ID A0A9R1U6I1_9HYME Unreviewed; 997 AA.
AC A0A9R1U6I1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12B {ECO:0000256|ARBA:ARBA00072757};
DE AltName: Full=Myosin phosphatase-targeting subunit 2 {ECO:0000256|ARBA:ARBA00083252};
GN Name=Mbs {ECO:0000313|RefSeq:XP_011309027.1};
OS Fopius arisanus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC Opiinae; Fopius.
OX NCBI_TaxID=64838 {ECO:0000313|Proteomes:UP000694866, ECO:0000313|RefSeq:XP_011309027.1};
RN [1] {ECO:0000313|RefSeq:XP_011309027.1}
RP IDENTIFICATION.
RC STRAIN=USDA-PBARC FA_bdor {ECO:0000313|RefSeq:XP_011309027.1};
RC TISSUE=Whole organism {ECO:0000313|RefSeq:XP_011309027.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+)
CC sensitivity of the contractile apparatus.
CC {ECO:0000256|ARBA:ARBA00059024}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12B mediates
CC binding to myosin. Isoform 3 and isoform 4 bind PPP1R12A, but not
CC isoform 1 of PPP1R12B itself. Binds IL16.
CC {ECO:0000256|ARBA:ARBA00065548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the NRARP family.
CC {ECO:0000256|ARBA:ARBA00038386}.
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DR RefSeq; XP_011309027.1; XM_011310725.1.
DR GeneID; 105270029; -.
DR CTD; 49070; -.
DR OrthoDB; 19014at2759; -.
DR Proteomes; UP000694866; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:TreeGrafter.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21930; IPD_PPP1R12; 1.
DR FunFam; 1.25.40.20:FF:000004; Phosphatase 1 regulatory subunit 12A; 1.
DR FunFam; 1.25.40.20:FF:000007; 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:SF21; MYOSIN BINDING SUBUNIT, ISOFORM O; 1.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 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; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694866};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 76..108
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 109..141
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 202..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 235..267
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 898..993
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 290..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..380
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..391
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..572
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..611
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..709
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..784
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..825
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..885
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 109390 MW; A740AA04B6CA2990 CRC64;
MSLETRSSSA LFKRAEQLKR WEQSETNSQP AQPKQIARKI KFSADCVFLA ACAAGDKDEV
VRLLQKGADI NTGNVDGLTA LHQACIDDDL DMVEFLVEQG ADINRGDNEG WTPLHATASC
GFISIAKYLI EQGCNLAAVN NDGELAVDIA ESNEMEDLLQ QHINKAGIDC DQARSEEERS
MLSDARAWRS GAPGKDATHP RSGATALHVA AAKGYIKVMN ILLQARCDVN AQDYDGWTPL
HGAAHWGQIE ACKLLVENFC DMDMKNYAGQ TAFDIADNDI VKALEELQKK QQGMMKDQPQ
LNNKKQSTIP KKRVSPTIEN AVVSQEGNDT FEEETPNKVI KVELEIQSDK EDTSTGTNSD
VESGEETDIE ASEVEGESES NSETQTSSGS NRSHPSDQSV GLTDDEKKNR ANKDDTGSLS
PVSPAEISKV PNQAPILPPK QQTENAEEGI IPSWRRSGSF RNRIQEAEST NSLTSKIEDK
ENSSTKTPII PNKVNPEPEV VLRRTHSFEK DEKKKEVKLN LELSRVPQES NASSPTSVSN
KILSSPTLPT GTSSSTTSTA STTTSTATTT TSPVPANQIR SVQSVETSST NVSPTRNTAT
TTSAPNTPAG SKLSPGNIFK NFFKSFVPPV RDEESETQRK AHAKRVRETR RSTQGVTLDE
IKSAEQLVKK KQQQSNDTSP VSAPQPAASI GQTASITATI TTATPTTVTP NKLPEETNLP
ERRPSWRLRV DNGSKFQLED ANNIKSSDTT TAYIRRPSGG TGIPRPSSAP VETITTGTAD
ATVTLPLRRS LKSPEDKEQD KENDSRNAQA TQAVIQRRRR PKRRSTGVVH VDMDEIDPEK
QDGSSVGESE EGKNNHTESG NERSGRSSRL GSVTSVSSEV PSTPSRTKST NSENGELDYK
KLWEESQAEN ERLKDKLRRS DDQLKETRSL LEKAQSNQNK AALSEIEKRE RRAMERKLSE
MEEELKQLQK LKAENERLKA ENRALTRVVS KLTNTTK
//
