ID A0A093FYF4_DRYPU Unreviewed; 943 AA.
AC A0A093FYF4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12A {ECO:0000256|ARBA:ARBA00044128};
DE AltName: Full=Myosin phosphatase-targeting subunit 1 {ECO:0000256|ARBA:ARBA00044333};
DE Flags: Fragment;
GN ORFNames=N307_00093 {ECO:0000313|EMBL:KFV62940.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV62940.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV62940.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV62940.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KL215025; KFV62940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FYF4; -.
DR STRING; 118200.A0A093FYF4; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21944; IPD_MYPT1; 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; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR PANTHER; PTHR24179:SF20; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12A; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT REPEAT 1..25
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 26..58
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 59..92
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 119..151
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 152..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 844..943
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 211..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 849..930
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 224..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV62940.1"
FT NON_TER 943
FT /evidence="ECO:0000313|EMBL:KFV62940.1"
SQ SEQUENCE 943 AA; 104967 MW; D465A16E9CEE3059 CRC64;
ACIDDNVDMV KFLVENGANI NQPDNEGWIP LHAAASCGYL DIAEYLISQG AHVGAVNSEG
DTPLHIAEEE AMEELLQNEV NRQGVDIEAA RKEEERIMLR DARQWLNSGH INDVRHAKSG
GTALHVAAAK GYTEVLKLLI QARYDVNIKD YDGWTPLHAA AHWGKEEACR ILVENLCDME
AVNKVGQTAF DVADEDILGY LEELQKKQNL LHSEKREKKS PLIESTANMD NNQTQKTFKN
KETLIMEQEK ITSSTESLEQ EKADEEEEGK KDESSCSSEE EEDDDSESEA ETDKTKSLAA
VTNNSNTTST QSASVAVTAP SVAVGQGAPS SPVKKFPTST TKVSPKEEER KDESPATWRS
GLRKTGSYGA LAEITASKEA QKEKDSAGVI RSASSPRLSS SLDNKEKEKD GKGTRLAYVA
PTIPRRLAST SDIDEKENRD LSASSIRSGS SYTRRKWEDD AKKNSLNEGP ASLNTSYQRS
GSFGRRQDDL ISSNVPSTAS TVTSSAGLQK TLPASTNTTT KSTTGSTSAG VPSSTSNRLW
AEDSSEKDKD SGSTAVTVPV APSVVNAAAT TTAMTTATSG TVSSTSEVRE RRRSYLTPVR
DEESESQRKA RSRQARQSRR STQGVTLTDL QEAEKTMGRS RPTRTREQEN EEKEKEEKEK
QDKEKQEEKK ESETKDDDYR QRYSRTVEEP YHRYRPASTS SSSTSSLSTT TSSLSTSSQL
NRPNSLIGIT SAYSRSGTKE SEREGGKREE EKEEDKSQPK SIRERRRPRE KRRSTGVSFW
TQDSDENEQE HQSDSEEGTN KKETQSESLS RYDTGSLSMS SGERFDSAQG QSHCSRLEKE
DSTDFKKLYE QILAENEKLK AQLHDTNMEL TDLKLQLEKT TQRQERFADR SLLEMEKREK
RALERRISEM EEELKMLPDL KADNQRLKDE NGALIRVISK LSK
//
