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Database: UniProt
Entry: A0A3Q1M6G2_BOVIN
LinkDB: A0A3Q1M6G2_BOVIN
Original site: A0A3Q1M6G2_BOVIN 
ID   A0A3Q1M6G2_BOVIN        Unreviewed;       963 AA.
AC   A0A3Q1M6G2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN   Name=PPP1R12B {ECO:0000313|Ensembl:ENSBTAP00000065965.1,
GN   ECO:0000313|VGNC:VGNC:106875};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000065965.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000065965.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000065965.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000065965.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000065965.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   AlphaFoldDB; A0A3Q1M6G2; -.
DR   Ensembl; ENSBTAT00000070021.1; ENSBTAP00000065965.1; ENSBTAG00000011772.6.
DR   VEuPathDB; HostDB:ENSBTAG00000011772; -.
DR   VGNC; VGNC:106875; PPP1R12B.
DR   GeneTree; ENSGT00940000157067; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000011772; Expressed in corpus luteum and 105 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1M6G2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
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   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; IPR031775; PRKG1_interact.
DR   PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR   PANTHER; PTHR24179:SF18; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12B; 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; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   REPEAT          88..120
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          121..153
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          214..246
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          247..279
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          872..963
FT                   /note="cGMP-dependent protein kinase interacting"
FT                   /evidence="ECO:0000259|Pfam:PF15898"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          877..957
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..627
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  105503 MW;  1D773898197D760B CRC64;
     MAELEHLGGK RAESARARRA EQLRRWRGSP TEQEPADRPG AGPQARRGGP RVRFEDGAVF
     LAACSSGDTD EVRRLLARGA DVDTANVDGL TALHQACIDE NLDVVKFLVE NGASVNQQDN
     EGWTPLHAAA SCGYLNIAEY FINHGASVGI VNSEGEVPSD LAEEPAMKDL LLEQVKKQGL
     DLEQARRQEE QQMLQDARQW LNSGRIADVR QARSGATALH VAAAKGYSEV LRLLIQAGYE
     LNVQDHDGWT PLHAAAHWGV KEACSILAEA LCDMDIRNKL GQTPFDVADE GLVEHLETLQ
     KRQSVLRSEK ETRNKLIESD LNSKLHSRLF KNKEKMLCEE ETPKSQRVEE SKESSSSSSD
     EGEDEASESE AEKEAGDPEA GRPQSAGGRH VSEGRWSQPW GTDSQTGPRP FPSSLFSKPE
     ETRDESPCSW RLGLRKTGSQ NVLSEAAGAR EALRDRGASV HRSASSPRIS ALMDNREKER
     ETRSSLSSLG LRRPGSTSDL EEKENRESAA NLVRSGSQPR QPWRDAAKGS ETPQTAAPST
     YVSTFLKRTP YRSQADSTAE RADGVACSSP LCVITNRPPP STASGVPATT LLCAPGPEPS
     VEARQRRRSY LTPVRDEEAE SLRKARSRQA RQTRRSTQGV TLTDLQEAER TFSRSRVERQ
     AQEQPSLKPV GPGALEGGPR KHEPLAAPTQ EAGESRQPWG RSPEGEPVYH PLRCPAQPEQ
     PTAPASPSAP RPSLYSSSYL LRTGGSSAPD SQSSEPPTDT AGPRDMDKNG TLGFGKCSLQ
     SHCVLGAGWP LPRRACPVAL STSGENVRCP LASPPTPCCS RNQLPLPCVS HRLESGGSDA
     STERASARAR REAREARLAT LSSRTEEDGG RDYRKLYESA LTENQKLKTK LQEAQLELAD
     VKSKLEKMAQ VRRGEENQER RALERKMSEM EEEMKVLTEL KSDNQRLKDE NGALIRVISK
     LSK
//
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