ID   CPB2_CAEBR              Reviewed;         566 AA.
AC   Q6E3F3; A8WTZ3; Q620Z3;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cytoplasmic polyadenylation element-binding protein 2;
GN   Name=cpb-2; ORFNames=CBG02588;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=15231741; DOI=10.1101/gr.2639304;
RA   Cho S., Jin S.W., Cohen A., Ellis R.E.;
RT   "A phylogeny of Caenorhabditis reveals frequent loss of introns during
RT   nematode evolution.";
RL   Genome Res. 14:1207-1220(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Cytoplasmic polyadenylation element binding protein that
CC       binds to and regulates the translation of specific mRNAs.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP23955.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY589618; AAT72419.1; -; Genomic_DNA.
DR   EMBL; AY589611; AAT72448.1; -; mRNA.
DR   EMBL; HE601438; CAP23955.3; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q6E3F3; -.
DR   SMR; Q6E3F3; -.
DR   STRING; 6238.CBG02588; -.
DR   EnsemblMetazoa; CBG02588a.1; CBG02588a.1; WBGene00025614.
DR   WormBase; CBG02588a; CBP30367; WBGene00025614; Cbr-cpb-2.
DR   eggNOG; KOG0129; Eukaryota.
DR   HOGENOM; CLU_034584_0_0_1; -.
DR   InParanoid; Q6E3F3; -.
DR   OrthoDB; 1075356at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR   GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 4.10.640.40; -; 1.
DR   InterPro; IPR032296; CEBP_ZZ.
DR   InterPro; IPR038446; CEBP_ZZ_sf.
DR   InterPro; IPR034819; CPEB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR12566; PTHR12566; 1.
DR   Pfam; PF16366; CEBP_ZZ; 1.
DR   Pfam; PF16367; RRM_7; 2.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..566
FT                   /note="Cytoplasmic polyadenylation element-binding protein
FT                   2"
FT                   /id="PRO_0000081512"
FT   DOMAIN          430..512
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          17..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..98
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  65464 MW;  6FA75BDD4332FE00 CRC64;
     MSKSRRVFLS IQGDDDFWGN GDQLEGKTLS SIKQQESKKM DDSVEGMEEE KYFFRQSKLG
     RQNLERLHEK EEQECEEERL DWSEKVDSEE EEEDIQEQDE IITEGKETEM FDSGPETDQK
     MPVDPNEGFY NNYRSYFSGR PEMLFLIRSI DESATDYYEK PFIDLYETTR KRLEMYPNTE
     LNQILRCACN PNAGGGADYR VRNKHAVVVS NFREPDRRLG RYSKYYYHHN VGPEVYSRKV
     FVGGLPACVK EMDILHFFSR YGRLQVDWPS KHYGCKSDSD PSVYNEPSFT PPTSHLGLSS
     PPFGQINPFM TDCPPAPSDL QMSRHGSVDG GGGGFPTHGM SMRNIGFGGG SGPRSTGEGE
     KKQQHLGYVF LLFEKERSVR DLVTECFEEE EGLFIILESA IEPIRVQIRP WLLADAEFLM
     DFNVPINTKM VAFIGGVPRP LKAVELAHFF EQTYGNVVCV GIDIDNKFKY PRGSGRVAFS
     NYHAYVQAIT DRYIVLDHED IHKRVEIKPY FFHNQSCEEC SSRYHRQYAP FFCPSLECFQ
     YYCEPCWHKM HARPSRFHHM PVVKGI