ID A0A401T436_CHIPU Unreviewed; 1043 AA.
AC A0A401T436;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN ORFNames=chiPu_0015937 {ECO:0000313|EMBL:GCC37433.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC37433.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC37433.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(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:GCC37433.1}.
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DR EMBL; BEZZ01001000; GCC37433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401T436; -.
DR STRING; 137246.A0A401T436; -.
DR OMA; RKYETNA; -.
DR Proteomes; UP000287033; 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; 6.10.250.1820; -; 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; 3.
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:UP000287033}.
FT REPEAT 142..174
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 175..207
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 268..300
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 301..333
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 944..1043
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 949..1030
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 116497 MW; 5E69EA5D80991149 CRC64;
MWRGRGPKSR GRGPDQTAFK KQKEREPQWS GRGHAYDGRV WARVGDEQRH GSQGDGIASG
RRRRPRPSDR QKMADAKQKR NEQLKRWLGS ETELEPPVLK KKKTKVKFDD GAVFLAACSS
GDTDEVKKLL DRGSDINYAN VDGLTALHQA CIDDNLDMVK FLVEHSANIN QPDNEGWIPL
HAAASCGYAD IAEYLISHGA NVAAVNSEGE TPLDIAEEEA MEELLQEEIS RQGVDIEAAR
KEEERIMLRD ARQWLNSGQI NDNRHPKSGG TALHVAAAKG YSEVLKLLIQ AGYDVNIKDY
DGWTPLHAAA HWGKEETCRI LVESFCDMEM INKVGQTAFD VADEDILGYL EELQKRQNML
FREKQANKSP LIESTATMEN NQELKPIKSK ETLLNEQKVP VHIESLEQEK VDDEEEGKKD
DSSCSSEEEE EEDSESEAET EKNKPIVHVN NVNRINSGGI QSAAVAPTSV PTNQVAPASP
VKKLATPFIK SSKEEEKKRK DEEEKKDASP ASWRSGLRKT GSYGALAEIS TSKEAQKERD
VTGVMRSASS PRLSSTLDNK EKDKDQKGAK LAYVVPTIPS RRLASTSDID EREIRDSAST
LVRSGSYTRR RWEEDLKRKE INHASTSEGS ASQNAAVTSV VPGYQRSNSY LLAIGRSNSA
RDLPTSSSSA ISLDPTNTKP RPPSSTQYSS YSIYKSSSFG RRKEDLISPI QSAISTNTIA
TITSSSSLQP VPRSTASTPS GSTSNRFSTG DNAERDKENV PSTVATTGTV SSTTEVRERR
RSSTTTTSTA TVSAFNSSHV ASQLNRPNSL IGITSAYSAY NRSSGEVEKE MDKRDDERDG
EEKLDDKSQN KPSIRERRRP REKRRSTGVS YWTQDSDENE QEQQSDAEDG TNKKYQNDRL
SRFDTGLSTT HNEGPEQLAN RTGFSTYKGS KQASLRTEKE DTLDYKKLYE QFLAENEKLK
ASLHDTNLEL NELKVQLEKT TQRQERIADR SLLEMEKRER RALERKIAEM EEELKMLPDL
KADNQRLKDE NGALIRVISK LSK
//
