ID   NBP1A_XENLA             Reviewed;         791 AA.
AC   Q6GQ80;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Nuclear cap-binding protein subunit 1-A;
GN   Name=ncbp1-a;
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=Ovary;
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; BC072867; AAH72867.1; -; mRNA.
DR   RefSeq; NP_001085510.1; NM_001092041.1.
DR   AlphaFoldDB; Q6GQ80; -.
DR   SMR; Q6GQ80; -.
DR   BioGRID; 102099; 1.
DR   IntAct; Q6GQ80; 1.
DR   MaxQB; Q6GQ80; -.
DR   DNASU; 443936; -.
DR   GeneID; 443936; -.
DR   KEGG; xla:443936; -.
DR   CTD; 443936; -.
DR   Xenbase; XB-GENE-5841293; ncbp1.L.
DR   OMA; QPFKIPF; -.
DR   OrthoDB; 270650at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 443936; Expressed in blastula 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-A"
FT                   /id="PRO_0000239782"
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;  91979 MW;  282C08A424697838 CRC64;
     MSRRRHSDEN DGGQAHKRRK TSEPLEIEDR LESLICRVGE KSTSSLESNL EGLAGVLEAD
     LPNYKSKILR ILCFVARLLP EKMSVYSTLV GLLNARNYNF GGEFVEAMIR HLKETIKLNA
     YSEAVYLVRF LSDLVNCHVI AAPSMVAMFE SFVGVTQEED IPQVRSDWYV YAVLSSLPWV
     GKELYEKKDV EMDRILSQIE AYLKQRQKLH VSILQVWSAE KPHPQEEYLD CLWAQIQKLK
     KDRWQERHIL RPYLAFDSVL CEALQHNLPP FTPPPHTEDS VYPVPRVVFR MFDYTDAPEG
     PVMPGSHSVE RFVIEENLHC ILKSHWRERK TCAAQLLSYP EKNKIPLNYH IVEVIFGELF
     QLPTPPHIDV MYTTLLIELC KLQPGSLPQV LAQASEMLYT RLDTMNTICI DRFINWFSHH
     LSNFQFRWNW EDWADCLSQD LNKPKPQFVR EVLEKCMRLS YHQRILDIVP ATFSALYPAS
     PSCVFKYGDE SNSALPGYSV AVTLTNEIKN KASDKEIFNI LKDIPNPNQD DDDDEGISFN
     PLKIEVFVQS LLNLASKSFS HAFSALAKFH DIFKALSESD EGKLHILRVA YDVWKNHPQM
     IAVLVDKMIR TQIVDCAAVA NWIFSPELSH DFTRFYIWEI LHSTIRKMNK HVQKIQKELE
     ETKQRLAKQH KHRDSDDNDE DSGRKDGPLE EQIERLQEKV ESAQSEQKNL FLVIFQRFIM
     ILTEHLVRCE TGAIDVNTAW YKNCRERLQQ IFLQHHQTIQ QYMVTLENLL FTAELDHHIL
     TVFQQFCALQ S