ID   NCBP3_XENLA             Reviewed;         618 AA.
AC   Q6DE94;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000250|UniProtKB:Q53F19};
GN   Name=ncbp3 {ECO:0000250|UniProtKB:Q53F19};
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 (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC077240; AAH77240.1; -; mRNA.
DR   RefSeq; NP_001086653.1; NM_001093184.1.
DR   AlphaFoldDB; Q6DE94; -.
DR   SMR; Q6DE94; -.
DR   PRIDE; Q6DE94; -.
DR   DNASU; 446488; -.
DR   GeneID; 446488; -.
DR   KEGG; xla:446488; -.
DR   CTD; 446488; -.
DR   Xenbase; XB-GENE-5831162; ncbp3.L.
DR   OrthoDB; 535499at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 446488; Expressed in blastula and 19 other tissues.
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: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..618
FT                   /note="Nuclear cap-binding protein subunit 3"
FT                   /id="PRO_0000308586"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..178
FT                   /note="RNA recognition motif (RRM) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q53F19"
FT   REGION          170..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           146..149
FT                   /note="WLDD motif; essential for 7-methylguanosine-
FT                   containing mRNA cap binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q53F19"
FT   COMPBIAS        175..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..220
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..366
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..569
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  69741 MW;  CBC26F98FDB211D6 CRC64;
     MAAVRGLRVS VKAGGGAEPE PMEVEEGEVE AAAGRTSPVE ATADQTSPRE VVPGSDRRYE
     NRAGTFITGI DVTSKEAIEK KEQRAKRFHF RAEVSDDQRN VVLDREMMRK VPKVRLETLY
     ICGVDEMSTQ DIFAFFKQYP PGYIEWLDDS SCNVVWLDEV TASRALLNLS SKPTNEKGQR
     KKDGEHRSAR SKKDRLDDSP QSSGDETEEG EVEEDNPNDA EVETENKSEN PPETLSQAEQ
     ASILKNDLRP SIKTVKGNRL YMRFATKDDK KEHGAASKSQ YYMKYGNPNY GGMKGILSNS
     WKKRYHSRRI QRDVIKKRTF IGDDVGLTPT YKHHHSGLVN VPEEPIEEEE EEEEEEEEDM
     DEDDRVVEYR DELQAFKRER EGARRCAASN SDSDEMDYDL ELKMISTPSP KKSMKMTMYA
     DEVESQLKTI RHSMRSDSAG NSVKSRIGSK SHSEKPADVR LILEEKRQST ASRQQSSSSG
     KSDVRQRLGK RAHSPEIRKT LSIAPTSRRE PLSDVHSRLG LPKQPEGKGL YSDSKEKKTG
     SLWNRLGTAP KEKDRASEKS GEKSQAAPEE EDSALQQAWG ALIKEKEQIR QKKSRLDNLP
     SLQIEISRES SSGSDTDS