ID A0A7J8G2A2_MOLMO Unreviewed; 1030 AA.
AC A0A7J8G2A2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN ORFNames=HJG59_014659 {ECO:0000313|EMBL:KAF6453532.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6453532.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6453532.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6453532.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6453532.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6453532.1}.
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DR EMBL; JACASF010000010; KAF6453532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8G2A2; -.
DR InParanoid; A0A7J8G2A2; -.
DR OrthoDB; 539213at2759; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
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:UP000550707};
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 931..1030
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 290..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 936..1017
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 383..402
FT /note="Low complexity"
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 644..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 771..795
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..852
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 115365 MW; B0B8DC41786C208E CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGHGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDDEEEGKK DESSCSSEED
EEDDSESEAE TDKTKPMASV TNASTSSTQA APVAVTTPTV SSGQATPTSP VKKFPTSATK
ISSKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVMRS ASSPRLSSSL
DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKRN
SSINEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTS
EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR
EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR TYDETYQRYR SVSTSSSTTP
SSSLSTMSSS LYASSQLNRP NSLVGITSAY SRGLTKENER EGEKREEEKE GEDKSQPKSI
RERRRPREKR RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSASDR
YDSLLGRSAS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL HDTNMELTDL
KLQLEKATQR QERFTDRSLL EMEKRERRAL ERRISEMEEE LKMLPDLKAD NQRLKDENGA
LIRVISKLSK
//
