ID A0A3Q7T8V2_VULVU Unreviewed; 2799 AA.
AC A0A3Q7T8V2;
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 X9 {ECO:0000313|RefSeq:XP_025857207.1};
GN Name=AKAP13 {ECO:0000313|RefSeq:XP_025857207.1};
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_025857207.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025857207.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857207.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025857207.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_025857207.1; XM_026001422.1.
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 1776..1823
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1979..2176
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2216..2318
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..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2452..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2685..2799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2332..2363
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2556..2667
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 1744..1768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2464..2487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2702..2718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2730..2755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2799 AA; 303946 MW; 82C22C0C2E499C41 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 EKEKEKEKIK EKEKDLKEKD KKTINGHTFS PIPVVGPISC SQCVKPFTSK
DAYTCAGCSA FVHKGCRESL ASCAKVKMKQ PRGSLQAQDT SSLPTVIMRS KPSQPKERPR
SAVLLADEAT AIPMFANRRS QQSISLSKSV SIQNIAGVGN DENISNTWKF LSHSTDSLNK
ISKVNESTES LTDEGVGTDM NEGQLMGDFE MESKQLEAES WSRVVDSKFL KQQKKDVVKR
QEVIYELMQT ELHHIRTLKI MSDVYSRGMM TELLFEQQTV EKLFPCLDEL ISIHSQFFQR
ILERKKESLV DKSEKNFLIK RMGDVLVNQF SGENAERLKK TYGKFCGQHN QSVNYFKDLH
TKDKRFQAFV KKKMSSAVVR RLGIPECILL VTQRITKYPV LFQRILQCTK DNEVEQEDLA
QSLSLVKDVI GAVDSKVASY EKKVRLNEIY TKTDSKSIMR MKSGQMFAKE DLKRKKLVRD
GGVFLKNAAG RLKEVQAVLL TDILVFLQEK DQKYVFASLD QKSTVISLKK LIVREVAHEE
KGLFLISMGM KDPEMVEVHA SSKEERNSWI QIIQDTINTL NRDEDEGIPS ENEEEKRILD
TKARELKEQL QQKDQQILLL LEEKEMIFRD MTECSTPLPE DCSPTHSSRI LFRSNTEEAL
KGGPLMKSAI NEVEILQGLV SGSLGGTLGP AVSSPVEQEG IVGPVSLPRR AETFGGFDSH
QMNASKGGEK EEGEDGQDLR RTESDSGLKK GGNANLVFML KRNSEQLVQS VIHLHELLST
LQGVVLQQDS YIEDQKLLLA ERALTRSSSR PSSLVEQEKQ RSLEKQRQDL ANLQKQQAQH
LEEKRRRERE WEARERALQE REARLAQREQ DVWRGQQDLD REREELQHKK GAYQCDLERL
RAAQKQLERE QEQLKRDAER LSQRQVEHDA CQVSYQHTKL LRIPSFFPNP EEPPMPSVPS
IAKSGSLDSE LSVSPKRNSI SRTHKDKGPF HILSSTSQTN KVPEGQSQTP VPASASTRLF
GLAKPKEKKE KKKKNKGSRS QPCDGPGSEV PAEGEEIFC
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