ID A0A9J7HQV9_BRAFL Unreviewed; 781 AA.
AC A0A9J7HQV9;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
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=LOC118407388 {ECO:0000313|RefSeq:XP_035663753.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035663753.1};
RN [1] {ECO:0000313|RefSeq:XP_035663753.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035663753.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035663753.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_035663753.1; XM_035807860.1.
DR GeneID; 118407388; -.
DR Proteomes; UP000001554; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; 2.
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 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:UP000001554};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 77..109
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 110..142
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 203..235
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 236..268
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 683..781
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..448
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..615
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 87775 MW; B2C8731DD0157D39 CRC64;
MAVDYSRLAS AKEKRQEQLK RWLESDTERE PTVPKRKRSR VKFQEGCVFL AACAAGDTEE
VGQLLTNGAD INTANVDGLT ALHQACIDDN MDMVKFLVEK EADMEYPDNE GWTALHATVS
CGHLEITQYL IESGADLSAV NNEGETPLDL AEDEEMEQLI HKFVEHQSID LDAARREEER
RMIEDANQWL NSRVIKEKKH SKSGASALHV AAAKGYIKVM QLLIQAGVPI NAVDNDGWTP
LHAAAHWGQK EACEVLAESM CNMNVTNFAG QSPFDIADVD VLPYLEELKK RQATIKKERP
AEKLVIDITN EHEKAPLKRS MGSQSAPFSS YNGPADPELR TSVSRISLKD KTSFMQDISE
ERRTLESSIL KKNKKQASSS EESSSEESSE ETNSEDEGVD KERRQGGGVT LTRITPADTN
QHGPTTTPTA ALTHKPSDTD ATATAAAASR KVLDDKAPTS WRAGLRKTGS SSAVPETNNG
ESKDKLQRSP STPSIFYKPW EERLKEREKD KERERKESRE DRLRRLGIMP PETKDNKDKT
ESREDRLRRL GILPPADNKD KDKDNTANTD TAGTSLYMRR KGGSESETAV ARTGSSLTVT
QSTAPSTVTT TTSTSNRRSY LAPQRDEESE TQRKARSRRA RETRRSTQGV TMDDLEAAEK
TIRKDKEEKE RRDKEGKENG TAKELYEDAV AENEKLKEKV NELKTELAGS KVQMERDKQR
RDRFPDRSLL LETEKREKRA LERRISEMEE ELKQLADLRA DNQRLKDENG ALIRVISKLS
K
//
