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Database: UniProt
Entry: A0A3Q7SNL0_VULVU
LinkDB: A0A3Q7SNL0_VULVU
Original site: A0A3Q7SNL0_VULVU 
ID   A0A3Q7SNL0_VULVU        Unreviewed;      2894 AA.
AC   A0A3Q7SNL0;
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 X3 {ECO:0000313|RefSeq:XP_025857151.1};
GN   Name=AKAP13 {ECO:0000313|RefSeq:XP_025857151.1};
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_025857151.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025857151.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857151.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025857151.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   RefSeq; XP_025857151.1; XM_026001366.1.
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          1795..1842
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1997..2194
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          2234..2336
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          1547..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1757..1787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2470..2509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2703..2808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2350..2381
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2574..2685
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        1763..1787
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        2720..2736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2748..2773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2894 AA;  314786 MW;  5AFB5AA09D4AE4B3 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
     SDAEMNQRSS LQVLGDVVRR PPIHRRSMSW CPSGVQYSAA LSADFNYRSF SLEGLTGGAG
     AGNKPSSSLD VNSINTKELR HPFNGEERGD SLVSLSEEDL ESGQREHRML DQQACHRSKQ
     QGFNYCTSAI SSPLTKSISL MTISHPGLDH SRPFHSTSAN LTESITEETY SFLPQSPSKK
     DFEGKSGTKV SRTFSYIKNK MSSSKKSRQE KEKEKEKIKE KEKDLKEKDK KTINGHTFSP
     IPVVGPISCS QCVKPFTSKD AYTCAGCSAF VHKGCRESLA SCAKVKMKQP RGSLQAQDTS
     SLPTVIMRSK PSQPKERPRS AVLLADEATA IPMFANRRSQ QSISLSKSVS IQNIAGVGND
     ENISNTWKFL SHSTDSLNKI SKVNESTESL TDEVGTDMNE GQLMGDFEME SKQLEAESWS
     RVVDSKFLKQ QKKDVVKRQE VIYELMQTEL HHIRTLKIMS DVYSRGMMTE LLFEQQTVEK
     LFPCLDELIS IHSQFFQRIL ERKKESLVDK SEKNFLIKRM GDVLVNQFSG ENAERLKKTY
     GKFCGQHNQS VNYFKDLHTK DKRFQAFVKK KMSSAVVRRL GIPECILLVT QRITKYPVLF
     QRILQCTKDN EVEQEDLAQS LSLVKDVIGA VDSKVASYEK KVRLNEIYTK TDSKSIMRMK
     SGQMFAKEDL KRKKLVRDGG VFLKNAAGRL KEVQAVLLTD ILVFLQEKDQ KYVFASLDQK
     STVISLKKLI VREVAHEEKG LFLISMGMKD PEMVEVHASS KEERNSWIQI IQDTINTLNR
     DEDEGIPSEN EEEKRILDTK ARELKEQLQQ KDQQILLLLE EKEMIFRDMT ECSTPLPEDC
     SPTHSSRILF RSNTEEALKG GPLMKSAINE VEILQGLVSG SLGGTLGPAV SSPVEQEGIV
     GPVSLPRRAE TFGGFDSHQM NASKGGEKEE GEDGQDLRRT ESDSGLKKGG NANLVFMLKR
     NSEQLVQSVI HLHELLSTLQ GVVLQQDSYI EDQKLLLAER ALTRSSSRPS SLVEQEKQRS
     LEKQRQDLAN LQKQQAQHLE EKRRREREWE ARERALQERE ARLAQREQDV WRGQQDLDRE
     REELQHKKGA YQCDLERLRA AQKQLEREQE QLKRDAERLS QRQVEHDACQ VSYQHTKLLR
     IPSFFPNPEE PPMPSVPSIA KSGSLDSELS VSPKRNSISR THKDKGPFHI LSSTSQTNKV
     PEGQSQTPVP ASASTRLFGL AKPKEKKEKK KKNKGSRSQP CGELPTPGPL QPHCPQILKG
     GQVSVAWGWL NWGHSGVCCL ARRTCFACEG CWDSHLEYQL CGHLRHPPPL CTRVPRRVCR
     SHIPGICFPT EAPR
//
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