ID A0A2Y9MF37_DELLE Unreviewed; 968 AA.
AC A0A2Y9MF37;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN Name=PPP1R12B {ECO:0000313|RefSeq:XP_022417652.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022417652.1};
RN [1] {ECO:0000313|RefSeq:XP_022417652.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022417652.1};
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, cytoskeleton, stress fiber
CC {ECO:0000256|ARBA:ARBA00004529}.
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DR RefSeq; XP_022417652.1; XM_022561944.2.
DR AlphaFoldDB; A0A2Y9MF37; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0001725; C:stress fiber; 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: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 SMART; SM00248; ANK; 5.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR038141};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT REPEAT 90..122
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 123..155
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 216..248
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 249..281
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 867..968
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 107165 MW; 1FEB07D34F1B61F0 CRC64;
MAEMERLGGK RAESARARRA EQLRRWRGSL TEQEPADRPG AELPPQAQRG GPRVRFEDGA
VFLAACSSGD TDEVRRLLAR GADVDTANVD GLTALHQACI DENVDMVKFL VENGASVNQQ
DSEGWTPLHA AASCGHLNIA EYFISHGASV GVVNSEGEAP SDLAEEPAVK DLLLQQVKKQ
GVDLEQSRKA EEQQMLQDAR QWLNSGKIQD VRQARSGATA LHVAAAKGYS EVLRLLTQAG
YELNVQDRDG WTPLHAAAHW GVKEACSILA EALCDMDVRS KLGQTPFDVA DEGLVEHLEM
LQKKQSVLRS EKETRNKLIE SDLNSKLHGR LFKNKEKMLY EEEAPKPQEM EDENKESSSS
SSDEDEGEDE ASESETEKEA GDAETLCLQS TGGHCLSQDK KPGAIVNRSN SESKSSAAEQ
TPAPAQIISS TSSARRFSGL FNKPEEPRDE SPSSWRLGLR KTGSQNVLGE AARSREALRD
RGASIHRSAS SPRISTVLDT REKERESRSS FSALGPRRLS AASDLEEKEN RESAAHLVRS
GPPARQLRRD GAEGSESLQM AAPSTYVTTY LKRPPYKSQA DSAAERTVDG VSCGTPLCVI
TNRPPPSTAN GVTAAALLSI PGTDSSVEAR ERRRSYLTPV RDEEAESLRK ARSRQARQTR
RSTQGVTLTD LQEAERTFSR SRAERQAQEQ PSPKPVGPRG LDGSAQKHEP LAAPAEEAGE
SRQPWDRSLE DQPVYRRLRI PAQPDKPMTP VSPPAPRPSL YTSSYLLRTE GEEADLGDQS
SNRLSIRERR RPKERRRGTG ISFWTKDEDE TDVSEEVKAA WHERLSRLEL GGSDASSERA
SARARREARE ARLATLSSRA GEDSSRDYRK LYESALTENQ KLKTKLQEAQ LELADVKSKL
EKMAQQKQDK TADRSSVLEM EKRERRALER KMSEMEEEMK VLTELKSDNQ RLKDENGALI
RVISKLSK
//
