CPB3_CAEJA
ID CPB3_CAEJA Reviewed; 734 AA.
AC Q6E3D2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
GN Name=cpb-3;
OS Caenorhabditis japonica.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=281687;
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; AY589640; AAT72446.1; -; Genomic_DNA.
DR EMBL; AY589639; AAT72446.1; JOINED; Genomic_DNA.
DR EMBL; AY589609; AAT72417.1; -; mRNA.
DR AlphaFoldDB; Q6E3D2; -.
DR SMR; Q6E3D2; -.
DR STRING; 281687.CJA17238; -.
DR eggNOG; KOG0129; Eukaryota.
DR HOGENOM; CLU_377774_0_0_1; -.
DR InParanoid; Q6E3D2; -.
DR Proteomes; UP000005237; Unassembled WGS sequence.
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 SUPFAM; SSF54928; SSF54928; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; RNA-binding.
FT CHAIN 1..734
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 3"
FT /id="PRO_0000081518"
FT DOMAIN 294..316
FT /note="RRM"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 81196 MW; C6FF719F44B310F9 CRC64;
MDRNDDSAPV QAAAEPAEHP GDEKSGKRNV PPALKLVENV VATGEKSPAP ASVYDLFKKY
HKGEKNGEEN VNVNVGFDQL SSDEKSGFLR KLQMLTVGSK KKDGESSQSP AGRLLKKFVP
SRRTTPTASA STAKTTSPSR FSVFGRSAKK VSESFSSQKP IHRKQSARRL QFTEKENPQP
DAARNKVVAA MTREYEKLSK ECAPVPINNK PARVQMQIPR GSLETPTDSP VKSFSSTTTS
SSPEKEREKE KEKIEQPRYG TTQRQSVNSQ QSSASWHGEL PPRDYTSPTF SRKIFVGGVP
WDITEAALKD SFGEFGSCAV EWPGQEARYR SGQSNVMPPN ANLRAHSKYS GQATTGYVYM
IFEDERAVAA LLHECSQEIG GAGEWYFKIR AQRSKSTEIR QVQIIPWVTS DSLYCHEESI
LEVGIEPKRT VFVGALHGMM TAQVLHSIME DCFGCVECVQ LDTDKFKYPI GSGRVTFREH
GAYFKAIEIG YLHVHTSKFR KRVQIDPFLE STSCMVCNLE PAHCFCRNRN CFKYYCHSCW
SIDHGKDTVV DVHVPVIVPS SATKAYQGHA SRHSHLSSNS PSKARDGQNS NNSQFSQLLS
PAFPMIVGAP TPTLSALYGY IQNNHTMSPT VYDGPLTPPS SETMSKRGSR EFSSNSNGGP
VFISPAPVLS SQKLETPIPS YFANSTAILT PTSTYYGSPS TQQTYYAPNV YYGYMPQPIP
YDGYVCPPPA NYTQ