ID S4RZ36_PETMA Unreviewed; 989 AA.
AC S4RZ36;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000010477.1};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000010477.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; S4RZ36; -.
DR STRING; 7757.ENSPMAP00000010477; -.
DR Ensembl; ENSPMAT00000010523.1; ENSPMAP00000010477.1; ENSPMAG00000009524.1.
DR GeneTree; ENSGT00940000156120; -.
DR HOGENOM; CLU_000134_54_0_1; -.
DR OMA; TIFDNRE; -.
DR Proteomes; UP000245300; 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:SF18; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12B; 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; 3.
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}.
FT REPEAT 1..25
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 26..58
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 119..151
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 152..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 887..989
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 252..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 885..983
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..834
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 107793 MW; 1A48587A2E44FE3D CRC64;
ACIDENFDMV KFLVERDANI NQADNEGWTP LHAAASCGYI DIAKYLIAHG ANVAAVNSES
ELPLDITEDE ALEDMLQEEL SKHGVDQDAA RKEEEQVMMR DARQWLNSGR IDEVRHPKSG
GTALHVAAAK GYIDVIKLLL QAGFDVNVRD NDGWTPLHAA AHWGKDEACR VLVENFCNME
ALNKVGQTAF DVSDEDVLSY LEELQTKQKT MKIEKEKQPI NSEIIESNDT NSIKSRGKTN
IEWQESVLGI ETEEMKEGDG ESKHDETSSS SSEEEDDEDE EEDQTRKNRP SVKENNNNNN
KTTPSPAPLT VTNTQPPAAA TTTTTPTSPS RKFPSSFPRA GAGGIAAGAA APKEEEKKTV
DVAPPASAPA SWRSGLRKTG SYGALPEAAA AAAAAGAAGA GEPPRDALRE RGDVTQAGSG
IARSASSPRL TTTETRERER DSLGTKLARV PPTISDNKFA FPRKLGTAAL EEKENSRDTV
GMLLARSSSY TRRRFDDSSE NTAPAYQRRQ VCIFGKDSSS GLSPSSPPPV LPTSTSTTPV
PTVRVSDDVT NVTSTAPVSA VAPSVGRVEE APERGSREGI GGGSGGTVPA VTVTVPPTVS
GGSAPSLESG AALSGENRER RRSYLTPVRD EESESQRKAR SRQARQTRRS TQGVTLTDLH
EAEKIRRYGS DKRGGREQPE EKESAERLDD KKDTESREAS DARGRPSRTY GSDTQDGAYQ
RLRPSASLAP ASSGINKGGS LLMQSRFLSA KGSLLGVSSR LLRVTAPIAS PSDSGEEDSQ
TEGDKGKNKL SVVRDRRRPR EKRRSTGVSF MSPDSQSDEN DHDLSDEEEE SEEVEKFNTV
ATSTSLSENY SERYADRMRS VAAGRPGRPV PSLAPAPQPT ELPDTKDYRK LYEQMRKENE
EMRKKLRDAQ LQLAETKVQL ERVTQDAVFV ERPPRIDVLC SLNQEKRALE RKVSEMEEEM
KGLGDLRADN QRLKDENAAL IRVISKLSK
//