ID A0A1U7Q8W0_MESAU Unreviewed; 1031 AA.
AC A0A1U7Q8W0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 18-JUN-2025, entry version 36.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN Name=Ppp1r12a {ECO:0000313|RefSeq:XP_005068108.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005068108.1};
RN [1] {ECO:0000313|RefSeq:XP_005068108.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_005068108.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates
CC binding to myosin. As part of the PPP1C complex, involved in
CC dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent
CC suppression of HIF1A activity. {ECO:0000256|ARBA:ARBA00053337}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12A mediates
CC binding to myosin. Interacts with ARHA and CIT. Binds PPP1R12B, ROCK1
CC and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2
CC dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1.
CC Interacts with PPP1CB; the interaction is direct. Interacts (when
CC phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts
CC with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of
CC ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN. Interacts with
CC NCKAP1L. {ECO:0000256|ARBA:ARBA00063863}.
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_005068108.1; XM_005068051.3.
DR AlphaFoldDB; A0A1U7Q8W0; -.
DR STRING; 10036.ENSMAUP00000025068; -.
DR GeneID; 101822552; -.
DR KEGG; maua:101822552; -.
DR CTD; 4659; -.
DR eggNOG; KOG0505; Eukaryota.
DR OrthoDB; 539213at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0031672; C:A band; IEA:TreeGrafter.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:TreeGrafter.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:TreeGrafter.
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 FunFam; 1.25.40.20:FF:000004; Phosphatase 1 regulatory subunit 12A; 1.
DR FunFam; 1.25.40.20:FF:000876; Protein phosphatase 1 regulatory subunit 12A; 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; IPR051226; PP1_Regulatory_Subunit.
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; 1.
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|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038141};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 72..104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 105..137
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 198..230
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 231..263
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 932..1031
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 290..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 930..1018
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..480
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..610
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..660
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..693
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..800
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..853
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..914
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 115137 MW; 070A6806F681F45F CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADVNYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEDEGKK DESSCSSEED
EEDDSESEGE ADKTKPMASV TNAHTSSTQA APAAVTTPTL SSSQGTPTSP VKKFPTSTTK
ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL
DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN
SSINEGSTYH RSCSFGRRQD DLISSSVPST TSTPTVTSAT GLQKSLLSST STTAKSPTGS
SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTS
EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR
EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR SYDETYTRYR PVSTSSSTTP
PSSSLSTVSS SLYASSQLSR PNSLVGITSA YSRGLTKDNE REGEKKEEEK EGEDKSQSKS
IRERRRPREK RRSTGVSFWT QDSDENEQER QSDTEDGSNK KETQTDSVSR YDSSSTSSSD
RYDSLLGRSG SYSYLEERKP YSSRLEKDDS ADFKKLYEQI LAENEKLKAQ LHDTNMELTD
LKLQLEKATQ RQERFADRSL LEMEKRERRA LERRISEMEE ELKMLPDLKA DNQRLKDENG
ALIRVISKLS K
//
