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Database: UniProt
Entry: A0A3Q3L366_9TELE
LinkDB: A0A3Q3L366_9TELE
Original site: A0A3Q3L366_9TELE 
ID   A0A3Q3L366_9TELE        Unreviewed;       701 AA.
AC   A0A3Q3L366;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000007937.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000007937.1}
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; A0A3Q3L366; -.
DR   STRING; 205130.ENSMAMP00000007937; -.
DR   Ensembl; ENSMAMT00000008153.2; ENSMAMP00000007937.1; ENSMAMG00000005377.2.
DR   GeneTree; ENSGT00940000161425; -.
DR   InParanoid; A0A3Q3L366; -.
DR   Proteomes; UP000261640; 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; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR   PANTHER; PTHR24179:SF27; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12C; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF15898; PRKG1_interact; 1.
DR   PIRSF; PIRSF038141; PP1_12ABC_vert; 4.
DR   SMART; SM00248; ANK; 4.
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:UP000261640}.
FT   REPEAT          118..150
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          151..183
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          244..276
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          277..309
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          601..701
FT                   /note="cGMP-dependent protein kinase interacting"
FT                   /evidence="ECO:0000259|Pfam:PF15898"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          668..695
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   701 AA;  78234 MW;  B804E3E228429C74 CRC64;
     MGDSARTKRR EQLKRWAGSC TDKASAVPRR RWRGDAEDTT GEPEAELSDR PRDELVRDEI
     SPLLKRRKRV RFDKAAEFLA ACASGDTEEA KAMLKEAKDA KSRNGEDVEE IINCSNADGI
     TALHQACIDG SMEMVTFLLK HGAKVNKVDS EGWTPLHVAA SCGHPEIADF LLQQGASLSA
     VNCDGDVPLD IASDETTESL IQDYTMRQGV DVEAAKRLEE EQIMMDARAW LTEGVPASVH
     HPRTGATPLH VAAAKGYLEA LKILCQCGLD VSAMDFDGWT PLHAAAHWGQ GEACRILAEQ
     LCNMEVRSNA GQTPFDVADE SVEELLEELS KKQANWRNER SILDKQNQQG STAANAQNKR
     RRSSVCRMSS KDKMNVQDQS KERGVTGELE LSEEKDSSPE SSIVSSPDTE SVTTSIASPA
     DKTPEEKEME EKEQDKANRT ARVQPTPQTR DATAESPNNL NSDKRKFQAP VRDEESESQR
     KARSRRLRQS RRSTQGVTLT DLKEAEKTVT QAAEPLSSNI QHVSPIVTVT PAERDTDPVK
     QMEPEAEKRL GVKDRRRGRR ERRSTGIVHL GGENEEEDGN LDDTNGNSYS IVSQLGDLSA
     DYRTLYFRVL QENLSLKDKL QEMELLLSQN KVELERLRQS QESSTDRPAL LELERFEKLA
     LQRKAIELED ELKVLGDLRA DNQRLKDENA ALIRVISKLS R
//
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