ID A0A6I8TMW8_AEDAE Unreviewed; 1588 AA.
AC A0A6I8TMW8;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=cGMP-dependent protein kinase interacting domain-containing protein {ECO:0000259|Pfam:PF15898};
GN Name=5576767 {ECO:0000313|EnsemblMetazoa:AAEL012751-PL};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL012751-PL, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL012751-PL, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL012751-PL,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL012751-PL}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL012751-PL};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the NRARP family.
CC {ECO:0000256|ARBA:ARBA00038386}.
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DR EnsemblMetazoa; AAEL012751-RL; AAEL012751-PL; AAEL012751.
DR OrthoDB; 19014at2759; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:TreeGrafter.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:TreeGrafter.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR CDD; cd21930; IPD_PPP1R12; 1.
DR FunFam; 1.25.40.20:FF:000198; Myosin binding subunit, isoform P; 1.
DR FunFam; 1.25.40.20:FF:000007; Phosphatase 1 regulatory subunit 12A; 1.
DR Gene3D; 6.10.140.390; -; 1.
DR Gene3D; 6.10.250.1820; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR051226; PP1_Regulatory_Subunit.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179:SF21; MYOSIN BINDING SUBUNIT, ISOFORM O; 1.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF15898; PRKG1_interact; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820}.
FT DOMAIN 1481..1577
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 330..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1479..1572
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 341..372
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..675
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..733
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..783
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..851
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1009
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1029
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1235
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1308
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1401
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1419
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 171347 MW; 9E39344B4AB4EFBB CRC64;
MSMDNRSTSA LFKRAEQLKR WEESEANKHS GIPKSPSMRR IKFSSGCIFL AACMAGDKDE
VSRLLETGAD IDTANVDGLT ALHQACIDDN LDMVEFLVQN GADVNRKDNE GWTPLHATSS
CGFLSIARYL IENGADLAAI NSDGELALDL ACSDAMEDLI QRHIDEQGID CEDARQAEEK
IMLSDAKRWL RTDSTDCDKP HPKTGATALH VAAAKGYTKV LGLLLDGRGD FDKQDVDGWT
ALHAAAYWGQ KEAVQMLLSA NVDIDIQNYS GQYAIDIAQK DIVPLLDEAR KNFKRPKRRP
ASQIRITDTI ENSIETPTKV IRVEVKPIDS KEQEEVVSGS DAEEVEEEEF QEVEQEEEEE
EEEENGIEDE GSGSDREGSI EPEESAEEEM EEAEESEEDA EKQESDEEPT VEPEEEEEQA
SDAESSPYSS SSESSSSNES SMTEESEAAK LPKPVPIISR PSPVPVAEQI IVPKPRIEGV
HRELPAAPPL PPPPAVSQQM APPPVPWRRA RATPTPVPTD EHAHQQQQSL QKFQNGHTTV
NRLSPYRNLP EKENQPTEPD VILRRTQSFE SDEKFYQKYV ELRARIQANS CPILPNTNPT
TNAKPATANN TSTNNSYLVQ RSASLKDHRT LRKASSNLVL GSTGSTTGTA TTNVQTATTS
PPTSPTGTPV TTPSTGQIRS ITPANNKNSH TTSNSPSIPP VEVTAAATTT TNNNNNINNN
SNNNNKNDTS SNAVNKNHSL FELNRKYIEQ AQKTKINNER NKFLSSLNEK RLQQQQQQQE
AQQPETKGPS QSPSAKSGAA AEKEPSQPAE APATVKSVAP LYASSASNNN YALNNHAASN
FNNNNSISTP SQQPPPTVVT STNKLSPGNI FKNFFKSFVP PTRDEESETQ RKAHAKRVRE
TRRSTQGVTL DEIKSAEQLV KKKNSTNSSD SDPSSTTATA STPSTTSTSS SSTLVNDRVP
SVDASASEVS SQVPSSSSST STSAEQQQVS ASFTISAPPS SSLSTSASIK SHRGDVGGGG
GGGGGGGGDT ASAPDEDSSS KISVSYTITT PRLSSSITSS SSSDSATIAK DSKSKEASVP
SVTATFSVPS ATPITSSSTT NNNTSNSSNN NLYKKTDSDD STKTTTTTTA TTKSTITPAG
DSASIGTPAS STSVTATVRT PGPYSTSKRS LFDIDNANSL TLAEKLRQEA NKYAESDKEN
FVSSKGPTST ATSASATTTT KSSESTSSNT TPAAAVEGTV LLRKDTSAPS SPLHHHHQQQ
PSTLAERRPS WRLKVDGGSK FKLEDASVPP TSAATTTSSS TVTALDSSAH SRPHSQNELN
SISMSSLAQR RQNGDSSSFN TSRPTSAPEL GLSAVASSQN DASLHLRVRP LKASEENKEN
DKENENRTGG SSSGTTTTNS SAQATQAVIQ RRRRQKRRST GLVHVDMEDI DPERQDSPVD
GEEKESGTER GRSRVGSTAS ELADQQKDGS ESKENGGDYI DYKALYEQAK ADNNKLKSDL
RKRDEEVASL QAALERFTVA TTKNNSLSEL EKREKRAMER KMSEMEEELK LLQKYKTENE
RLRAENRALT RVVSKLTTSA QNQLHNKQ
//
