PP4R1_RAT
ID PP4R1_RAT Reviewed; 951 AA.
AC Q8VI02;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 1;
GN Name=Ppp4r1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11729228; DOI=10.1681/asn.v12122601;
RA Wada T., Miyata T., Inagi R., Nangaku M., Wagatsuma M., Suzuki D.,
RA Wadzinski B.E., Okubo K., Kurokawa K.;
RT "Cloning and characterization of a novel subunit of protein
RT serine/threonine phosphatase 4 from mesangial cells.";
RL J. Am. Soc. Nephrol. 12:2601-2608(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4.
CC May play a role in regulation of cell division in renal glomeruli. The
CC PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and
CC regulation of HDAC3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complex PPP4C-PPP4R1. Interacts with
CC HDAC3 (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in anti-Thy1 glomerulonephritis.
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DR EMBL; AF332004; AAL37490.1; -; mRNA.
DR EMBL; BC061726; AAH61726.1; -; mRNA.
DR RefSeq; NP_543183.1; NM_080907.2.
DR AlphaFoldDB; Q8VI02; -.
DR STRING; 10116.ENSRNOP00000061977; -.
DR PhosphoSitePlus; Q8VI02; -.
DR jPOST; Q8VI02; -.
DR PaxDb; Q8VI02; -.
DR GeneID; 140943; -.
DR KEGG; rno:140943; -.
DR UCSC; RGD:619798; rat.
DR CTD; 9989; -.
DR RGD; 619798; Ppp4r1.
DR eggNOG; KOG0211; Eukaryota.
DR InParanoid; Q8VI02; -.
DR OrthoDB; 249499at2759; -.
DR PhylomeDB; Q8VI02; -.
DR PRO; PR:Q8VI02; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR031087; PP4R1.
DR PANTHER; PTHR10648:SF8; PTHR10648:SF8; 1.
DR Pfam; PF02985; HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..951
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 1"
FT /id="PRO_0000071529"
FT REPEAT 26..63
FT /note="HEAT 1"
FT REPEAT 82..119
FT /note="HEAT 2"
FT REPEAT 127..164
FT /note="HEAT 3"
FT REPEAT 168..206
FT /note="HEAT 4"
FT REPEAT 208..246
FT /note="HEAT 5"
FT REPEAT 248..285
FT /note="HEAT 6"
FT REPEAT 287..324
FT /note="HEAT 7"
FT REPEAT 502..539
FT /note="HEAT 8"
FT REPEAT 699..735
FT /note="HEAT 9"
FT REPEAT 777..815
FT /note="HEAT 10"
FT REPEAT 820..858
FT /note="HEAT 11"
FT REPEAT 862..899
FT /note="HEAT 12"
FT REGION 326..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF05"
SQ SEQUENCE 951 AA; 105615 MW; A71CB93FD24F8D17 CRC64;
MADLSLLQED LPEDADGLGV DDYSSESDVI IIPSALDFVS QDEMLTPLGR LDKYAASENV
FNRQMVARSL LDTLREVCGE ERDCIAVLER ISRLADDSEP TVRAELMEQV PHIALFCQEN
RPSIPYAFSK YLLPIVVRYL ADQNNQVRKT SQAALLALLE QELIERLDVE TKVCPVLIDL
TAPDSNDDVK TEAVAIMCKM APMVGKDITE RLILPRFCEM CCDCRMFHVR KVCAANFGDI
CSVVGQQATE EMLLPRFFQL CSDNVWGVRK ACAECFMAVS CATCQEIRRT KLSALFINLI
SDPSRWVRQA AFQSLGPFIS TFANPSSSGQ CFKDESKSSE DKDRIRDDGV VQEEQSRPED
APSDLSAPHS SARLDGTLEG CAAETPGDSA GDMRVPADSS LLCTLSSESP QEAASDAESG
KKHDNNSKSA SRPDVGTSSP EPTPLDQEMF NSFHFWRTPL PQIDLDKELQ QDPGERPSPE
RTGDAPAAPV PGSPSITMAT RKELEEMIEN LEPHMDDPDV KAQVEVLSAA LRASTLDAHD
EAGGAEQRSE LQDDAVGAGG ELPNCSISED TSEPLVIAAE ENMEATPDYI HGGADVGPGG
GGGFSPDEER RPKVQDVVPQ ALLDQYLSMT DPSRAQTVDT EIAKHCAYSL PGVALTLGRQ
NWHCLRETYE TLASDMQWKV RRTLAFSIHE LAVILGDQLT AADLVPIFNG FLKDLDEVRI
GVLKHLHDFL KLLHIDKRRE YLYQLQEFLV TDNSRNWRFR AELAEQLILL LELYSPRDVY
DYLRPIALNL CADKVSSVRW ISYKLVSEMV KKLHMATPPT FGVELINELV ENFGRCPKWS
GRQAFVFVCQ TVIEDDCLPM DQFAVHLMPH LLTLANDRVP NVRVLLAKTL RQTLLEKEYF
LASASCHQEA VEQTIMALQM DRDSDVKYFA SIHPSSTKLS EDAMSTASST Y
