ID A0A3L8ST00_CHLGU Unreviewed; 1083 AA.
AC A0A3L8ST00;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN ORFNames=DV515_00004539 {ECO:0000313|EMBL:RLW06445.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW06445.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW06445.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW06445.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW06445.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, and one or several
CC targeting or regulatory subunits. {ECO:0000256|PIRNR:PIRNR038141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR038141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW06445.1}.
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DR EMBL; QUSF01000009; RLW06445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8ST00; -.
DR STRING; 44316.ENSEGOP00005017030; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:UniProtKB-UniRule.
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; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038141};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT REPEAT 129..153
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 154..186
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 247..279
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 280..312
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 984..1083
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 339..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 989..1070
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 352..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120508 MW; BB17AB8842505A98 CRC64;
MHGKLAVKFP QNGCFVHVEL HSSLIGISKR VFATVYVEGS VRASGGIFLV PDMFEQGVSL
QSKCKHTGFS LLITDVFAQS IPGSQSLLFL AGRDIEWLPT KTLQTFPMLR RCKIIYGIDQ
STNLISERAC IDDNVDMVKF LVENGANINQ PDNEGWIPLH AAASCGYLDI AEYLISQGAH
VGAVNSEGDT PLDIAEEEAM EELLQNEVNR QGVDIESARK EEERIMLRDA RQWLNSGHIN
DVRHAKSGGT ALHVAAAKGY TEVLKLLIQA HYDVNIKDYD GWTPLHAAAH WGKEEACRIL
VENLCDMEAV NKVGQTAFDV ADEDILGYLE ELQKKQNLLH SEKREKKSPL IESTANMDNN
QTQKTFKNKE TLIMEQEKNA SSIESLEQEK ADEEEEGKKD ESSCSSEEEE DDDSESEAET
DKTKTLAANN ANTTSTQSAS GAVMAPSVAG GQGAPTSPVK KFPTSTTKVS PKDEERKDES
PASWRLGLRK TGSYGALAEI TASKEAQKEK DSAGVMRSAS SPRLSSSLDN KEKEKDGKGT
RLAYVAPTIP RRLASTSDID EKENRDSSAS SIRGGSSYTR RKWEEDVKKN SLNEGPTSLN
TSYQRSGSFG RRQDDLISSN VPSTASTVTS SAGPQKTLPA STNTTTTKST TGSTSAGVQS
STSNRLWAED STEKEKDSVP TAVTVPVAPS VVNAAATTTA MTTATSGTVS STSEVRERRR
SYLTPVRDEE SESQRKARSR QARQSRRSTQ GVTLTDLQEA EKTIGRSRPT RTREQENEEK
EKEEKEKQDK EKQEEKKESE TKDDDYRQRY SRTVEEPYHR YRPSSTSTSS SSTSSLSTST
SSLSSSSQLN RPNSLIGITS AYSRSGTKES EREGGKKEEE KEEDKSQPKS IRERRRPREK
RRSTGVSFWT QDSDENEQDH QSDSEEGTNK KETQSESLSR YDTGSLSMSA GDRYDSAQGR
SGSQSYLEDR KPYCSRLEKD DSPDFKKLYE QILAENEKLK AQLHDTNMEL TDLKLQLEKT
TQRQERFADR SLLEMEKRER RALERRISEM EEELKMLPDL KADNQRLKDE NGALIRVISK
LSK
//
