ID A0A384BB61_BALAS Unreviewed; 1671 AA.
AC A0A384BB61;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=A-kinase anchor protein 12 {ECO:0000313|RefSeq:XP_007196937.1};
GN Name=AKAP12 {ECO:0000313|RefSeq:XP_007196937.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007196937.1};
RN [1] {ECO:0000313|RefSeq:XP_007196937.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007196937.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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DR RefSeq; XP_007196937.1; XM_007196875.2.
DR STRING; 310752.A0A384BB61; -.
DR GeneID; 103016243; -.
DR KEGG; bacu:103016243; -.
DR CTD; 9590; -.
DR InParanoid; A0A384BB61; -.
DR OrthoDB; 4259343at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
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 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; 2.
DR PROSITE; PS51893; AKAP_CAM_BD; 3.
PE 4: Predicted;
KW Calmodulin-binding {ECO:0000256|PROSITE-ProRule:PRU01241};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681}.
FT DOMAIN 500..520
FT /note="A kinase-anchoring proteins AKAP-5 and AKAP-12
FT calmodulin (CaM)-binding"
FT /evidence="ECO:0000259|PROSITE:PS51893"
FT DOMAIN 650..670
FT /note="A kinase-anchoring proteins AKAP-5 and AKAP-12
FT calmodulin (CaM)-binding"
FT /evidence="ECO:0000259|PROSITE:PS51893"
FT DOMAIN 695..715
FT /note="A kinase-anchoring proteins AKAP-5 and AKAP-12
FT calmodulin (CaM)-binding"
FT /evidence="ECO:0000259|PROSITE:PS51893"
FT REGION 7..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 500..520
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01241"
FT MOTIF 650..670
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01241"
FT MOTIF 695..715
FT /note="AKAP CaM-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01241"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 180713 MW; 8E87B21FCE2CB9A3 CRC64;
MLGIIAITVG QRESEDASER DSDKDMAADS AAVQDITKEG QEEMPETMEQ TPASESSVDE
LTQPAEAQAN DVGFKKVFKF VGFKFTVKKD KTEKSDTVQL LTVKKEEDGG PGGSDGAGDH
REPSQETGDA TPKDTELKES TEKPEETPRH EQSRPEVSLQ AESAPPAEEG KDEGEEEQEK
EPARSPDSPT SPVASETASP FKKFFTQGWA GWRKKTSFRK AREDELEASE KKKEQEPEKA
DTEENEKTED LSERPPSQEA RESAQDARLS AEYEKVELPP EDQVQAPPEE KPAPLATEVF
DEKVEIVAEV HVSTAEKDTE EQKAQAEEIV EPSPPEQTLE TDADLQDAEP TEARLRMEEE
AGAASGDHAQ PAELGAGADA KAPPTPPEGI VGEAEMPSSQ ERVKVQGSPL KKLFTSSGLK
KLSGKKQKVK RGGDEESREQ HPASADSPDS PDEPKAESSA SSPEEPEEIT CLEKGVAEAP
QDGETEEGTT SDGEKKREGV TPWASFKKMV TPKKRVRRLS ESDKEDEVDK VKSATLSSTE
SAASEVQEEG KGNGEEQKPE EPKRKVDTSV SWEALICVGS SKKRARKASS SDDEGGPKPL
GGGDSQKPEE AGRDREPGPD ALPAGSQDHD QPPGSSSPEQ ASSPCEGEGV STWESFKRLV
TSRKKSKSKL EEKSEDLVAG SGLEYSASDA ELGKEESWVS IRKFIPGRRK KRLDGKQEQA
TMEDTGPTEV NEDDSDVPAV VPLSEYDAVE REKTEAQQAP KSEEGPEQRL AVDVSEELSK
SLVHTVTVAV MDGTRAVTNI EERAPSWISA SVTEPLEQAE DEDKSPSGEV FEEEVVAEET
PVDTKTLPES QEATDDTIAS KVELAPEALT AAETTEASCA EEATEASGAE ETTDMVSAVS
QLTDFPDTTE EATPVQEVEG SVPDMEDQAK RTQEVLQAVA EKVKEESQLP DARGLDDTIQ
TTQKGQAKIL EQVEEAEEDS HALDWKEAMD GASKVHVQET KTETLTQGPV IVQATPESLE
KVPPGTESAE ARELTSTCPA ETVAAVKPET VPEQAVAPDS AETLTDSETN GSTPVADFEA
TNVSQQTKIM EIDEDGEVPS GTQYQVTEGE ALPALKEKPP EPSNFQSQEE KHSEMEEVLE
HTDKEVTVET VPILSKTEVI QEAGRCADEE TKEEPSVEGL VVSADTEITE KKITEVALED
EVTKKAEFQN DDLQLQSPAK SLPTPVERER VVEVERDKTE LEPTQVNEEK LECKPAVTTC
EELTKQLVQA VNVTVIDGEK EVISFEGSSS LPVHEEEACT EIQVQSSEAS LALAAAAVGE
KVLAEAIKVL ETAETLESAE ARLVPEEKSS EKDEVSPAQP GEDAVPTGTE SQAVSIPVIV
SVTPEKGIIA DLEGDKTTSQ KWESDGDSEQ VGCQEGRVSK TREEDLKAEN EILKLQTESC
KLVQNVIQTV VDQLGSTEET AAAFQTQAQL MEADSQEAGQ KIEKEESKLQ ACTLDETQTI
EAKEESPLSA GEHTHPDVSK DVNEALEKMA ATRVESSRVG GQQLEEVAFP SKEKREAPET
KSVPEDDGGA GFGERTEKSS PFESQEDEKG DAADDPGNQT SAPEDAEASG GSTSESPDTI
GPKLKEKGDG QEVEFQEEKG QSESEKEIKT QTQEETQDQE REPAKPEPTE S
//
