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Database: UniProt
Entry: A0A452QLW8_URSAM
LinkDB: A0A452QLW8_URSAM
Original site: A0A452QLW8_URSAM 
ID   A0A452QLW8_URSAM        Unreviewed;       985 AA.
AC   A0A452QLW8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN   Name=PPP1R12A {ECO:0000313|Ensembl:ENSUAMP00000006333.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000006333.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000006333.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A452QLW8; -.
DR   STRING; 9643.ENSUAMP00000006333; -.
DR   Ensembl; ENSUAMT00000007160.1; ENSUAMP00000006333.1; ENSUAMG00000005344.1.
DR   GeneTree; ENSGT00940000156120; -.
DR   OMA; DETCQRY; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0043292; C:contractile fiber; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:Ensembl.
DR   GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR   GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR   GO; GO:0019208; F:phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
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   PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR   PANTHER; PTHR24179:SF20; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12A; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR   PRINTS; PR01415; ANKYRIN.
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   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:UP000291022}.
FT   REPEAT          72..104
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          105..137
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          198..230
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          231..263
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          290..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          927..961
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        303..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  109932 MW;  70F8F4130A4AA35A CRC64;
     MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
     HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
     IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
     ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
     HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP
     LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDDEEEGKK DESSCSSEED
     EEDDSESEAE TDKTKPMASV TNANTSSTQA APVAVTTPVS SGQATPTSPM KKFPTSATKV
     SPKEEERKDE SPASWRLGLR KTGSYGALAE ITASKEAQKD KDTAGVMRSA SSPRLSSSLD
     NKEKEKDSKG TRLAYVAPTI PRRLASTSDI EEKENRDSSS LRTSSSYTRR KWEDDLKKNS
     SVNEGSTYHK SCSFGRRPDD LISSSVPSTT STPTVTSAAG LQKSLLSSTS TTTKITTGSS
     SAGTQSSTSN RLWAEDSTEK EKDSVPTALT IPVAPTVVNA AASTTTLTTT TAGTVSSTSE
     VRERRRSYLT PVRDEESESQ RKARSRQARQ SRRSTQGVTL TDLQEAEKTI GRSRSTRTRE
     QENEEKEKEE KEKQDKEKQE EKKESETSRE DEYKQKYSRT YDETYQRYRP VSTSSSTTPS
     SSISTMSSSL YASSQLNRPN SLVGITSAYS RGLTKENERE GEKREEEKEG EDKSQPKSIR
     ERRRPREKRR STGVSFWTQD SDENEQEQQS DTEEGSNKKE TQVKSSFSGD RYDSLLGRSG
     SYTYLEERKP YSSRLEKDDS TDFKKLYEQI LAENEKLKAQ LHDTNMELTD LKLQLEKATQ
     VCTFFSLDQT QHIVRISDFE QVSKH
//
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