ID   RBBP9_RAT               Reviewed;         186 AA.
AC   O88350; Q3T1H7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Serine hydrolase RBBP9 {ECO:0000250|UniProtKB:O75884};
DE            EC=3.-.-.- {ECO:0000250|UniProtKB:O75884};
DE   AltName: Full=B5T-overexpressed gene protein {ECO:0000303|PubMed:9697699};
DE            Short=Protein BOG {ECO:0000303|PubMed:9697699};
DE   AltName: Full=Retinoblastoma-binding protein 9;
DE            Short=RBBP-9;
GN   Name=Rbbp9 {ECO:0000312|RGD:3542};
GN   Synonyms=Bog {ECO:0000303|PubMed:9697699};
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], FUNCTION, INTERACTION WITH RB1; RBL1 AND RBL2,
RP   TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-63.
RC   TISSUE=Liver;
RX   PubMed=9697699; DOI=10.1038/1258;
RA   Woitach J.T., Zhang M., Niu C.-H., Thorgeirsson S.S.;
RT   "A retinoblastoma-binding protein that affects cell-cycle control and
RT   confers transforming ability.";
RL   Nat. Genet. 19:371-374(1998).
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).
CC   -!- FUNCTION: Serine hydrolase whose substrates have not been identified
CC       yet (By similarity). May negatively regulate basal or autocrine TGF-
CC       beta signaling by suppressing SMAD2-SMAD3 phosphorylation (By
CC       similarity). May play a role in the transformation process due to its
CC       capacity to confer resistance to the growth-inhibitory effects of TGF-
CC       beta through interaction with RB1 and the subsequent displacement of
CC       E2F1 (PubMed:9697699). {ECO:0000250|UniProtKB:O75884,
CC       ECO:0000269|PubMed:9697699}.
CC   -!- SUBUNIT: Interacts with RB1; the interaction disrupts RB1 binding to
CC       E2F1 (PubMed:9697699). Interacts with RBL1 and RBL2 (PubMed:9697699).
CC       {ECO:0000269|PubMed:9697699}.
CC   -!- INTERACTION:
CC       O88350; P33568: Rb1; NbExp=4; IntAct=EBI-1211014, EBI-1162932;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the spleen, testis and kidney.
CC       Also found in the heart, liver, lung and brain.
CC       {ECO:0000269|PubMed:9697699}.
CC   -!- SIMILARITY: Belongs to the RBBP9 family. {ECO:0000305}.
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DR   EMBL; AF025819; AAC40205.2; -; mRNA.
DR   EMBL; BC101915; AAI01916.1; -; mRNA.
DR   RefSeq; NP_062092.2; NM_019219.2.
DR   AlphaFoldDB; O88350; -.
DR   SMR; O88350; -.
DR   IntAct; O88350; 3.
DR   STRING; 10116.ENSRNOP00000010678; -.
DR   ESTHER; ratno-rbbp9; Hydrolase_RBBP9_YdeN.
DR   iPTMnet; O88350; -.
DR   PhosphoSitePlus; O88350; -.
DR   jPOST; O88350; -.
DR   PaxDb; O88350; -.
DR   PRIDE; O88350; -.
DR   GeneID; 29459; -.
DR   KEGG; rno:29459; -.
DR   UCSC; RGD:3542; rat.
DR   CTD; 10741; -.
DR   RGD; 3542; Rbbp9.
DR   VEuPathDB; HostDB:ENSRNOG00000007972; -.
DR   eggNOG; ENOG502QVNM; Eukaryota.
DR   HOGENOM; CLU_088863_1_0_1; -.
DR   InParanoid; O88350; -.
DR   OMA; NHWFPWL; -.
DR   OrthoDB; 1320428at2759; -.
DR   PhylomeDB; O88350; -.
DR   TreeFam; TF106470; -.
DR   PRO; PR:O88350; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000007972; Expressed in ovary and 19 other tissues.
DR   Genevisible; O88350; RN.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0009624; P:response to nematode; ISO:RGD.
DR   GO; GO:0060510; P:type II pneumocyte differentiation; ISO:RGD.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010662; Hydrolase_RBBP9/YdeN.
DR   Pfam; PF06821; Ser_hydrolase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..186
FT                   /note="Serine hydrolase RBBP9"
FT                   /id="PRO_0000097182"
FT   REGION          63..67
FT                   /note="Involved in binding to RB1"
FT                   /evidence="ECO:0000250|UniProtKB:O75884"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75884"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75884"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75884"
FT   MUTAGEN         63
FT                   /note="L->Q: Loss of binding to RB1 binding."
FT                   /evidence="ECO:0000269|PubMed:9697699"
SQ   SEQUENCE   186 AA;  20995 MW;  41EC9779708E5E19 CRC64;
     MASPTKAVIV PGNGGGDVAT HGWYGWVRKG LEQIPGFQCL AKNMPDPITA RESIWLPFME
     TELHCDEKTI IIGHSSGAIA AMRYAETHQV YALILVSAYT SDLGDENERA SGYFSRPWQW
     EKIKANCPHI IQFGSTDDPF LPWKEQQEVA DRLDAKLYKF TDRGHFQNTE FHELIRVVKS
     MLTPAL