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Database: UniProt
Entry: F7FKK9_CALJA
LinkDB: F7FKK9_CALJA
Original site: F7FKK9_CALJA 
ID   F7FKK9_CALJA            Unreviewed;      2832 AA.
AC   F7FKK9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=A-kinase anchoring protein 13 {ECO:0000313|Ensembl:ENSCJAP00000023955.4};
GN   Name=AKAP13 {ECO:0000313|Ensembl:ENSCJAP00000023955.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000023955.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000023955.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000023955.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   STRING; 9483.ENSCJAP00000023955; -.
DR   Ensembl; ENSCJAT00000025340.5; ENSCJAP00000023955.4; ENSCJAG00000009388.5.
DR   eggNOG; KOG3520; Eukaryota.
DR   GeneTree; ENSGT00940000154146; -.
DR   HOGENOM; CLU_000597_0_0_1; -.
DR   InParanoid; F7FKK9; -.
DR   TreeFam; TF325887; -.
DR   Proteomes; UP000008225; Chromosome 6.
DR   Bgee; ENSCJAG00000009388; Expressed in testis and 6 other cell types or tissues.
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:UP000008225};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1811..1858
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          2012..2209
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          2249..2351
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          305..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1196..1226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1469..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1777..1813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2485..2526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2720..2832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2365..2396
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2589..2700
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        325..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..952
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1469..1496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1779..1810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2497..2520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2735..2752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2763..2788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2832 AA;  309959 MW;  0F7A35C7DD272465 CRC64;
     MKLTPQQAPL YGDCVVTVLL AEEDKVADDV VFYLVFSGST LHHCASTRKV SSDTLETITP
     GHDCCETVKV QLCASKEGLP VFVVAEEDFH FIQDEAYDAA QFLATSAGNQ QALNFTRFLD
     QSGPPSGDVN SLDKKVVLAF RHLKLPAEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT
     WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
     DCSVRHHREL DIYTLTSESE SQYEHPFPGD SCTGHIFKLM NIQQQLTKTN LKQMDNLKPL
     MVTAQDSSGA PQTDGQFLPC APEPMDSQQL SSPEETESSQ CCPGSSVAQT ESPCDLSSIV
     EEENTDRSCR KKNKGMERKG EEVGPAPIVD SGTVSDQDSC LQSLPDYGVK GTKRRLSCGN
