CHSP1_RAT
ID CHSP1_RAT Reviewed; 147 AA.
AC Q9WU49;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Calcium-regulated heat stable protein 1;
DE AltName: Full=Calcium-regulated heat-stable protein of 24 kDa;
DE Short=CRHSP-24;
GN Name=Carhsp1;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=9712905; DOI=10.1074/jbc.273.35.22738;
RA Groblewski G.E., Yoshida M., Bragado M.J., Ernst S.A., Leykam J.,
RA Williams J.A.;
RT "Purification and characterization of a novel physiological substrate for
RT calcineurin in mammalian cells.";
RL J. Biol. Chem. 273:22738-22744(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 DEPHOSPHORYLATION BY CALCINEURIN.
RX PubMed=7515049; DOI=10.1016/s0021-9258(17)36580-8;
RA Groblewski G.E., Wagner A.C., Williams J.A.;
RT "Cyclosporin A inhibits Ca2+/calmodulin-dependent protein phosphatase and
RT secretion in pancreatic acinar cells.";
RL J. Biol. Chem. 269:15111-15117(1994).
RN [4]
RP REGULATION OF PHOSPHORYLATION.
RX PubMed=12801884; DOI=10.1152/ajpgi.00111.2003;
RA Schaefer C., Steffen H., Krzykowski K.J., Goke B., Groblewski G.E.;
RT "CRHSP-24 phosphorylation is regulated by multiple signaling pathways in
RT pancreatic acinar cells.";
RL Am. J. Physiol. 285:G726-G734(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION AT SER-30; SER-32; SER41 AND SER-52, AND DEPHOSPHORYLATION
RP BY CALCINEURIN.
RX PubMed=19477163; DOI=10.1016/j.bbrc.2009.05.096;
RA Lee S., Wishart M.J., Williams J.A.;
RT "Identification of calcineurin regulated phosphorylation sites on CRHSP-
RT 24.";
RL Biochem. Biophys. Res. Commun. 385:413-417(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41 AND
RP SER-52, AND 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: Binds mRNA and regulates the stability of target mRNA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with STYX (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9712905}.
CC Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
CC Note=Detected at cytoplasmic stress granules and P-bodies. Detected at
CC exosome granules where mRNA is degraded (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9712905}.
CC -!- PTM: Can be phosphorylated by DYRK2 (in vitro) (By similarity).
CC Dephosphorylated by calcineurin in a Ca(2+) dependent manner, and
CC probably by PP2A or PP4 serine phosphatases in cAMP- and PKC-mediated
CC pathways. {ECO:0000250, ECO:0000269|PubMed:19477163,
CC ECO:0000269|PubMed:9712905}.
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DR EMBL; AF115346; AAD25022.1; -; mRNA.
DR EMBL; BC071173; AAH71173.1; -; mRNA.
DR RefSeq; NP_690003.1; NM_152790.2.
DR RefSeq; XP_006245812.1; XM_006245750.3.
DR AlphaFoldDB; Q9WU49; -.
DR SMR; Q9WU49; -.
DR STRING; 10116.ENSRNOP00000003514; -.
DR iPTMnet; Q9WU49; -.
DR PhosphoSitePlus; Q9WU49; -.
DR jPOST; Q9WU49; -.
DR PaxDb; Q9WU49; -.
DR PRIDE; Q9WU49; -.
DR Ensembl; ENSRNOT00000003514; ENSRNOP00000003514; ENSRNOG00000002610.
DR GeneID; 260416; -.
DR KEGG; rno:260416; -.
DR UCSC; RGD:708415; rat.
DR CTD; 23589; -.
DR RGD; 708415; Carhsp1.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00390000000022; -.
DR HOGENOM; CLU_139526_1_0_1; -.
DR InParanoid; Q9WU49; -.
DR OMA; THERWED; -.
DR OrthoDB; 1560417at2759; -.
DR PhylomeDB; Q9WU49; -.
DR TreeFam; TF324381; -.
DR PRO; PR:Q9WU49; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002610; Expressed in liver and 19 other tissues.
DR Genevisible; Q9WU49; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT CHAIN 2..147
FT /note="Calcium-regulated heat stable protein 1"
FT /id="PRO_0000100232"
FT DOMAIN 62..129
FT /note="CSD"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19477163,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19477163,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:16641100, ECO:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19477163,
FT ECO:0007744|PubMed:16641100, ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2V2"
SQ SEQUENCE 147 AA; 15906 MW; F0C65FA29A02B573 CRC64;
MSSEPPPPPQ PPTHQTSIGL LDTPRARDRS PSPLRGNVVP SPLPTRRTRT FSATVRASQG
PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK
LQAVEVVITH LAPGTKHETW SGHVISS
