NCBP3_DANRE
ID NCBP3_DANRE Reviewed; 694 AA.
AC Q803E1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000250|UniProtKB:Q53F19};
GN Name=ncbp3 {ECO:0000250|UniProtKB:Q53F19}; ORFNames=zgc:55870;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap-
CC binding complex (CBC) which plays a key role in mRNA export. NCBP3
CC serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA)
CC to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both
CC small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
CC export from the nucleus, the alternative CBC with NCBP3 does not bind
CC snRNA and associates only with mRNA thereby playing a role in only mRNA
CC export. {ECO:0000250|UniProtKB:Q53F19}.
CC -!- SUBUNIT: Component of an alternative cap-binding complex (CBC) composed
CC of NCBP1/CBP80 and NCBP3. {ECO:0000250|UniProtKB:Q53F19}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53F19}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q53F19}.
CC -!- SIMILARITY: Belongs to the NCBP3 family. {ECO:0000305}.
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DR EMBL; BC044520; AAH44520.1; -; mRNA.
DR RefSeq; NP_956437.1; NM_200143.1.
DR AlphaFoldDB; Q803E1; -.
DR SMR; Q803E1; -.
DR STRING; 7955.ENSDARP00000065503; -.
DR PaxDb; Q803E1; -.
DR PRIDE; Q803E1; -.
DR GeneID; 393112; -.
DR KEGG; dre:393112; -.
DR CTD; 55421; -.
DR ZFIN; ZDB-GENE-040426-826; ncbp3.
DR eggNOG; ENOG502QRX4; Eukaryota.
DR InParanoid; Q803E1; -.
DR OrthoDB; 535499at2759; -.
DR PhylomeDB; Q803E1; -.
DR PRO; PR:Q803E1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR019416; NCBP3.
DR PANTHER; PTHR16291; PTHR16291; 1.
DR Pfam; PF10309; NCBP3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA capping; mRNA processing; mRNA transport; Nucleus;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..694
FT /note="Nuclear cap-binding protein subunit 3"
FT /id="PRO_0000308585"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..187
FT /note="RNA recognition motif (RRM) domain"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT REGION 183..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..158
FT /note="WLDD motif; essential for 7-methylguanosine-
FT containing mRNA cap binding"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT COMPBIAS 12..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 78338 MW; FCCF38B755073D40 CRC64;
MAAVRSLRVS VKSDSASDRS ESDSESDSDR DAREAEPMEV EEGEVELESI PVRRSLKELL
PDTSRRYENK AGTFITGIDV TSKEAIEKKE KRARRFHFRA EENLTQKDVV LERDLLKKMI
PKVRLEALHM SGVDDMSTQD VFGYFKEYPP AHIEWIDDAS CNVVWLDDIT STRALINLSR
MPDKEEVTNT DSSKPSELPV QTQKARRSRG SDDDDDDDEE EEGEVDDDDD DDEEDEKARD
IEDETEKKPQ ETRETSLSQA ERDSLLQNEP RPTVKPFKGN KLFLRFATHD DKKELGAARR
SRYYMKYGNP NYGGMKGILS NSWKRRYHTR RIQRDILKTK KPLIGDSMGH TPPYTHRHSA
DLVNLPEEPI EEEEEEEEDG EEDMDADDRV VEYKDRGEKE RGPRLVEGGL RSRLGGPSPT
SSDSDEMDYD LELKMISTPS PKKSMKMTMY ADEVETNLRS LRNSIRTESS GSVKSRIGGG
GGGGSGGAVE GRGEGGSSKS TSEKVTDVRQ LLEEKRQGLS QQRSRPPVAT SGKTDVRQRL
GKRPHSPERR RSVSPVISRK TASRREPLSD VRSRLGVAKH DNRSLFSEPP KDKKTGGLWS
RLGPSHKDSG SGDEDKPSSR ASSSRGIRRR KDEDSDGVED EDEEDDSHLQ KMWGAMIKQK
EQQSNKMKKS RLDNLPSLQI EISRDGSNGS DSDS
