PPR37_RAT
ID PPR37_RAT Reviewed; 710 AA.
AC B2RYF1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 37;
DE AltName: Full=Leucine-rich repeat-containing protein 68;
GN Name=Ppp1r37; Synonyms=Lrrc68;
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] {ECO:0000312|EMBL:EDM08187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI66755.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI66755.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581, AND IDENTIFICATION BY
RP 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: Inhibits phosphatase activity of protein phosphatase 1 (PP1)
CC complexes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP1R37 family. {ECO:0000305}.
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DR EMBL; CH473979; EDM08187.1; -; Genomic_DNA.
DR EMBL; BC166755; AAI66755.1; -; mRNA.
DR RefSeq; NP_001100952.1; NM_001107482.1.
DR AlphaFoldDB; B2RYF1; -.
DR SMR; B2RYF1; -.
DR STRING; 10116.ENSRNOP00000023866; -.
DR CarbonylDB; B2RYF1; -.
DR iPTMnet; B2RYF1; -.
DR PhosphoSitePlus; B2RYF1; -.
DR jPOST; B2RYF1; -.
DR PaxDb; B2RYF1; -.
DR PeptideAtlas; B2RYF1; -.
DR PRIDE; B2RYF1; -.
DR Ensembl; ENSRNOT00000023867; ENSRNOP00000023866; ENSRNOG00000017692.
DR GeneID; 308398; -.
DR KEGG; rno:308398; -.
DR UCSC; RGD:1595870; rat.
DR CTD; 284352; -.
DR RGD; 1595870; Ppp1r37.
DR eggNOG; KOG1908; Eukaryota.
DR GeneTree; ENSGT00940000157454; -.
DR HOGENOM; CLU_014302_0_0_1; -.
DR InParanoid; B2RYF1; -.
DR OMA; EHELRCP; -.
DR OrthoDB; 1186874at2759; -.
DR PhylomeDB; B2RYF1; -.
DR PRO; PR:B2RYF1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000017692; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; B2RYF1; RN.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13516; LRR_6; 3.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome; Repeat.
FT CHAIN 1..710
FT /note="Protein phosphatase 1 regulatory subunit 37"
FT /id="PRO_0000398617"
FT REPEAT 224..244
FT /note="LRR 1"
FT REPEAT 252..273
FT /note="LRR 2"
FT REPEAT 281..301
FT /note="LRR 3"
FT REPEAT 310..330
FT /note="LRR 4"
FT REPEAT 338..358
FT /note="LRR 5"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75864"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 710 AA; 76934 MW; CA92E638236BA23A CRC64;
MEIPPQEAPP GPGADADADA EAEEAPAEAG SSSGASPPTD GRLKAAAKRV TFPSDEDIVS
GAVEPKDPWR HAQNVTVDEV ISAYRQACQK LNCRQIPKLL RQLQEFTDLE QRINCLDLKG
EKLDYKTCEA LEEVFKRLQF KVVDLEQTNL DEDGASALFD MIEYYESATH LNISFNKHIG
TRGWQAAAHM MRKTSCLQYL DARNTPLLDH SAPFVARALR IRSSLAVLHL ENASLSGRPL
MLLATALKMN MNLQELYLAD NKLNGLQDSA QLGNLLKFNC SLQILDLRNN HVLDSGLAYI
CEGLKEQRKG LVTLVLWNNQ LTHTGMAFLG MALPHTQSLE TLNLGHNPIG NEGVRNLKNG
LISNRSVLRL GLASTKLTCE GAVAVAEFIA ESPRLLRLDL RENEIKTGGL MALSLALKVN
HSLLRLDLDR EPKKEPVKSF IETQKALLAE IQNGCKRNFV LVREREEKQQ LQPSASMPEI
TITAPQPLEE SGDLPAMGAQ NGTPGPGPGP DSDSDSDSDR EEQEEEEEDQ SDQQRDEGGT
DQSSSAPCPA LLPSTDSLGP GDKSPPGSPS SPTEQRISVS SPGRGHKVFV VTRVESPPER
PEPPVPPTSV SSPPPSPPSP PASPPSQTMD TQDPESSEAQ PQTEPSQAGQ PLPNGLKPEF
ALALAPEAPP GLEAKGSSCS LEHALHRSHG VSKLEELLLE ASQEAPRDTL