ID   NCBP3_XENTR             Reviewed;         611 AA.
AC   Q6DFQ2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000250|UniProtKB:Q53F19};
GN   Name=ncbp3 {ECO:0000250|UniProtKB:Q53F19};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC076682; AAH76682.1; -; mRNA.
DR   RefSeq; NP_001005015.1; NM_001005015.1.
DR   AlphaFoldDB; Q6DFQ2; -.
DR   STRING; 8364.ENSXETP00000028410; -.
DR   DNASU; 448518; -.
DR   GeneID; 448518; -.
DR   KEGG; xtr:448518; -.
DR   CTD; 55421; -.
DR   Xenbase; XB-GENE-5831122; ncbp3.
DR   eggNOG; ENOG502QRX4; Eukaryota.
DR   InParanoid; Q6DFQ2; -.
DR   OrthoDB; 535499at2759; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; 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..611
FT                   /note="Nuclear cap-binding protein subunit 3"
FT                   /id="PRO_0000308587"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..169
FT                   /note="RNA recognition motif (RRM) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q53F19"
FT   REGION          159..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           137..140
FT                   /note="WLDD motif; essential for 7-methylguanosine-
FT                   containing mRNA cap binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q53F19"
FT   COMPBIAS        167..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  69124 MW;  159229E5C66D15AA CRC64;
     MAAVRGLRVS VKAGGGAEPE PMEVEEGEVE AAADRASPRE VVSGSNRRYE NRAGTFITGI
     DVTSKEAIEK KEQRAKRFHF RAEVSDQQRN VVLDREMIRK AIPKVRLETL YVYGVDDMST
     EDIFAFFKQY PPGYIEWLDD SSCNVVWLDE VTPSRALLNL SSMPTNEKGQ RKKDGEHSSA
     RSKKDRLDDS PLSSGDETEE GEVEEDNPSE AEDEDETETE KKSVNPPDTL SEAEQASLLK
     NELRPSSKPV KGNSLYMRFA TKDDKKELGA ARRSQYYMKY GNPNYGGMKG ILSNSWKRRY
     HSRRLQRDVI KKSTFIGDDV EITPTYKHLH SGLVNVPEEP IEEEEEEEEE EEDMDEDDRV
     VVEYRDELQA FKREREGARR SAASNSDSDE MDYDLELKMI STPSPKKSMK MTMYADEVES
     QLKTIRNSMR SDSVGNSVKS RIGSKSHAEK PADVRLILEE KRQSTASRQQ SSSGKSDVRQ
     RLGKRPHSPE IRKTLSIAPT SRREPLSDVH SRLGLPKQLE GKGLYSDSKE KKTGSLWNRL
     GTAPKDKERP SEKSEKSPAA PEEEDSVLQQ AWGALIKEKE QIRQKKSRLD NLPSLQIEIS
     RESSSGSDTD S