CPB3_CAERE
ID CPB3_CAERE Reviewed; 766 AA.
AC Q6E3D4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
GN Name=cpb-3;
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.
CC {ECO:0000250}.
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DR EMBL; AY589637; AAT72444.1; -; Genomic_DNA.
DR EMBL; AY589607; AAT72415.1; -; mRNA.
DR RefSeq; XP_003111092.1; XM_003111044.1.
DR AlphaFoldDB; Q6E3D4; -.
DR SMR; Q6E3D4; -.
DR STRING; 31234.CRE03781; -.
DR PRIDE; Q6E3D4; -.
DR EnsemblMetazoa; CRE03781.1; CRE03781.1; WBGene00066597.
DR GeneID; 9810986; -.
DR CTD; 9810986; -.
DR eggNOG; KOG0129; Eukaryota.
DR HOGENOM; CLU_377774_0_0_1; -.
DR OMA; IEMGYLH; -.
DR OrthoDB; 534330at2759; -.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IEA:InterPro.
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.
PE 2: Evidence at transcript level;
KW RNA-binding.
FT CHAIN 1..766
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 3"
FT /id="PRO_0000081519"
FT DOMAIN 310..332
FT /note="RRM"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 85248 MW; 49AED8DB9D544CAF CRC64;
MSQEEVPGEI PGDIAIEKAE NTVQDDVEAK NTSETKKTIP PMLNVEKVDV AAVGEKSPAP
VSVYDLFKKY QKPDVKSDSE DMNIGFDQLT TDEKNGFLRK LQMLTVGNKK TLKVPGESTP
SPASRLLKKF VPSRRPSTEN KSCESPSRFS LFGKSNKKAP ELERPMNGGQ PRKKSARRLN
FGKEIEERTE TDFQNNRVVA AMTREYEKIV TLKGVPVPIN KPPRQQGPRG SLETPTDSPA
KTETSSISKS YGSDYQSSRD RYTSINEDSL TKKRISTPNR GQGLSNRDNA TWHGELPPRD
YTSPTFSRKI FVGGVPWDIT EAALKDSFGE FGSCAVEWPG HEARYRNAQS NTASLNLRNQ
SKYTGQAATG YVYMIFEDER AVASLLHECS QEIGGAGEWY FKIRAQRSKS TEIRQVQIIP
WVTSDSMFCE DESLLEVGIE PKRTVFVGAL HGMMTAQVLH SIMEDCFGSV ECVQLDTDKF
KYPIGSGRVT FREHGAYFKA IEMGYLHVHT SKFRKRVQID PFLESTNCMV CTTELAHCFC
RNRNCFKYYC HTCWAVDHGH GHDGEVHVPV IVPSSASKAF SGPNRRSHLS SNSPSKPASL
MSSSNSQVAH MVSPAYPVLV GAPAQNLSAL YGYIQNSQQM MITPAAVYEP PMTPSPNEMK
RRSFPEFQPQ PTVFFNSTPM MTPQKGVPCS DGSAVPAYYA NSAAFLTPPS SYYNSPSHST
SSNLSPQQPQ QYYGANLYYG YMPQMSYDGG PNQSAMHLPH TPNYQQ