ID   PCBP1_BOVIN             Reviewed;         356 AA.
AC   Q5E9A3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Poly(rC)-binding protein 1;
DE   AltName: Full=Alpha-CP1;
GN   Name=PCBP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC       preferentially to oligo dC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Loosely bound in the nucleus. May shuttle between the nucleus and
CC       the cytoplasm (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated; lowers poly(rC)-binding activity. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT021017; AAX09034.1; -; mRNA.
DR   RefSeq; NP_001015565.1; NM_001015565.1.
DR   AlphaFoldDB; Q5E9A3; -.
DR   SMR; Q5E9A3; -.
DR   IntAct; Q5E9A3; 1.
DR   MINT; Q5E9A3; -.
DR   STRING; 9913.ENSBTAP00000049383; -.
DR   PaxDb; Q5E9A3; -.
DR   PeptideAtlas; Q5E9A3; -.
DR   PRIDE; Q5E9A3; -.
DR   GeneID; 509917; -.
DR   KEGG; bta:509917; -.
DR   CTD; 5093; -.
DR   eggNOG; KOG2190; Eukaryota.
DR   HOGENOM; CLU_022670_0_1_1; -.
DR   InParanoid; Q5E9A3; -.
DR   OrthoDB; 954970at2759; -.
DR   TreeFam; TF318292; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:AgBase.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:AgBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
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; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN           1..356
FT                   /note="Poly(rC)-binding protein 1"
FT                   /id="PRO_0000239138"
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