPPTQHP PLALCCEGSQ ANAATPGPMR
DTLEQVEFCP VEVSDKKGQG EDLKLGTSST NMLEVHPQAV VPKAKKELVP DQAVTSDKTF
SLASSPGSES VTKDDALFLF PSQKEKGIAT PELHTAADGR DGPGRDSNDP DKQPLEDGAT
GLSTPSLAVQ LQPSMGNTSP MGLGGEHGSV CLSAAPEVLD IEGAVDSSVL CAGKAAVASD
SILTEEGKNL VVPESSEAQG QDGRDKAAAC SFLKEDTHSS GTFQEEQRTP PPGQEALGFC
GEPGSAACAE DRARKRGNSL GTPSACLNAE TEHNKEVAPP VSLLTEGGAA QSLVPLGASL
AADPSQEALG AQKSSSALLP DLLPDLLPDL LPDLLPDGSE ALSRNGSFAL DVGVQNPESQ
GKNTAHEVSG NVQLDVAVVN ALQGNAGARR KAISHNARDL PIPEVLSQEK NMFLGFPGAL
ADEGVTDLQG AAAPEMVPLR GKERDNNCGL ANSGKAQVDP KAHHILEQPL AKELPTETGL
SSSGDQALGR ARGTLLLPCA VPLPKGADSI EEAACRIVEA VLDQVRFSGA LITGQEISHM
SLSRPSESDP VTEQPEGAST GQVSTFLPVQ TVHMGSICEE APGTFAGYLA ETEEPEKMVL
PAEGSEPATE MPDLKAADEV DFLSNTGVSS ASTEVAVKDA ATPPDMKQGL MTQAINRESW
CTIKPCPDAT SLLAAAQSPE CENFLDVGLS RECASKQAVL KRESGSDSDL FHSPSEEVDS
IIFPKPEEEQ LVCDITGSSS STDDTASLDR HSSHGSDVSL PQISNLNRSR DQQCLDSFYS
HGVGAEGRES EGEAAGSGEM EEEEMDSITE VPANCSVLRS SMRSLSPFRR HSWGPGKNAA
SDAEMNQRSM SWCPSGVQYS AALSADFNYR SFSLEGLTGG AGAGNKPSSS LDVNSINTKE
LRHPFNGEER GDSLVSLSEE DLESGQREHR MLDQQACHRS KQQGFNYCTS AISSPLTKSI
SLMTISHPGL DHSRPFHSTS ANLTESITEE TYSFLPQSPS KKDFEGKSGT KVSRTFSYIK
NKMSSSKKSR QEKEKEKEKI KEKEKDLKEK DKKTINGHTF SPIPVVGPIS CSQCVKPFTS
KDAYTCAGCS AFVHKGCRES LASCAKVKMK QPRGSLQAQD TSSLPTVIMR SKPSQPKERP
RSAVLLADEA TAIPMFANRR SQQSISLSKS VSIQNIAGVG NDENISNTWK FLSHSTDSLN
KISKVNESTE SLTDEGVGTD MNEGQLMGDF EMESKQLEAE SWSRVVDSKF LKQQKKDVVK
RQEVIYELMQ TELHHIRTLK IMSDVYSRGM MTELLFEQQT VEKLFPCLDE LISIHSQFFQ
RILERKKESL VDKSEKNFLI KRMGDVLVNQ FSGENAERLK KTYGKFCGQH NQSVNYFKDL
HTKDKRFQAF VKKKMSSAVV RRLGIPECIL LVTQRITKYP VLFQRILQCT KDNEVEQEDL
AQSLSLVKDV IGAVDSKVAS YEKKVRLNEI YTKTDSKSIM RMKSGQMFAK EDLKRKKLVR
DGGVFLKNAA GRLKEVQAVL LTDILVFLQE KDQKYVFASL DQKSTVISLK KLIVREVAHE
EKGLFLISMG MKDPEMVEVH ASSKEERNSW IQIIQDTINT LNRDEDEGIP SENEEEKRIL
DTKARELKEQ LQQKDQQILL LLEEKEMIFR DMTECSTPLP EDCSPTHSSR ILFRSNTEEA
LKGGPLMKSA INEVEILQGL VSGSLGGTLG PAVSSPVEQE GIVGPVSLPR RAETFGGFDS
HQMNASKGGE KEEGEDGQDL RRTESDSGLK KGGNANLVFM LKRNSEQLVQ SVIHLHELLS
TLQGVVLQQD SYIEDQKLLL AERALTRSSS RPSSLVEQEK QRSLEKQRQD LANLQKQQAQ
HLEEKRRRER EWEARERALQ EREARLAQRE QDVWRGQQDL DREREELQHK KGAYQCDLER
LRAAQKQLER EQEQLKRDAE RLSQRQVEHD ACQVSYQHTK LLRIPSFFPN PEEPPMPSVP
SIAKSGSLDS ELSVSPKRNS ISRTHKDKGP FHILSSTSQT NKVPEGQSQT PVPASASTRL
FGLAKPKEKK EKKKKNKGSR SQPCGELPTP GPLQPHCPQI LKGGQVSVAW GWLNWGHSGV
CCLARRTCFA CEGCWDSHLE YQLCGHLRHP PPLCTRVPRR VCRSHIPGIC FPTEAPR
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