ID A0A3Q1GJP3_9TELE Unreviewed; 882 AA.
AC A0A3Q1GJP3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000030881.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000030881.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR038141}.
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DR AlphaFoldDB; A0A3Q1GJP3; -.
DR Ensembl; ENSAPOT00000032947.1; ENSAPOP00000030881.1; ENSAPOG00000017659.1.
DR GeneTree; ENSGT00940000156120; -.
DR Proteomes; UP000257200; Unplaced.
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 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:SF32; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 2.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
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:UP000257200}.
FT REPEAT 85..117
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 118..150
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 210..242
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 243..275
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 782..882
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 787..869
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97197 MW; 2191BD14AA87A2F0 CRC64;
MAATDHSRSE AAKQRRQDQL QRWLGSETDQ TGSEARETSS GSGTRRAKVR FAQGAVFMAA
CSAGDREEVS ALLRQGADIN HANIDGLTAL HQACIDENAE MVQFLVESGS DVNRGDNEGW
TPLHAAASCG FIQIAKYLIE HGAQVGAVNS EGELPLDVAT EDAMERLLKG EIKKQGIDVD
KARKEEERIM LQDATAVLAG GGTLTPHPNT KATALHVAAA KGYIEVLKVL LQCRVDVDGR
DIDGWTPLHA AAHWGQEEVC TLLADNMCDM GAVNNVGQTP LDVADENLVD ALEELQKKQN
ALRSEKEKQT PVIETSPPIS MVPLRTRRTS ISRMSSKEKI CLHEREKHPP PALQSSPAED
EEEEGQTGQS QTQSQTKASS SSSSEEESES ESDAESEKAK NREIINNLNN KRNASLLPTS
MSSSTTASQV KKQEPSKPPA TEAPGSWRTS LRKAGSSVTL GSAGLSDTSQ DTSRPAESAL
GMTRSASSPR LSSEADTKEP RLARVPPIPT RRLYSIPDSR PDNSNSSSYG KRLDDPSVTS
ASTGTSSTGF SRLNSVLAQR IPQEQTEKKD QSAITTSNSQ STTGEPETKQ RRKSYLTPVR
DEEAEAQRKA RSRHARQSRR STQGVTLTDL QEAEKTMKTM KTDNKGREKK EEEEKEKEAK
QKKGEEGEVS WRSRIASLQK SDLLGLTQPA GTPRPQTSDR RDVEASTGES ETERWARERR
ERRQARARRK AQRTGESDDN DPSGEEEFSG SGLDPQTGQQ LSSRLNVSCN DRTLGGGSET
KDFKKLFEEV SRENSQLQSQ LQDTQRIISQ TRLDLEKATQ RQERFSDCSA LLELERKDRR
MLERRMAELE EELKVLVDLR ADNQRLKDEN GALIRVISKL SK
//
