ID   TIPRL_RAT               Reviewed;         271 AA.
AC   A2VCX1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=TIP41-like protein;
GN   Name=Tiprl;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, 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: May be a allosteric regulator of serine/threonine-protein
CC       phosphatase 2A (PP2A). Inhibits catalytic activity of the PP2A(D) core
CC       complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase
CC       activity. Acts as negative regulator of serine/threonine-protein
CC       phosphatase 4 probably by inhibiting the formation of the active
CC       PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA
CC       damage response by promoting H2AX phosphorylated on Ser-140 (gamma-
CC       H2AX). May play a role in the regulation of ATM/ATR signaling pathway
CC       controlling DNA replication and repair (By similarity).
CC       {ECO:0000250|UniProtKB:O75663}.
CC   -!- SUBUNIT: Interacts with PPP2CA. Interacts with PPP2CB, PPP4C and PPP6C.
CC       Interacts with IGBP1; the interaction is dependent on PPP2CA.
CC       Associates with a protein phosphatase 2A PP2A(C):IGBP1 complex.
CC       Interacts with PPP4C and PPP4R2 (By similarity).
CC       {ECO:0000250|UniProtKB:O75663, ECO:0000250|UniProtKB:Q8BH58}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TIP41 family. {ECO:0000305}.
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DR   EMBL; BC128780; AAI28781.1; -; mRNA.
DR   RefSeq; NP_001103137.1; NM_001109667.1.
DR   AlphaFoldDB; A2VCX1; -.
DR   SMR; A2VCX1; -.
DR   STRING; 10116.ENSRNOP00000004083; -.
DR   iPTMnet; A2VCX1; -.
DR   PhosphoSitePlus; A2VCX1; -.
DR   jPOST; A2VCX1; -.
DR   PaxDb; A2VCX1; -.
DR   PeptideAtlas; A2VCX1; -.
DR   PRIDE; A2VCX1; -.
DR   GeneID; 360869; -.
DR   KEGG; rno:360869; -.
DR   CTD; 261726; -.
DR   RGD; 1310442; Tiprl.
DR   VEuPathDB; HostDB:ENSRNOG00000003048; -.
DR   eggNOG; KOG3224; Eukaryota.
DR   HOGENOM; CLU_039187_2_0_1; -.
DR   InParanoid; A2VCX1; -.
DR   OMA; GIPIPEM; -.
DR   OrthoDB; 1377237at2759; -.
DR   PhylomeDB; A2VCX1; -.
DR   TreeFam; TF105943; -.
DR   PRO; PR:A2VCX1; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003048; Expressed in thymus and 20 other tissues.
DR   Genevisible; A2VCX1; RN.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   InterPro; IPR007303; TIP41-like.
DR   PANTHER; PTHR21021:SF16; PTHR21021:SF16; 1.
DR   Pfam; PF04176; TIP41; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..271
FT                   /note="TIP41-like protein"
FT                   /id="PRO_0000301855"
FT   REGION          173..271
FT                   /note="Interaction with PPP2CA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         106
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75663"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75663"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   271 AA;  31225 MW;  49558C71AE13EA7F CRC64;
     MMIHGFQSSH QDFSFGPWKL TASKTHIMKS ADVEKLADEL HMPSLPEMMF GDNVLRIQHG
     SGFGIEFNAT DALRCVNNYQ GMLKVACAEE WQESRTEGEH SKEVIKPYDW TYTTDYKGTL
     LGESLKLKVV PTTDHIDTEK LKAREQIKFF EEVLLFEDEL HDHGVSSLSV KIRVMPSSFF
     LLLRFFLRID GVLIRMNDTR LYHEADKTYM LREYTSRESK IANLMHVPPS LFTEPNEISQ
     YLPIKEAVCE KLVFPERIDP NPVDSESAPS E