ID A0A2D0T348_ICTPU Unreviewed; 1029 AA.
AC A0A2D0T348;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN Name=ppp1r12a {ECO:0000313|RefSeq:XP_017349236.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017349236.1};
RN [1] {ECO:0000313|RefSeq:XP_017349236.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017349236.1};
RG RefSeq;
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 RefSeq; XP_017349236.1; XM_017493747.3.
DR AlphaFoldDB; A0A2D0T348; -.
DR GeneID; 108279475; -.
DR KEGG; ipu:108279475; -.
DR CTD; 4659; -.
DR OrthoDB; 5482573at2759; -.
DR Proteomes; UP000221080; Chromosome 19.
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; 2.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR038141}.
FT REPEAT 70..102
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 103..135
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 196..228
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 229..261
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 925..1029
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 293..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 115417 MW; EB2DE226DF033F45 CRC64;
MADAKQKRNE QLKRWLGSET DLEPPVLKKK KTKVKFDEGA VFLAACSSGD TEEVLRLLER
GADINYANVD GLTALHQACI DDNVDMVTFL VEHGACINQP DNEGWIPLHA AASCGYMDIA
EYLINQGANV GVVNSEGETP LDIAEEEPME ELLKNEINRQ GVDIEAARKE EERIMLRDAR
QWLNSGQIND VRHAKSGGTA LHVAAAKGYT EVLKLLIQAG YDVNIKDYDG WTPLHAAAHW
GKDEACRILV ENLCDMDVVN KVGQTAFDVS DEDVLGYLEE LQKKQNLLMS EKKDAKKSPL
IETTTTADNN QSTKPAVKSK ETLLLEVEKN TPRIENLESE KADDVEEVKK DESSCSSEDE
DEDDSESENE ADKTKSAVPV SNSTSSVPAP TTIPVSASSN TPVTPTSPVK KVSVPAGKVS
PKEEERKDES PASWRLGLRK TGSYGALAEI SATKEAQKEK DPSGVMRSAS SPRLTSSLDN
KDKEKEKEKS LVYVAPTFPR RHLSVSDMDE KENRDSAATL VRSGSYTRRR WDEDLKNNDT
TSLNRMSSYQ RSTSHTLTLG RSSSSRDLPA KSSSASSLDP TSTKASSSYY QSYSIHRSGS
FGRRQDDAVS STSSTVSTTT SSTSTTTITS PTGHRSVSRY WSEDGAEKEK ESATVIPTIN
TAATTTTTTT HTTAGDGRER RRSYLTPVRD EESESQRKAR SRQARQSRRS TQGVTLTDLQ
EAEKTIGRNR PIRSREEEKE KEEKEKQDKE KKEAETKEDD YRSRYRFEER FRTPSFSSST
STTVPTSSVT SSSLYTSSSS SSLNRPDSLS GITPSYRSSA RDTEKDKKEE EKEGEDKTQP
RSIRDRRRPR EKRRSTGVPF WTQDSDENDP EQHSDSEEGS TKAEPQSERL LRNDGVSSGS
SLTDRYDHRE SRRSYSRLDR EDNTDYKKLY EQIQAENEKL KSQLRDTHLE LDDLKRQLEK
ATQVRGLQRQ ERFADRSQLE MEKRERRALE RKISEMEEEL KTLPDLKADN QRLKDENGAL
IRVISKLSK
//
