ID A0A2Y9QWB3_TRIMA Unreviewed; 2561 AA.
AC A0A2Y9QWB3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A-kinase anchor protein 13 isoform X3 {ECO:0000313|RefSeq:XP_023583659.1};
GN Name=LOC101359092 {ECO:0000313|RefSeq:XP_023583659.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023583659.1};
RN [1] {ECO:0000313|RefSeq:XP_023583659.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_023583659.1; XM_023727891.1.
DR Proteomes; UP000248480; 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:UP000248480};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1533..1580
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1736..1933
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1973..2075
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2205..2250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2299..2321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2462..2561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2089..2120
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2221..2244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2486..2514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2561 AA; 280188 MW; A1AF71F9344FBB0B CRC64;
MKTNLKQMDN LMPLMVTAQD PSSLPSTPGI DGQSLPCASE PMDSLQPSPP PPKYTGSTPC
CQGSSAKGQI ESSCDLSSVV KEENTVCSCQ EEDKGVERNG EEVEPTPVVD SGTVSDQDSC
PQSMPDCGKK GTEGFVSCGN RNEETGTKSC GMTADQESLS SGDNVLQEDL AAEPGTAQHF
SGGELTVSST TDVSVPETVG ETEHGLMNPD STFQKNVLEV GESTKERIEN FHLSTAGASD
IKATSKPVDK ASVPNCVSAT SSLDDHKPAE SLLAFSNGEN STEKTTETET SRRSYEESAD
VPVGQNSLVI PAASKDKILD GSKPDTPSAS ICEAVSASDL TFPGPEKDLI PNQKSETNSS
HVESQSSRSP IYPITGDDKL CADSACQQQN TVTSSGKLMA KHCDDIVAQP EDSITGQPIT
QHPPSAVLCE DPQINAIISD PVRDTQEHAD LCPPEVTDKE GQGEDLNLDI PLTNMCEVAL
DPHPVVPKAE KEVVQDQAVT SDSTFSPASR PGSESVTKDD ALSPVPSQKE KGTATPELHQ
ATDCRDDPGG DSSDPNKQPL EDSTASLDTS FSATDLQPRM GNTSSLGLGG QHEEPCPSAA
SEVLSIEGLD TESSLLSVSK ASLATDSVLT GEGKQLVVPE SSAAQGQDDK DKAVICHFIE
EDSLSSGVLQ EEQRTPPPGK EALGFCEEPS SAACAEGNTL QHSNSLDTSS AFLNVETENN
KKVAPQGSLL TEGGAAQSLV PPGASLTVAS RQEALGPEQS NPPLLLGLVP DSSEALNYSQ
SFVQDAGVKD AQTQGETAAC EVNENVTLDV AMVSTQQDTV GARRKDISHN TQDIPASKVL
LSPEKNMILG LPEALPDKSM TDLQVAVTPE VLPLDWEKGK LEGAGHSCTL GNSKEAQMDD
EANQVPLQPV AKELTADRGL STTENRAPPG MKEVRQAAAP RKERSVPTLS STVSAKAVTL
PEGADLIEEA ASQIVAVVIE RVKASGALIT DREISHILPP SPSESGPVTE QLENVSPEKV
NAFLPGQTPQ VVSIHGEATV NVAGCCAGKE EPEKSILPVQ GPEPATEMPD TKAEDEVDFL
SNSKKSSVSE ELTVGHITTP MMKQNPKTQV INQESWCTIE PCPEAASLLS PKQSPECDEN
FLDVGLGREC TSSQSGLKRQ SGSDSDLFHS PSDEMDRIVF SKPEEEQLVC DTTGSSSSTD
DTASLDRHSS HGSDVSLPQI SNLNKSKDPQ SLDGFYSHGM GAERLESESE PTGSGEMEEE
EMDSITEVPA NCSVLRGSMR SLSPFRRHSW GPGKNAASDA EMNQRSSMRV LGDVVRRPPI
HRRSMSWCPS GVQYSAALSA DFTCRSFSLE GLTGGADVRN KPSSSLEANS ANTKELRHPF
SVEARGDSLV SLSEEDLESG QRERRMFDQQ TSHRSKQQGF NYCTSAISSP LTKSISLMTI
SHPGLDNTRL FHNTSANLAE SITEENYDFL PQSPSKKDFE GKSGTKVSRT FSYIKNKMSS
SKKSKEKEKE KDKIKEKEKD SKEKEKDKKT LNGHTFGSIP IVGPISCSQC MKPFTNKDAY
TCANCGAFVH KGCRESLASC AKVKMKQPKG SLQAHDTSSL PTVIMRNKPS QPKERPRSAV
LLADENTAAP MFANRRSQQS VLLSKSVSIQ NIAGVGNDES MSNTWKFLSH STDSLNKISK
VNESTESLTD EGVGTDMNEG QLMGDFEIDS KQLEAESWSR IVDSKFLKQQ KKDVIKRQEV
IYELMQTELH HIRTLKIMSD VYSRGMMTDL LFEQQMVEKL FPCLDELISI HSQFFQRILE
RKKESLVEKS EKNFLIRRIG DVLVNQFSGE NADRLKKTYG KFCEQHNQSV NYFKDLYTKD
KRFQAFVKKK MSSSVVRRLG IPECILLVTQ RITKYPVLFQ RMLQCTKDND VEQEDLAQSL
SLVKDVIGAV DSRVASYEKK VRLSEIYTKT DSKSIMRMKS GQMFAKEDLK RKTLVRDGSV
FLKNAAGRLK EVQAVLLTDI LVFLQEKDQK YVFASLDQKS TVISLKKLIV REVAHEEKGL
FLISMGMKDP EMVEVHASSK EERNSWIHII QDTINTLNRD EDEGIPSENE EEKKMLDTKA
RELKEQLQQK DQQILHLLEE KEMIFRDMTE CSTPLPEDCS PTHSSRILFR SNTEEALKGG
PLMKSAINEV EILQGLVSGS LGGTLGPAVS SLIEQEGMVG PVSLPRRAET FGGFDSHQMN
ASKGGEKEEG DDGQDLRRTE SDSGLKKGGN ANLGFMLKRN SEVIQSIVHL HELLSTLQGV
VLQQDSYIED QKLMLSERAL TRSSSRPSSL IEQEKQRSLE KQRQDLANLQ KQQAQHLEEK
RRREREWEAR ERELLEREAR LAQWEEKVQR GQQDLERDRE ELQQKKGTYQ YDLERLRAAQ
KQLEREQEQL KRDTEQLSQR RIEGDVCQVS HQHTKTMRIP SFCPNPEESP LPSAPSVVKS
VSLDSELSMS PKRNSISRTH RDRTFHILSS ASQTSRVPEG SSQTPVSTST SARLFGLAKP
KEKKEKKKKS KGGRPQPGGE YTHPPAPGSE EWGLRFQKGI F
//
