ID   CSDC2_RAT               Reviewed;         154 AA.
AC   Q63430;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 3.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Cold shock domain-containing protein C2;
DE   AltName: Full=RNA-binding protein PIPPin;
GN   Name=Csdc2; Synonyms=Pippin;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8573167; DOI=10.1006/bbrc.1996.0068;
RA   Castiglia D., Scaturro M., Nastasi T., Cestelli A., di Liegro I.;
RT   "PIPPin, a putative RNA-binding protein specifically expressed in the rat
RT   brain.";
RL   Biochem. Biophys. Res. Commun. 218:390-394(1996).
RN   [2]
RP   FUNCTION.
RX   PubMed=10446180; DOI=10.1074/jbc.274.34.24087;
RA   Nastasi T., Scaturro M., Bellafiore M., Raimondi L., Beccari S.,
RA   Cestelli A., di Liegro I.;
RT   "PIPPin is a brain-specific protein that contains a cold-shock domain and
RT   binds specifically to H1 degrees and H3.3 mRNAs.";
RL   J. Biol. Chem. 274:24087-24093(1999).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10923677; DOI=10.1097/00001756-200007140-00034;
RA   Nastasi T., Muzi P., Beccari S., Bellafiore M., Dolo V., Bologna M.,
RA   Cestelli A., di Liegro I.;
RT   "Specific neurons of brain cortex and cerebellum are PIPPin positive.";
RL   NeuroReport 11:2233-2236(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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: RNA-binding factor which binds specifically to the very 3'-
CC       UTR ends of both histone H1 and H3.3 mRNAs, encompassing the
CC       polyadenylation signal. Might play a central role in the negative
CC       regulation of histone variant synthesis in the developing brain.
CC       {ECO:0000269|PubMed:10446180}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=PIPPin-RNA complexes are
CC       located to the nucleus.
CC   -!- TISSUE SPECIFICITY: Brain-specific. Expression restricted to the
CC       pyramidal neurons of the cerebral cortex and in the Purkinje cells of
CC       the cerebellum. {ECO:0000269|PubMed:10923677}.
CC   -!- DEVELOPMENTAL STAGE: At E18 dpc, expressed in the cerebellum.
CC       {ECO:0000269|PubMed:10923677}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA62001.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X89962; CAA62001.2; ALT_INIT; mRNA.
DR   PIR; JC4588; JC4588.
DR   RefSeq; NP_001164013.1; NM_001170542.1.
DR   AlphaFoldDB; Q63430; -.
DR   SMR; Q63430; -.
DR   STRING; 10116.ENSRNOP00000007091; -.
DR   iPTMnet; Q63430; -.
DR   PhosphoSitePlus; Q63430; -.
DR   PaxDb; Q63430; -.
DR   Ensembl; ENSRNOT00000007091; ENSRNOP00000007091; ENSRNOG00000005332.
DR   GeneID; 266600; -.
DR   KEGG; rno:266600; -.
DR   UCSC; RGD:628780; rat.
DR   CTD; 27254; -.
DR   RGD; 628780; Csdc2.
DR   eggNOG; KOG3070; Eukaryota.
DR   GeneTree; ENSGT00390000000022; -.
DR   HOGENOM; CLU_139526_1_0_1; -.
DR   InParanoid; Q63430; -.
DR   OMA; PVWPIFP; -.
DR   OrthoDB; 1560417at2759; -.
DR   PhylomeDB; Q63430; -.
DR   TreeFam; TF324381; -.
DR   PRO; PR:Q63430; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000005332; Expressed in cerebellum and 18 other tissues.
DR   Genevisible; Q63430; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IDA:RGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
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   Cytoplasm; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..154
FT                   /note="Cold shock domain-containing protein C2"
FT                   /id="PRO_0000100353"
FT   DOMAIN          69..136
FT                   /note="CSD"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   154 AA;  16877 MW;  5827AC90328BF613 CRC64;
     MTSESTSPPV VPPLHSPKSP VWPTFPFHRE SSRIWERGGG VSPRDLPSPL PTKRTRTYSA
     TARASAGPVF KGVCKQFSRS QGHGFITPEN GSEDIFVHVS DIEGEYVPVE GDEVTYKMCP
     IPPKNQKFQA VEVVLTQLAP HTPHETWSGQ VVGS