NBP1B_XENLA
ID NBP1B_XENLA Reviewed; 791 AA.
AC Q6GQD0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Nuclear cap-binding protein subunit 1-B;
GN Name=ncbp1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in
CC various processes such as pre-mRNA splicing, translation regulation,
CC nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by
CC microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA
CC export from the nucleus, leading to the recruitment of the mRNA export
CC machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3'
CC direction through the nuclear pore. The CBC complex is also involved in
CC mediating U snRNA and intronless mRNAs export from the nucleus. The CBC
CC complex is essential for a pioneer round of mRNA translation, before
CC steady state translation when the CBC complex is replaced by
CC cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA
CC translation mediated by the CBC complex plays a central role in
CC nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs
CC bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex
CC enhances NMD in mRNAs containing at least one exon-junction complex
CC (EJC), promoting the interaction between UPF1 and UPF2. The CBC complex
CC is also involved in 'failsafe' NMD, which is independent of the EJC
CC complex, while it does not participate in Staufen-mediated mRNA decay
CC (SMD). During cell proliferation, the CBC complex is also involved in
CC microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is
CC required for miRNA-mediated RNA interference. The CBC complex also acts
CC as a negative regulator of parn, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly
CC capped RNAs (m7GpppG-capped RNA) but is required to stabilize the
CC movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a
CC high affinity cap-binding state with the cap structure. Associates with
CC NCBP3 to form an alternative cap-binding complex (CBC) which plays a
CC key role in mRNA export. The conventional CBC with NCBP2 binds both
CC small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
CC export from the nucleus whereas the alternative CBC with NCBP3 does not
CC bind snRNA and associates only with mRNA thereby playing a role only in
CC mRNA export (By similarity). {ECO:0000250|UniProtKB:Q09161}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of ncbp1/cbp80 and ncbp2/cbp20 that interacts with
CC m7GpppG-capped RNA. Component of an alternative nuclear cap-binding
CC complex (CBC) composed of ncbp1/cbp80 and ncbp3 (By similarity).
CC {ECO:0000250|UniProtKB:Q09161}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09161}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q09161}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; BC072815; AAH72815.1; -; mRNA.
DR RefSeq; NP_001085472.1; NM_001092003.1.
DR AlphaFoldDB; Q6GQD0; -.
DR SMR; Q6GQD0; -.
DR PRIDE; Q6GQD0; -.
DR DNASU; 443898; -.
DR GeneID; 443898; -.
DR KEGG; xla:443898; -.
DR CTD; 443898; -.
DR Xenbase; XB-GENE-6251717; ncbp1.S.
DR OrthoDB; 270650at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 443898; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000339; F:RNA cap binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027159; CBP80.
DR InterPro; IPR015172; MIF4G-like_typ-1.
DR InterPro; IPR015174; MIF4G-like_typ-2.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR12412; PTHR12412; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF09088; MIF4G_like; 1.
DR Pfam; PF09090; MIF4G_like_2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; mRNA capping; mRNA processing; mRNA splicing;
KW mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing; Translation regulation;
KW Transport.
FT CHAIN 1..791
FT /note="Nuclear cap-binding protein subunit 1-B"
FT /id="PRO_0000239783"
FT DOMAIN 28..240
FT /note="MIF4G"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 641..714
FT /evidence="ECO:0000255"
SQ SEQUENCE 791 AA; 92093 MW; 865824B0D6F1808C CRC64;
MSRRRHSDEN DGGQPHKRRR TSEPLEIEDR LESLICRVGE KSTSSLESNL EGLAGVLEAD
LPNYKNKILR ILCFVARLLP EKMTVYTTLV GLLNARNYNF GGEFVEAMIR HLKETIKLNA
YNEAIYLVRF LCDLVNCHVI AAPSMVAMFE SFVGVTQEED IPQVRSDWYV YAVLSSLPWV
GKELYEKKDV EMDQILSQIE AYLKQRQKLH LSILQVWSAE KPHPQEEYLD CLWAQVQKLK
KDRWQERHIQ RPYLAFDSVL CEALQHNLPP FTPPPHTEDS VYPVPRVIFR MFDYTDAPEG
PVMPGSHSVE RFVIEENLHC ILKSHWRERK TCAAQLLSYP EKNKIPLNYH IVEVIFGELF
QLPSPPQIDV MYTTLLIELC KLQPGSLPQV LAQASEMLYT RLDTMNTTCI DRFINWFSHH
LSNFQFRWNW EDWADCLSQD LDKPKPQFVR EVLEKCMRLS YHQRILDIVP ATFSALYPAN
PSNVIKYGDE SNSALPGYSV AVILTNAIKN KASDKEIFNI LKDIPNPNQD DYDDEGIGFN
PLKIEVFVQT LLNLASKSFS HSFSALAKFH DIFKALSESD EGKLHILRVV YDVWKNHPQM
IAVLLDKMIR TQIVDCAAVA NWIFSPELSP DFTRFYIWEI LHSTIRKMNK HVQKIQKELE
DTKQRLAKQH KHRDSDDNDE DSGRKDGPLE EQIERLQEKV ESAQSEQKNL FLVIFQRFIM
ILTEHLVRCE TGGIDVNTAW YKNCRERLQQ IFLQHHQTIQ QYMVTLENLL FTAELDHHIL
TVFQQFCALQ S
