PP1R8_ARATH
ID PP1R8_ARATH Reviewed; 369 AA.
AC Q9FIK2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein phosphatase 1 regulatory inhibitor subunit PPP1R8 homolog {ECO:0000305};
GN OrderedLocusNames=At5g47790 {ECO:0000312|Araport:AT5G47790};
GN ORFNames=MCA23.11 {ECO:0000312|EMBL:BAB11326.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN PROTEIN
RP PHOSPHATASE PPP1CC.
RX PubMed=21222654; DOI=10.1042/bj20101035;
RA Templeton G.W., Nimick M., Morrice N., Campbell D., Goudreault M.,
RA Gingras A.C., Takemiya A., Shimazaki K., Moorhead G.B.;
RT "Identification and characterization of AtI-2, an Arabidopsis homologue of
RT an ancient protein phosphatase 1 (PP1) regulatory subunit.";
RL Biochem. J. 435:73-83(2011).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1 (PP1). Binds to and
CC inhibits PP1 activity. {ECO:0000250|UniProtKB:Q9LTK0}.
CC -!- SUBUNIT: Interacts with human protein phosphatase PPP1C.
CC {ECO:0000269|PubMed:21222654}.
CC -!- INTERACTION:
CC Q9FIK2; Q8S307: BZR1; NbExp=3; IntAct=EBI-25523851, EBI-1803261;
CC Q9FIK2; O24409: IAA19; NbExp=3; IntAct=EBI-25523851, EBI-632257;
CC Q9FIK2; Q8LAL2: IAA26; NbExp=3; IntAct=EBI-25523851, EBI-3947418;
CC Q9FIK2; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-25523851, EBI-3946459;
CC Q9FIK2; P33078: IAA5; NbExp=3; IntAct=EBI-25523851, EBI-3946487;
CC Q9FIK2; Q38824: IAA6; NbExp=3; IntAct=EBI-25523851, EBI-1554124;
CC Q9FIK2; Q38827: IAA9; NbExp=3; IntAct=EBI-25523851, EBI-632216;
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DR EMBL; AB016886; BAB11326.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95572.1; -; Genomic_DNA.
DR EMBL; AY075675; AAL77682.1; -; mRNA.
DR EMBL; BT010168; AAQ22637.1; -; mRNA.
DR RefSeq; NP_199590.1; NM_124153.6.
DR AlphaFoldDB; Q9FIK2; -.
DR SMR; Q9FIK2; -.
DR IntAct; Q9FIK2; 7.
DR STRING; 3702.AT5G47790.1; -.
DR iPTMnet; Q9FIK2; -.
DR PaxDb; Q9FIK2; -.
DR PRIDE; Q9FIK2; -.
DR ProteomicsDB; 249084; -.
DR EnsemblPlants; AT5G47790.1; AT5G47790.1; AT5G47790.
DR GeneID; 834830; -.
DR Gramene; AT5G47790.1; AT5G47790.1; AT5G47790.
DR KEGG; ath:AT5G47790; -.
DR Araport; AT5G47790; -.
DR TAIR; locus:2160872; AT5G47790.
DR eggNOG; KOG1880; Eukaryota.
DR HOGENOM; CLU_032430_0_0_1; -.
DR InParanoid; Q9FIK2; -.
DR OMA; PHKNGSV; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q9FIK2; -.
DR PRO; PR:Q9FIK2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIK2; baseline and differential.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..369
FT /note="Protein phosphatase 1 regulatory inhibitor subunit
FT PPP1R8 homolog"
FT /id="PRO_0000442227"
FT DOMAIN 87..138
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 39985 MW; F54F9D5E33E87774 CRC64;
MYGRSGLDRF KKSQTSEPFS VSANPPPVVQ QHLSPEALSG QKTQIGAGQS NWHPPDWAIE
PRAGVYSLEV VKDGQILDRI HLDRRRHIFG RQHQTCDFVL DHQSVSRQHA AVVPHKNGSI
FVIDLGSAHG TFVANERLTK DTPVELEVGQ SLRFAASTRI YLLRKNSEAL FSRPPPPAEI
KLPPPPDASD EEAVVAYNTL LNRYGLSNGE SGGMLGKRKE KTGSEAGVAK RMKKVRVSFR
DQLGGELAEI VGMSDGADVE TEPGPINVKE GSLVGKYESL VRVTLIPKGK VKEEKAFTGG
TRGGVTDRLQ EAMNMLKRGP KTGIYDDLYG GDSLAKAVGT SWASVSQPAA ETECGGVGEE
DDNDDLFGD
