ID A0A2Y9JTW8_ENHLU Unreviewed; 981 AA.
AC A0A2Y9JTW8;
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=LOC111151011 {ECO:0000313|RefSeq:XP_022364418.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022364418.1};
RN [1] {ECO:0000313|RefSeq:XP_022364418.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022364418.1};
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_022364418.1; XM_022508710.1.
DR AlphaFoldDB; A0A2Y9JTW8; -.
DR Proteomes; UP000248482; 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 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:UP000248482}.
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 881..981
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 342..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 109810 MW; B7ADAC765789C16D CRC64;
MAELEHLGGK RAESARMRRA EQLRRWRGSL TEQEPAERRG AGRQPQTRRG SPRVRFEDGA
VFLAACSSGD TDEVKKLLAR GADINTVNVD GLTALHQACI DENLDMVKFL VENRANVNQQ
DNEGWTPLHA AASCGYLNIA EYFINHGASV GIVNSEGEVP SDLAEEPAMK DLLLEQVKKQ
GVDLEQSRKE EEQQMLQDAR QWLNSGKIED VRQPRSGATA LHVAAAKGYS EVLRLLIQAG
YELNVQDYDG WTPLHAAAHW GVKEACSILA EALCDMDIRN KLGQTPFDVA DEGVVEHLEM
LQKKQNMLRS EKETRNKLIE SDLNSKLQSG LFKNKEKMLY EEEVPKSQEM EEESKESSSS
SSEEEEGEDE ASESETEKEA DKKPEAIVNH SNSESKSIIT EQIPPPAQNT FSASSARRFS
SSLFNKPEEP RDESPSSWRL GLRKTGSHNM LSEVANSREA LRDRGSSIYR SSSSPRISAL
LDSKDKEREN KSYFSSLAPR RLSSTSDIEE KENRESAVNL VRSGSYTRQL WRDEAKGSET
PQTVAPSTYV STYLKRTPYK SQADSTTEKT VDNVSSSTPL CVITNRPPPS TANGVTTATQ
LSAPGTDSSV EARDRRRSYL TPVRDEEAES LRKARSRQAR QTRRSTQGVT LTDLQEAERT
FSRSRAERQA QEQPSQKPAG TEGLEGSSEK REPSAAPAKE AGEGRQPWGG SLDGEPVYRR
LRYPTQPDKP TTPVSPSASR PSLYTSSHLL QTSRSSVPDS ESSETTTNTA VAKEMDKNES
EEADVDDQTS NRLSIRERRR AKERRRGTGI NFWTKDEDEA DVSEEVKAAL HERLSRLESG
GSNPTSSDSY GDRASARARR EAREARLASL TSRVEEDSNR DYKKLYESAL TENQKLKTKL
QEAQLELADI KSKLEKMAQK QEKTSDRSSM LEMEKRERRA LERKMSEMEE EMKVLTELKS
DNQRLKDENG ALIRVISKLS K
//
