ID A0A2K5I1Z3_COLAP Unreviewed; 1430 AA.
AC A0A2K5I1Z3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=A-kinase anchoring protein 13 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000010655.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000010655.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCANT00000033545.1; ENSCANP00000010655.1; ENSCANG00000028557.1.
DR Proteomes; UP000233080; 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; 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:UP000233080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 407..454
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 610..807
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 847..949
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 47..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 963..994
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1187..1298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 161510 MW; C6BA03C47167C60A CRC64;
MLYINRENWC TIEPCPDAAS LLASKQSPEC ENFLDVRLGR ECTSKQGVLK RESGSDSDLF
HSPSDDMDSI VFPKPEEEQL TCDITGSSSS TDDTASLDRH SSHGSDVSLS QILKPNRSRD
RQSLDGFYSH GMGAEGRESE SEPADPGDME EEEMDSITEV PANCSVLRSS MRSLSPFRRH
SWGPGKNAAS DAEMNHRSSM RALGDVVRRP PIHRRSFSLE GLTGGAGVGN KPSSSLEVSS
ANAKELRHPF GGEERVDSLV SLSEEDLESG QREHRMFDQQ ICHRSKQQGF NYCTSAISSP
LTKSISLMTI SHPGLDNSRP FHSTFHNTSA NQTESVTEEN YNFPPQSLFK KDSEWKSATK
VSRTFSYIKN KMSSSKKSKE KEKEKDKIKE KEKDSKDKEK DKKTLNGHTF SSIPVVGPIS
CSQCMKPFTN KDAYTCANCS AFVHKGCRES LASCAKVKMK QPKGSLQAHD TSSLPTVIMR
NKPAQPKERP RSAVLLVDET TTTPIFASRR SQQSVLLSKS VSIQNITGVG NDENMSNTWK
FLSHSTDSLN KISKVNESTE SLTDEGVGTD MNEGQLLGDF EIDSKQLEAE SWSRIIDSKF
LKQQKKDVVK RQEVIYELMQ TELHHVRTLK IMSEVYSRGM MTDLLFEQQM VEKLFPCLDE
LISIHSQFFQ RILERKEESL VDKSEKNFLI KRIGDVLVNQ FSGENAERLK KTYGKFCGQH
NQSVNYFKDL YAKDKRFQAF VKKKMSSSVV RRLGIPECIL LVTQRITKYP VLFQRILQCT
KDNEVEQEDL AQSLSLVKDV IGAVDSKVAS YEKKVRLNEI YTKTDSKSIM RMKSGQMFAK
EDLKRKKLVR DGSVFLKNAA GRLKEVQAVL LTDILVFLQE KDQKYIFASL DQKSTVISLK
KLIVREVAHE EKGLFLISMG MKDPEMVEVH ASSKEERNSW IQIIQDTINT LNRDEDEGIP
SENEEEKKML DTKARELKEQ LQQKDQQILL LLEEKEMIFR DMAECSTPLP EDCSPTHSPR
VLFRSNTEEA LKGGPLMKSA INEVEILQGL VSGSLGGTLG PTVSSPIEQE GAVSPVSLPR
RAETFGGFDS HQMNASKGGE KEEGDDGQDL RRTESDSGLK KGGNANLVFM LKRNSEQVVQ
SIVHLHELLS TLQGVVLQQD SYIEDQKLVL SERALTRSLS RPCSLIEQEK QRSLEKQRQD
LANLQKQQAQ YLEEKRRRER EWEARERELR EREALLAQRE EKVQQGQQDL EKEREELQQK
KGTYQYDLER LRAAQKQLER EQEQLRREAE RLSQRQTERD LCQVSHPHNK LMRIPSFFPS
PEEPASPSAP SMAKSGLLDS ELSVSPKRNS ISRTHKDKGP FHILSSTSQT NKGPEGQSQA
PVSTSASTRL FGLAKPKEKK EKKKKNKTSR SQPGDGPTSE VSAEGEEIFC
//
