NCBP3_CHICK
ID NCBP3_CHICK Reviewed; 604 AA.
AC Q5ZM19;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000250|UniProtKB:Q53F19};
GN Name=NCBP3 {ECO:0000250|UniProtKB:Q53F19}; ORFNames=RCJMB04_3g9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719565; CAG31224.1; -; mRNA.
DR RefSeq; NP_001012823.1; NM_001012805.1.
DR AlphaFoldDB; Q5ZM19; -.
DR SMR; Q5ZM19; -.
DR STRING; 9031.ENSGALP00000004171; -.
DR PaxDb; Q5ZM19; -.
DR PRIDE; Q5ZM19; -.
DR GeneID; 417552; -.
DR KEGG; gga:417552; -.
DR CTD; 55421; -.
DR VEuPathDB; HostDB:geneid_417552; -.
DR eggNOG; ENOG502QRX4; Eukaryota.
DR InParanoid; Q5ZM19; -.
DR PhylomeDB; Q5ZM19; -.
DR PRO; PR:Q5ZM19; -.
DR Proteomes; UP000000539; 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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019416; NCBP3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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..604
FT /note="Nuclear cap-binding protein subunit 3"
FT /id="PRO_0000308584"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..177
FT /note="RNA recognition motif (RRM) domain"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT REGION 168..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 145..148
FT /note="WLDD motif; essential for 7-methylguanosine-
FT containing mRNA cap binding"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT COMPBIAS 177..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 68726 MW; 9F08009D6F5E42E4 CRC64;
MAAVRGLRIS VKAEATATTA EPRGPEPEPM EVEEGELETI PVRRSLRELI PDTSRRYENK
AGSFITGIDV TSKEAIEKKE QRAKRFHFRA EVNLAQRNVA LDRDMMKKAI PKVRLDTIYI
CGVDEMSTQD IFAYFKEYPP AHIEWLDDTS CNVVWLDEVT ATRALINMSS FPDQEKPKGG
ENNEEKTAEK NKKEKQEEST DDETEEGEVE DENPSDIELD ALTQVEEDSL LRNDLRPANK
LAKGNKLFMR FATKDDKKEL GAARRSQYYM KYGNPNYGGM KGILSNSWKR RYHSRRIHRD
VIKKRTLIGD DVGLTPPYKH RHSGLVNVPE EPIEEEEEEE EVQDMDEDDR VVVEYRDDLQ
PFKQSRDRGA ARRSSASASD SDEMDYDLEL KMISTPSPKK SMKMTMYADE VESQLKNIRN
SMRADSIATS NVKNRIGSKG LSDKVVDVRL LLEEKRQNNN GLRQPNSIVK SDVRQRLGKR
PHSPEVKPPS SISAPRREPI SDVHSRLGIP KQDVKGLYSD TREKKSGNLW TRLGSAPKTQ
EKTSDKPENS VASPEEDDSE LQRVWGALIK EKGESRQKKS RLDNLPSLQI EISRESSSGS
DTES
