ID A0A5G2QP28_PIG Unreviewed; 775 AA.
AC A0A5G2QP28;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN Name=PPP1R12C {ECO:0000313|Ensembl:ENSSSCP00000066648.1,
GN ECO:0000313|VGNC:VGNC:91720};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000066648.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000066648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000066648.1};
RX PubMed=32543654;
RA Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT "An improved pig reference genome sequence to enable pig genetics and
RT genomics research.";
RL Gigascience 9:0-0(2020).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000066648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Regulates myosin phosphatase activity.
CC {ECO:0000256|ARBA:ARBA00055480}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12C mediates
CC binding to myosin. Interacts via its N-terminus with PPP1CB. Interacts
CC with IL16. Interacts with the coiled-coil domain of MPRIP. Interacts
CC with NOD2. {ECO:0000256|ARBA:ARBA00065524}.
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; A0A5G2QP28; -.
DR SMR; A0A5G2QP28; -.
DR FunCoup; A0A5G2QP28; 988.
DR STRING; 9823.ENSSSCP00000066648; -.
DR GlyGen; A0A5G2QP28; 2 sites.
DR Ensembl; ENSSSCT00000087181.2; ENSSSCP00000066648.1; ENSSSCG00000027189.4.
DR VGNC; VGNC:91720; PPP1R12C.
DR GeneTree; ENSGT00940000161425; -.
DR InParanoid; A0A5G2QP28; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000027189; Expressed in stomach and 43 other cell types or tissues.
DR ExpressionAtlas; A0A5G2QP28; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0017020; F:myosin phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21945; IPD_PPP1R12C; 1.
DR FunFam; 1.25.40.20:FF:000004; Phosphatase 1 regulatory subunit 12A; 1.
DR FunFam; 1.25.40.20:FF:000212; Protein phosphatase 1 regulatory subunit; 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:SF27; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12C; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 4.
DR PRINTS; PR01415; ANKYRIN.
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 1: Evidence at protein level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038141};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A5G2QP28};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 100..132
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 133..165
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 226..258
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 259..291
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 692..746
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 696..737
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..11
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..542
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 83262 MW; 05956A4ACB447118 CRC64;
MSGEDGPGAG PGAAAAAARE RRREQLRQWG ARAGAEPGPG ERRARTVRFE RAAEFLAACA
GGDLDEARLM LRAADPDPDA ELDPSAPPPA RAVLDSTNAD GISALHQACI DENLEVVRFL
VEQGATVNQA DNEGWTPLHV AASCGYLDIA RYLLSHGANI ASVNSDGDLP LDLAESDAME
GLLKAEITRR GVDVEAAKRA EEELLLHDTR CWLNGGAMPE ARHPRTGASA LHVAAAKGYI
EVMRLLLQAG YDPELRDGDG WTPLHAAAHW GVEDACRLLA EHGGGMDSLT HAGQRPCDLA
DEEVLSLLEE LARKQEDLRN QKEASQSRGQ EPPVPSSSRH RRSSVCRLSS REKISLQDLS
KERRPGGAGG PPIRDEDEGE EGPSDSSPAE SRTLNGISSP PPSSPQSPTT PEEASFPRRF
GLQKTGSSGA LGPTGGRAAE VASRAGLQRS ASSSRLEGTS TQAREPRLAR VTPTPSRKVP
ESSAPILEPE SPGSPVKPNV PVASAAPPAD SRDRRRIYQM PVRDEESESQ RKARSRLMRQ
SRRSTQGVTL TDLKEAEKAA GKASEPEKSC PQSLDPSRRP RVPGLENSDG PAQREAPDGQ
GQGPPAAREH RRVGKERRGP AEGEEAEPVD RGPESRYLVG RKGLGLSVGL WARPLTPRLP
HPSTPEGGPS SRRQRDLNPE PEPESEEPDG GFRKLYADLR SENERLREAL TETTLQLAQL
KVELERATQR QERFAERPAL LELERFVSEG GGGGASCVSS LPSPCGRVRR AALPF
//
