ID A0A3B4X622_SERLL Unreviewed; 1481 AA.
AC A0A3B4X622;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=A-kinase anchor protein 12-like {ECO:0000313|Ensembl:ENSSLDP00000011586.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000011586.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000011586.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 1841481.ENSSLDP00000011586; -.
DR Ensembl; ENSSLDT00000011999.1; ENSSLDP00000011586.1; ENSSLDG00000009208.1.
DR GeneTree; ENSGT00730000111244; -.
DR OrthoDB; 4259343at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl.
DR GO; GO:0070121; P:Kupffer's vesicle development; IEA:Ensembl.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:InterPro.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IEA:InterPro.
DR GO; GO:1904969; P:slow muscle cell migration; IEA:Ensembl.
DR InterPro; IPR028540; AKAP12.
DR InterPro; IPR001573; AKAP_WSK.
DR PANTHER; PTHR23209; A-KINASE ANCHOR PROTEIN 12; 1.
DR PANTHER; PTHR23209:SF4; A-KINASE ANCHOR PROTEIN 12; 1.
DR Pfam; PF03832; WSK; 1.
DR PROSITE; PS51893; AKAP_CAM_BD; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 437..457
FT /note="A kinase-anchoring proteins AKAP-5 and AKAP-12
FT calmodulin (CaM)-binding"
FT /evidence="ECO:0000259|PROSITE:PS51893"
FT DOMAIN 606..626
FT /note="A kinase-anchoring proteins AKAP-5 and AKAP-12
FT calmodulin (CaM)-binding"
FT /evidence="ECO:0000259|PROSITE:PS51893"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 158898 MW; 5971141D23B79551 CRC64;
MLGTITLTVG QPDGVSVAQK DEAPETMGTI QDEVAPQVNG EKVEKESPDA NDISAVEEKA
AEEKPDDANE VGFKKIFRFV GFKFTLKKDK SEEKEPVKLL TVKDKEGEEV SGTEEPTKKE
EAAEEKNTAE EKEADTEAAA AETEVTKDDT DKAEATDALD EGTAAEATDE AVKEEGAEKE
EEATPPSQET TLSPFRKLFS GGLFSNLRKK ASIKKTKEEE DKEAAVEEET AKTEETPAAV
DEKEEKTEAE QETKEEAPAT PEEEKSEPKE EAPVAPEEEK SETTPEPNAT VETPAPAAAT
TDETKQEEEK AEGGAEEEKA PAEVTSEAEL LSSQEKAKPQ GSPLKKLFTG AGLKKLSTKK
QKNKKDAESK LTESGEQAAK QLQSSTELTE APKADSGPSS PEESGEHVIA VEVTQNGSSQ
ETEGEVASDG EKKKEGIIAW SSFKKLVTPK KIVKRSSESE DEATGEKPAK PLPSSESAAL
ADKSVEEDAE EEKPTEEEPK TENTEKLVSS TEEPKRKMDT SVSWEALMCM GGPKKKTRRT
SDSDDDDETK IEEEAAAAAA AAAASAAVEG EQESKTEAPI VTSQNTESEG EVVSSPEPLN
SPPERESTWD TLKRMVMSKN KAKAEEKPEE SAEQVQSDSE APKDESSFSL RKFFPGRRKK
KAEKQASTEM GSGEEDSDTP AVVPMSEYDE QVEAEQEAPA EPAAVQIKVS TEDRSPSWIP
ATVEDIDDKN DQLSDIPEEA ENAATPRSVD TDIAEDETED QATLPPKAPG RMGRRLSTAE
EKPVTLALAA KTTPVPQGPK SGTAQEVVGA IEAQISEIPA QTSVTVEDVQ VEVATENTEY
EPPTETAEAK ENTILVPHAQ DEAMAICTGL GTKEIAKVTL EKPVVPLVEC VAVVRDSLST
EVAIDEKPAS TEKATLAADE VIMAQAQEVE TIDLEPVVEN SQSEATDIQA ATESYEPELE
KVGVINTVLE ETEVIQATSV SENSPKSVVV NPITPTSEIA VCTQSIEVSE PIVETKEVKM
DTEQLAATEE NSPIKEVAQV TTEEMSSTIG ETAKITITKE TEPVIPVVIP SEEAPVITET
VVIVSSLSTE SDQVAISDEV VVKDPAASEA VCDKPVQVEE AKEEGMVVET VEATMVQTAE
SEISVVPEQA TEKTEDIKED VHPAREIEAQ SMVIAQAVIQ DAMEKVSEDK PEPKKPASPT
ATTPTPVQAI ATTEEEIAIT SVAPVITETP VAVICEKPAP KSPQPLHVAM EVTDTIQIEV
IESTDAYVGE EEKKPEEELR QAVEVKVSEE IVVVEEVVEI KAESEELEQV KEEQSKEEEA
VQEPDVKEAA EEVKPQSEET TPEAPSEGEK VLAIHMPVQV VLQTAEVVEE SVAEEAAEEF
ESNGPVTEDT SVKAESPASA SKLSTLSEEA PATASGEVSD PSQVTEAAAS QPETETETET
ETETEKPPSG KCAEVMAQVI EVIEEAVKEI EPVSTEITAA S
//
