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Database: UniProt
Entry: H3D536_TETNG
LinkDB: H3D536_TETNG
Original site: H3D536_TETNG 
ID   H3D536_TETNG            Unreviewed;      1025 AA.
AC   H3D536;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000015625.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000015625.1}
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|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR038141}.
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DR   AlphaFoldDB; H3D536; -.
DR   STRING; 99883.ENSTNIP00000015625; -.
DR   Ensembl; ENSTNIT00000015832.1; ENSTNIP00000015625.1; ENSTNIG00000012652.1.
DR   GeneTree; ENSGT00940000156120; -.
DR   HOGENOM; CLU_000134_54_0_1; -.
DR   InParanoid; H3D536; -.
DR   OMA; RKYETNA; -.
DR   TreeFam; TF105543; -.
DR   Proteomes; UP000007303; 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   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   PRINTS; PR01415; ANKYRIN.
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   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:UP000007303}.
FT   REPEAT          72..104
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          105..137
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          198..233
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          234..266
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          926..1025
FT                   /note="cGMP-dependent protein kinase interacting"
FT                   /evidence="ECO:0000259|Pfam:PF15898"
FT   REGION          298..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          924..1012
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        305..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..845
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..896
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  114488 MW;  195A12EAE9B8BE31 CRC64;
     MKMADAKQKR NEQLKRWIGS ETDLEPPVLK KKKTKVKFDD GAVFLAACSS GDTEEVLRML
     DHGADINYAN VDGLTALHQA CIDDNVDMVT FLVEHGASID QPDNEGWLPL HAASSCGYLD
     IAAYLISQGA NVGGVNSEGE TPLDIAEEEA MEELLQNEIN RQGVDIEAAR KEEERVMLRD
     ARQWLNSGQI QDVRHAKSGG TSLHVAAAKG YVEVLKTRRL LIQAGYDVNI KDYDGWTPLH
     AAAHWGKEEA CRILVENLCD MDLINKMGQT AFDVADEDVL GYLEELQKKQ NLLMSSKKDV
     KKSPLIETTT TGDNNQSLKP LKSKETLLLE PEKSTPRIET LEPEKVDEEE EGKKDESSCS
     SEEEEDEDSE SETEAEKTKP SSASVSNSTT TTSTSTVSPP TSPTNQVTSP TSPIKKATQP
     AGKATAKVDE ERKDESPASW RLGLRKTGSY GALAEITATK EAQREKDTSG VMRSASSPRL
     SSSLDNKDKE KEKDKGTRLA YVAPTIPRRL ASASDIDEKE NRDSPALIRS GSYTRRRWDD
     DLKNSEGSNR TSSYQRSGSF GRRHEDLSST TSSPSSSTTT TTSSSVTSTA GLRGLGSSAR
     TGSTSLTSRY WSEESAPTNP DTFPVWEQGV CVCVRVQAVH TRSLCRVSPP ACVFKWVECV
     FVCVRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT DLQEAEKTIG RSRPIKTHTE
     IKEEDYRSKY RSYEEVRPGL GCFLHLDRLK LSSRLISFLF SRLPQRYRPL SSSSSSTSAI
     STASTASTPS YSSTTLSSSS LNRPNSLTGI TSSYSRSSRD TEKETDRKEE EKEGEDKSQP
     RSIRDRRRPR EKRRSTGVSF WTQDGEENDP EQQSDSEEGG NKGEPQSDRL SRNELTSDRN
     DSLSSRGYGE SRRIYSSRLD RDDATDYKKL YEQILAENEK LKAQLRDTDL ELADLKLQLE
     KATQRQERYA DRSQLEMEKR ERRALERKIS EMEEELKTLP DLKADNQRLK DENGALIRVI
     SKLSK
//
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