ID A0A2I2UQH8_FELCA Unreviewed; 1431 AA.
AC A0A2I2UQH8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=A-kinase anchoring protein 13 {ECO:0000313|Ensembl:ENSFCAP00000034675.2};
GN Name=AKAP13 {ECO:0000313|Ensembl:ENSFCAP00000034675.2,
GN ECO:0000313|VGNC:VGNC:82456};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000034675.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000034675.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000034675.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000034675.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000034675.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000034675.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000034675.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AANG04000441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000034675; -.
DR Ensembl; ENSFCAT00000045235.3; ENSFCAP00000034675.2; ENSFCAG00000029834.4.
DR VGNC; VGNC:82456; AKAP13.
DR GeneTree; ENSGT00940000154146; -.
DR InParanoid; A0A2I2UQH8; -.
DR OMA; SIMTFHG; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000029834; Expressed in zone of skin and 10 other cell types or tissues.
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: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: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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 409..456
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 611..808
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 848..950
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 109..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 968..995
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1188..1233
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1262..1299
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 234..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1431 AA; 160421 MW; 34F51248D28EA207 CRC64;
MYERHKRRYS LCDISKVDRT VDVVLLKINR ESWCTIQPCP DAASLLAPTQ SPGCDSFLDV
GLARECASKP GVLKRESGSD SDLFQSPSEE VDSIIFSKPE EEQLVCDITG SSSSTDDTAS
LDRHSSHGSD VSLPQISNLN RSRDQQCLDS FYSHGAGAEG RESEGEAAGS GEMDEEEMDS
ITEVPTNRSV LRGSMRSLSP FRRHSWGPGK NAASDAEMNQ RSFSLEGLTG GAGVGNKPSS
SLDVNSANTK ELRHPFSGEA RGDSLMSLSE EDLESGQREH RMFDQQACHR SKQQGFNYCT
SAISSPLTKS ISLMTISHPG LDNSRPFHST SANLTESITE ETYSFLPQSP SKKDFEGKSG
TKVSRTFSYI KNKMSSSKKS REKEKEKEKI KEKEKDLKEK DKDKKTVNGH AFSSIPVVGP
VSCSQCVKPF TSKDAYTCAS CGAFVHKGCR ESLASCAKVK MKPKGTLQAH DTSSLPTVIM
RSKPSQPKER PRSAVLLVEE TTAVPMFATR RSQQSVSLSK SVSIQNIAGV GNDENISNTW
KFLSHSTDSL NKISKVNEST ESLTDEGVGT DMNEGQLMGD FEMESKQLEA ESWSRIVDSK
FLKQQKKDVV KRQEVIYELM QTELHHVRTL KIMSDVYSRG MMTELLFEQQ MVEKLFPCLD
ELISIHSQFF QRILERKKES LVDKSEKNFL IKRMGDVLVN QFSGENAERL KKTYGKFCGQ
HNQSVNYFKD LYTKDKRFQA FVKKKMSSSV VRRLGIPECI LLVTQRITKY PVLFQRILQC
TKDNEVEQGD LAQSLSLVKD VIGAVDSKVA SYEKKVRLNE IYTKTDSKSI MRMKSGQMFA
KEDLKRKKLV RDGSVFLKNA AGRLKEAQAV LLTDILVFLQ EKDQKYVFAS LDQKSTVISL
KKLIVREVAH EEKGLFLISM GMRDPEMVEV HAGSKEERNS WIQIIQDTIN TLNRDEDEGI
PSESEEEKRA LDSRARELKE QLQQKDQQIL LLLEEKEMIF RDMTECSTPL PEECSPTHSS
RVLFRSNTEE ALRGGPLMKS AINEVEILQG LVSGSLGGTL GQAVSSPVEQ EGTVGPVSLP
RRAETFGGFD SHQMNASKGG EKEEGEDGQD LRRTESDSGL KKGGNANLVF MLKRNSEQVV
QSVVHLHELL STLQGVVLQQ DSYIEDQKLL LAERALSRGS SRPSSLVEQE KQRSLEKQRQ
DLANLQRQQA QHLDEKRRRE REWEARERAL QEREARLAQR EQDVRQGRQD LDRDRDELQF
KKGAYQCDLE RLRAAQKQLE REQEQLRRDA ERLSQRQAEH DACQVSHPHT KLLRIPSFFP
NPEESPLPSV PAIAKSGSLD SELSVSPKRN SISRTHKDKG PFHILSSTSQ TNKVAEGPSP
APVPASASTR LFGLAKPKEK KEKKKKNKGS RSQSGDGPAS EVPTEGEEIF C
//
