ID G3HZ17_CRIGR Unreviewed; 982 AA.
AC G3HZ17;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN ORFNames=I79_016312 {ECO:0000313|EMBL:EGW07243.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07243.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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 EMBL; JH000955; EGW07243.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HZ17; -.
DR STRING; 10029.G3HZ17; -.
DR PaxDb; 10029-XP_007618328-1; -.
DR eggNOG; KOG0505; Eukaryota.
DR InParanoid; G3HZ17; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
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:SF20; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:UP000001075}.
FT REPEAT 1..17
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 18..50
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 111..143
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 144..176
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 883..982
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 203..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 888..969
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 216..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 109729 MW; 383A1295F4BCFFAA CRC64;
MVKFLVENGA NINQPDNEGW IPLHAAASCG YLDIAEFLIG QGAHVGAVNS EGDTPLDIAE
EEAMEELLQN EVNRQGVDIE AARKEEERIM LRDARQWLNS GHINDVRHAK SGGTALHVAA
AKGYTEVLKL LIQAGYDVNI KDYDGWTPLH AAAHWGKEEA CRILVDNLCD MEMVNKVGQT
AFDVADEDIL GYLEELQKKQ NLLHSEKRDK KSPLIESTAN MENNQPQKTF KNKETLIIEP
EKNASRIESL EQEKADEEDE GKKDESSCSS EEDEEDDSES EGEADKTKPM ASVTNAHTSS
TQAAPAAVTT PTLSSSQGTP TSPVKKFDFI ASLMPVESVD PASWRQGLRK TGIVLVPSKG
EKSMFPTSTT KISPKEEERK DESPASWRLG LRKTGSYGAL AEITASKEAQ KEKDSAGVIR
SASSPRLSSS LDNKEKEKDS KGTRLAYVAP TIPRRLASTS DIEEKENRDS SSLRTSSSYT
RRKWEDDLKK NSSINEGSTY HRSCSFGRRQ DDLISSSVPS TTSTPTVTSA TGLQKSLLSS
TSTTAKSPTG SSSAGTQSST SNRLWAEDST EKEKDSAPTA VTIPVAPTVV NAAASTTTLT
TTTAGTVSST SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK
TIGRSRSTRT REQENEEKEK EEKEKQDKEK QEEKKESETS REDEYKQKYS RSYDETYTRY
RPVSTSSSTT PSSSSLSTVS SSLYASSQLN RPNSLVGITS AYSRGLTKEN EREGEKKEEE
KEGEDKSQAK SIRERRRPRE KRRSTGVSFW TQDSDENEQE RQSDTEDGSN KKETQTDSVS
RYDSSSTSSS DRYDSLLGRS GSYSYLEERK PYSSRLEKDD STDFKKLYEQ ILAENEKLKA
QLHDTNMELT DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME EELKMLPDLK
ADNQRLKDEN GALIRVISKL SK
//
