ID   PCBP1_RABIT             Reviewed;         356 AA.
AC   O19048;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Poly(rC)-binding protein 1;
DE   AltName: Full=Alpha-CP1;
DE   AltName: Full=Heterogeneous nuclear ribonucleoprotein E1;
DE            Short=hnRNP E1;
GN   Name=PCBP1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10101190; DOI=10.1093/nar/27.8.1828;
RA   Thiele B.J., Berger M., Huth A., Reimann I., Schwarz K., Thiele H.;
RT   "Tissue-specific translational regulation of alternative rabbit 15-
RT   lipoxygenase mRNAs differing in their 3'-untranslated regions.";
RL   Nucleic Acids Res. 27:1828-1836(1999).
CC   -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC       preferentially to oligo dC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; AJ003023; CAA05814.1; -; mRNA.
DR   RefSeq; NP_001075593.1; NM_001082124.1.
DR   AlphaFoldDB; O19048; -.
DR   SMR; O19048; -.
DR   STRING; 9986.ENSOCUP00000020092; -.
DR   PRIDE; O19048; -.
DR   Ensembl; ENSOCUT00000003633; ENSOCUP00000020092; ENSOCUG00000003634.
DR   GeneID; 100008848; -.
DR   KEGG; ocu:100008848; -.
DR   CTD; 5093; -.
DR   eggNOG; KOG2190; Eukaryota.
DR   GeneTree; ENSGT00940000161582; -.
DR   HOGENOM; CLU_022670_0_1_1; -.
DR   InParanoid; O19048; -.
DR   OMA; GQDRCGD; -.
DR   OrthoDB; 954970at2759; -.
DR   TreeFam; TF318292; -.
DR   Proteomes; UP000001811; Chromosome 2.
DR   Bgee; ENSOCUG00000003634; Expressed in embryo and 15 other tissues.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0098847; F:sequence-specific single stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:Ensembl.
DR   Gene3D; 3.30.1370.10; -; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; SSF54791; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN           1..356
FT                   /note="Poly(rC)-binding protein 1"
FT                   /id="PRO_0000050089"
FT   DOMAIN          13..75
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          97..162
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          279..343
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60335"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15365"
SQ   SEQUENCE   356 AA;  37498 MW;  6D1A261276CA206D CRC64;
     MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT
     LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI
     KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT
     IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ
     VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA
     NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS