MYPT1_DANRE
ID MYPT1_DANRE Reviewed; 1049 AA.
AC Q6DRG7; Q4G0B0; Q5TZ13;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
DE AltName: Full=Myosin phosphatase-targeting subunit 1;
DE Short=Myosin phosphatase target subunit 1;
DE AltName: Full=Protein phosphatase myosin-binding subunit;
GN Name=ppp1r12a; Synonyms=mbs, mypt1; ORFNames=si:dkey-28j4.1, zgc:110448;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates myosin phosphatase activity. {ECO:0000250}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, and one or several
CC targeting or regulatory subunits. Ppp1r12a mediates binding to myosin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DRG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DRG7-2; Sequence=VSP_035913, VSP_035914;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH69075.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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 EMBL; AY648792; AAT68110.1; -; mRNA.
DR EMBL; BX537286; CAH69075.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC098558; AAH98558.1; -; mRNA.
DR RefSeq; NP_001003870.2; NM_001003870.2. [Q6DRG7-1]
DR AlphaFoldDB; Q6DRG7; -.
DR SMR; Q6DRG7; -.
DR STRING; 7955.ENSDARP00000118021; -.
DR PaxDb; Q6DRG7; -.
DR GeneID; 445393; -.
DR KEGG; dre:445393; -.
DR CTD; 4659; -.
DR ZFIN; ZDB-GENE-041011-3; ppp1r12a.
DR eggNOG; KOG0505; Eukaryota.
DR InParanoid; Q6DRG7; -.
DR OrthoDB; 477969at2759; -.
DR PhylomeDB; Q6DRG7; -.
DR TreeFam; TF105543; -.
DR Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DRE-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q6DRG7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031672; C:A band; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0019208; F:phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:ZFIN.
DR GO; GO:0070650; P:actin filament bundle distribution; IMP:ZFIN.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IGI:ZFIN.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:ZFIN.
DR GO; GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 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 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; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Cytoplasm; Reference proteome; Repeat.
FT CHAIN 1..1049
FT /note="Protein phosphatase 1 regulatory subunit 12A"
FT /id="PRO_0000355557"
FT REPEAT 39..68
FT /note="ANK 1"
FT REPEAT 72..101
FT /note="ANK 2"
FT REPEAT 105..134
FT /note="ANK 3"
FT REPEAT 138..164
FT /note="ANK 4"
FT REPEAT 198..227
FT /note="ANK 5"
FT REPEAT 231..260
FT /note="ANK 6"
FT REGION 302..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 560..623
FT /note="STSHTLALGRTSSSRDLPAKSSSASSLEPNNSKAWQPSSYYQSYSIHRSGSF
FT GRRHEDPLSSTS -> RLAFYSVLVLLVCQSMLLLLLLLSQMLLAPFTDKLLAPALSLH
FT LCLIVILKHHNHLINIVRVDV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035913"
FT VAR_SEQ 624..1049
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035914"
FT CONFLICT 489
FT /note="K -> E (in Ref. 3; AAH98558)"
FT /evidence="ECO:0000305"
FT CONFLICT 655..656
FT /note="Missing (in Ref. 1; AAT68110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1049 AA; 117322 MW; 74003FC6728147B4 CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPLLK KKKTKVKFDD GAVFLAACSS GDTEEVLRML
DRGADINYAN VDGLTALHQA CIDDNVDMVT FLVEHGACIN QPDNEGWIPL HAAASCGYLD
IAEYLISQGA SVGVVNSEGE TPLDIAEEEA MEELLQNEIN RQGVDIEAAR KEEERIMLRD
ARQWLNSGQI NDVRHTKSGG TALHVAAAKG YAEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVEHLCDMDV VNKVGQTAFD VADEDILGYL EELQKKQNLL LSEKKDVKKS
PLIETTTTGD NNQSVKPLKS KETLLLEPEK TAPRIETLEP EKVDEEEGEG KKDESSCSSE
EEEEEDSESE NEADKTKSSV PSSVSNSTPT TAPSSITVTS PTTPSNQVTT PTSPTKKVST
PAGKLSPKEE DRKDESPASW RLGLRKTGSY GALAEISTTK EAQKEKDTAG VMRSASSPRL
SSSLDNKDKE KEKEKTRLAY VAPTIPRRHV STSDIDEKEN RDSAASLVRS GSYTRRRWEE
DLKNSDGTAS TNRTSSYQRS TSHTLALGRT SSSRDLPAKS SSASSLEPNN SKAWQPSSYY
QSYSIHRSGS FGRRHEDPLS STSSSTTTTT TTSSVTSPTG HRSLLSRYWA EESAEKEKEK
EKESATVIPT INTAGTTTTT STTGTVLGSD GRERRRSYLT PVRDEESESQ RKARSRQARQ
SRRSTQGVTL TDLQEAEKTI GRSRPTRPRE DEKEEKEKQD KEKQEEKKET ETKEDDYRSR
YRSFEEKYRT SLASSTTASS TIPSSSSSSS SSLYSTSSLN RPNSLTGLTS TYSRSTRDTD
RESDRKEKDE DRDGDDKSQP RSIRDRRRPR EKRRSTGVSF WTQDSDENEP DHPSDSEGST
KGEPQSDRLS SNDPLSTSTS STDRYESLSS RGIGESRRPY SRFEKDDSTD YKKLYEQILA
ENEKLKAQLR DTELELSDLK LQLEKATQRQ ERFADRSQLE MEKRERRALE RKISEMEEEL
KMLPDLKADN QRLKDENGAL IRVISKLSK
