CPB1_CAERE
ID CPB1_CAERE Reviewed; 594 AA.
AC Q6E3C9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
GN Name=cpb-1;
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234;
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).
CC -!- FUNCTION: Cytoplasmic polyadenylation element binding protein that
CC binds to and regulates the translation of specific mRNAs. Essential for
CC progression through meiosis. Involved in spermatogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with fbf-1. {ECO:0000250}.
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DR EMBL; AY589643; AAT72427.1; -; Genomic_DNA.
DR EMBL; AY589593; AAT72410.1; -; mRNA.
DR AlphaFoldDB; Q6E3C9; -.
DR SMR; Q6E3C9; -.
DR STRING; 31234.CRE25597; -.
DR eggNOG; KOG0129; Eukaryota.
DR HOGENOM; CLU_035644_0_0_1; -.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Repeat; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..594
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000081511"
FT DOMAIN 257..364
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 381..452
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 66135 MW; 48C9FF66C418DC06 CRC64;
MQHQVKACGD SKSTTRSLQG NRRSGAASLK KPSGNGTFLA TDVTNLDMNS SFLSKKLKRN
GNPVIGMNIQ SSNAFLGAQL AANNFNFAQQ LNHAALYNNL EFQMAVASGD VPSLMSMPAH
KPSLSVSSID PSMDMSQFTE ELNAIQNMSY SPMMPSSAAL QSIFAANDSS AISPYMNLQK
TSLLPTSTLR VSGARKNRIV EVKTLNDRMV IVSIDPQATA STRPNIIPLN RPLMSVAQNC
IDMTKKRPLS AEALYSRKVF IGGLPIDVAE EEVWATFGAF GKVLVDWPRR PEHNNGRGGD
NMYEVEMGRR NLRSVSGYVF LVFTNERSVQ ELVNACEFYE NKYYLQLSSP TMSDKAVQVR
PWRLSDIDYF CDDSCSVDHR RTVFIGGVPR PTRASDLASS LQDYYGKVSY VGIDIDPELK
YPKGAARVTF ANSQSFVRAI SGRFVQVTHA ETNKRVEIKP YVMEDQHCDE CQGVLCKHNY
APYFCGDSSC LQYYCEACWD RMHYIVCDSR ADHRPMVRTG DQTRILPRPP HHQSSHYSPR
SHQMMNHDSM ESSNQSRGNT SSIISRIVNR NSAASVMDRQ TTKPFAATPA VIGY