NCBP1_SALSA
ID NCBP1_SALSA Reviewed; 796 AA.
AC C0H906;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Nuclear cap-binding protein subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=CBP80;
DE Short=NCBP 80 kDa subunit;
GN Name=ncbp1; Synonyms=cbp80;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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; BT058812; ACN10525.1; -; mRNA.
DR RefSeq; NP_001158814.1; NM_001165342.1.
DR AlphaFoldDB; C0H906; -.
DR SMR; C0H906; -.
DR STRING; 8030.ENSSSAP00000016077; -.
DR PRIDE; C0H906; -.
DR GeneID; 100306803; -.
DR KEGG; sasa:100306803; -.
DR CTD; 100306803; -.
DR OMA; TMQLECI; -.
DR OrthoDB; 270650at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Bgee; ENSSSAG00000007681; Expressed in testis and 14 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-mediated gene silencing; Translation regulation; Transport.
FT CHAIN 1..796
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385229"
FT DOMAIN 28..240
FT /note="MIF4G"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 641..719
FT /evidence="ECO:0000255"
FT COMPBIAS 664..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 92376 MW; 9DCD338A69C56425 CRC64;
MSRRRHSDGD DGGQSHKRRR TSEPVEIEDR LESLICRVGE KSTSSLESNL EGLAGVLEAD
LPNYKNKILR ILCAVARLLP EKLTVYTTLV GLLNARNYNF GGEFVEAMIR QLKETLKANL
YTDALYLVRF LCDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRSDWFV YAVLSSLPWV
GKELDEKKDV EMDRLLNQID GYLKRRLKTH VPMLQVWTAE KPHPQEEYLD CLYAQIQKLK
KDRWQERHIL RPYIAFDSVL CEALQHNLPP FTPPAHMPDC QYPMPRVIFR MFDYTDAPEG
PVMPGSHSVE RFVIEDNLHN IIKSHWKERK TCAAQLLSYP GKNKIPLNYH IVEVIFGELF
QLPCPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMMYV RLDTMNTICI DRLLNWFSHH
LSNFQFRWSW DDWVDCLALD ADKPKPKFVK EVLEKCMRLS YHQRIVDIVP PTFSGLIPAD
PIFFYKYQDE ANSALPGYAV AIAVGNAIKN RASNEEILTV LKDVPNPNQE DDDDEGEGFN
PLKIEVFLQT LLHLAAKSFS HSFSALAKFH EILKALTDCD EGKLHILRVV YEVWKNHPQM
VSVLVDKLIR TQIVDCAAVA NWLFSPSMAH EFTRFYVWEI LHSTIRKMNK HVQKIQKELE
EAKDKLERQQ HKKQKDSGDE EDMEKNSEDE DGQLEEQIER LQEKVESAQS EQKNLFLVIF
QRFIMMLTEH LVRCETGSVD FSTPWYKNCI ERLQQIFLMH HVTIQQYMGT LENLLFTAEL
DHHILAVYQQ FCALQL
