ID A0A2U4C932_TURTR Unreviewed; 1323 AA.
AC A0A2U4C932;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=A-kinase anchor protein 2 isoform X3 {ECO:0000313|RefSeq:XP_019801962.1};
GN Name=PALM2AKAP2 {ECO:0000313|RefSeq:XP_019801962.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019801962.1};
RN [1] {ECO:0000313|RefSeq:XP_019801962.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019801962.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_019801962.1; XM_019946403.2.
DR GeneID; 101333904; -.
DR OrthoDB; 4318462at2759; -.
DR Proteomes; UP000245320; Chromosome 6.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR InterPro; IPR029304; AKAP2_C.
DR InterPro; IPR004965; Paralemmin.
DR PANTHER; PTHR10498:SF10; PALM2 AND AKAP2 FUSION-RELATED; 1.
DR PANTHER; PTHR10498; PARALEMMIN-RELATED; 1.
DR Pfam; PF15304; AKAP2_C; 1.
DR Pfam; PF03285; Paralemmin; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 1172..1315
FT /note="A-kinase anchor protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF15304"
FT REGION 285..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..41
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 77..114
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 145243 MW; 91C1A636F835E453 CRC64;
MSQSASRMAE AELHKERLQA IAEKRKRQTE IEGKRQELDE QILLLQHSKS KVLREKWLLQ
GVPAGTAEEE EARRRQSEED ELRVKQLEGN IQRLEQEIQA LESEESQISA KEQIILEKLK
ETEKSFKDFQ KSFSSTDGDA VNYISSQLPD LPILCSRTAQ PSPGQDGTSR AAAVYAMEIN
VEKDKQTGET KILSTSTIGP EGVHQRGVKV FDDGTKVVYE VHSGGTIVEN GVHKLSSKDV
EELIQKAGQS SLRGGYVSER TVVADGSLSH PKEHMLCKEA KLEMVHKSRK DHTSGNPGQQ
APAPSTEGPE ANLDQPVTMI FMGYQNIEDE EETKKVLGYD ETIKAELVLI DEDDEKSLRE
KTVTDVSTID GNAAELVSGR PVSDTTEPSS PEGKEESLAT EPAPGVGWES VLLTGDELTS
KATDTSSADM TVQKAPELSE DDIRLKNEKD NCSGNPLEPA TSPLPPDHKN MEIEVSVAEC
KSVPGITSTP HSMDHPSPFY SPPHNGLLAD HHESLDNDVA REIRYLDEVL EASCCDSAVD
GTYNGTSSPE PGAAILVGSP SPPAHTAVQP EPTERVAGRQ APPPLELHQS TSDTMAEGER
ANGRPPDQPR DLLGNSLQVP VSPSSSTSSR CSSRDGEFTL TTLKKEAKFE LRAFHEDKKP
SKLFEDDESE KEQYCVRKVR PSEEMLELEK ERRELIRSQA VKKNPGIAAK WWNPPQEKTI
EEQLNEEHLE SHKKYKERKE RRAQQEQLLI RRQPAAPQLG AAPASSRERS SVTDSAKEDI
VTEQIDFSAA RKQFQLMENS RQTVAKGQST PRLFSIKPFY RPLGPVNSDK TLTISRPASV
GGPPEDSSAA KGQKAHCALE SQSSGGGGQG STAPQGKEGP YSEPSKRGPL SKLWAEDGEF
TSARAVLTVV KDDEPGILDQ FSRSVNVSLT PEELDSGLDE LSVRSQDTTV LETLSNDFSM
DNISDSGASN ETTNALQENL LADFSLPQTP QTDNPSEGRG EGVSKSFSDH GFYSPSSTLG
DSPSVDDPLE YQAGLLVQNA IQQAIAEQVD RAVSETNKGG AEQQGPQASL EEAETGASSS
EKPQSMFEPP QVSSPVQEKR DVLPKILPTE DRALRERGPS QPLPAVQTSG PINMEETRLE
GSYFSKYSEA AELRSTASLL ATQESDVMVG PFKLRSRKQR TLSMIEEEIR AAQEREEELK
RQRQVLQSTQ SPKAKNAPSL PSRTSCYKTA PGKIEKVQPP PSPTPEGPSL QPDLAPEEAA
GSQRPKNLMQ TLMEDYETHK SKRRERMDDS SVLEATRVNR RKSALALRWE AGIYANQEEE
DNE
//