     KNEETGTKSS GMPTDEESLS SGDAVLQRDV VMVPGTAQYS SAGELASIST TDVGTPESAG
     EAEHGLMNPD ATVQKNVLQV GESTKDNMGT AGASDMQVTS KPVDKVSVPN CASATSSLGG
     NKPAESSLAF SNEETSIEKT AETETSRSCE ESVHAPVEQN SVVLPAAAKD KISDGLEPCT
     VLAGIGEATS PSDLALPRLE VDVMPHQNSE INSSHAQSQK GKSSPICSTT GDYKLCSNSA
     CQQNTVTSSG ELVAQLCDNI VSQPKSTTAR QPNSQDPPKA THCEDPQANT ITSDPVRDTQ
     ERVDFCPFKV VDNEGQGKDV KFDKSLANML EVPSHPHPVV PKMEKELVPD QAVISDSTFF
     LANSPGSESV TRDDALSFVP SQKEKGTATP ALHEATDCRD GPDGDANDPD TQPLEDRAAG
     LSPCSTVAEL QLVMGNTSLT RLGGEHEGPA PSAAPEVLSI KGDTDSSLQN AGKATLALDS
     VLTEEGKILV VSESSGAQEQ DKDKAVTSSS IMENALSSGT LQEEQGTPSP EQETPRFHEK
     SISAASAKDE ALQLSNSPGA PSAYLKAETE HNKEVAPQVS LLTQGWAFQS LVLPGTSLGT
     NSRQEALGAE QNSSTLLQCL LPDGCDWSEA LNYSQPSPLD DEVKNTKCQG KPNISSCEVS
     GNVTMDITGF NDVQDTAEPR RKSVSHNTQD ILIPNVSSSQ EKKVILGLPV ALQDKAVTDP
     QGFGTPEMVP LDWVKGKLEG ADHSCNTGDS EEARIDNEAH PVLLQPAAKE LPTKMGLSAH
     HDGTPAGKRE VMRGPPSDRG RSTPSLPCLV SAQAAPLPKG VDLIEEAASR IVDAVIQGVK
     AAGALLTEEK ACHVSASSAE LDPLTEGLEN ASTEKVSAFS PGESLPVGST HEEATGSLGG
     CFAGGEEPEK IILPVRGPEA ATEMPDVKAE DEVDFLSNTR ASSVSEEVAV WSVPATPKTK
     QGPVAQAINR ESWCTIDPCP DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESEND
     SALFHSCSDE MDSIIFPKPE EEQLVCDITG SSSSTDDTAS LDRHSSHGSD ASLSHISKPS
     KSRDRQSLDG FYSHGMGAEG RESESEPVGP GDMEEEEMDS ITEVPANCSV LRSSMRSLSP
     FRRHSWGPGK NAANDAEMNH RSSMRVLGDV VRRPPIHRRS MSWCPPGVQY SAGLSADFNN
     RSFSLEGLTG GAGIGTKPSS SLEVGSVNAK ELRHPFSGEE RGDSLVSLSE EDLESDHREH
     RIFDQQICHR SKQQGFNYCT SAISSPLTKS ISLMTISHPG LDNSRPFHST FHNTSANVTE
     SITEENYNFL PQCPSKKDFE GKSGTKVSRT FSYIKNKMSS SKKSKEKEKE KIKEKEKDSK
     DKEKDKKTLN GHSFSSIPVV GPISCSQCTK PFTNKDAYTC ANCGAFVHKG CRESLASCAK
     VKMKQPRGNL QAQDTSSLPT VIMRNKPSQP KERPRSAVLL VDETTTTQIF ANRRSQQSVS
     LSKSVSIQNI TGVGNDENMS NTWKFLSHST DSLNKISKVN ESTESLTDEG TDMNEGQLLG
     DFEMDSKQLE AESWSRIIDS KFLKQQKKDV VKRQEVIYEL MQTELHHVRT LKIMSDVYSR
     GMMTDLLFEQ QMVEKLFPCL DELIGIHSQF FQRILERKKE SLVDESEKNF LIKRIGDVLV
     NQFSSENAER LKKTYGKFCG QHNQSVNYFK DLYTKDKRFQ AFVKKKMSSS VVRRLGIPEC
     ILLVTQRITK YPVLFQRILQ CTKDDEVEQE DLAQSLSLVK EVIGAVDSKV ASYEKKVRLN
     EIYTKTDSKS IMRMKSGQMF AKEDLKRKKL IRDGSVFLKS AAGRLKEVQA VLLTDILVFL
     QEKDQKYIFA SLDQKSTVIS LKKLIVREVA HEEKGLFLIS MGMKDPEMVE VHASSKEERN
     SWIQIIQDTI NMLNRDEDEG IPSENEEEKK MLDTKARELK EQLQQKDQQI LLLLEEKEMI
     FRDMAECSTP LPEDCSPKHS PRVLFRSHTE EALKGGPLMK SAINEVEILQ GLVSGSLGGT
     LGQTVSSPVE QEGVVGPVSL PRRAETFGGF DSHQMNASKG GEKEEGDDGQ DLRRTESDSG
     LKKGGNGNLV FMLKRNSEQV VQSIVHLHEL LSTLQGVVLQ QDSYIEDQKL VLSERALTRS
     LSRPSSLVEQ EKQRSLEKQR QDLANLQKQQ AQYLEEKRRR EREWEARERE LREREALLAQ
     REEKVQQGQQ DLEKEREELQ QKKGTYQYDL ERLRAAQKQL EREQEQLHRE AERLGQRQAE
     RDLCQVSHPH TKLMRIPSFF PSAEEPPLPS APSIAKSGSL DSELSVSPKR NSISWTHKDK
     GPFHILSSTS QTNKGSEGQS QAPAPTSAST RLFGLAKPKE KKEKKKKNKT SRSQPGDGPT
     SEVSAEGEEI FC
//
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