NCBP3_MOUSE
ID NCBP3_MOUSE Reviewed; 615 AA.
AC Q8BZR9; Q3TNF4; Q3TQ96; Q4G0C3; Q8BMB1; Q9CRM6; Q9CS93; Q9D0G9; Q9DBT0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000250|UniProtKB:Q53F19};
GN Name=Ncbp3 {ECO:0000250|UniProtKB:Q53F19};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cecum, Head, Lung, Spleen, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Trophoblast stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
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. The alternative CBC is particularly important in cellular
CC stress situations such as virus infections and the NCBP3 activity is
CC critical to inhibit virus growth (PubMed:26382858).
CC {ECO:0000269|PubMed:26382858}.
CC -!- SUBUNIT: Component of an alternative cap-binding complex (CBC) composed
CC of NCBP1/CBP80 and NCBP3. Interacts with SRRT, KPNA3, THOC5 and EIF4A3.
CC {ECO:0000250|UniProtKB:Q53F19}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53F19}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q53F19}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BZR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZR9-2; Sequence=VSP_029001, VSP_029002;
CC Name=3;
CC IsoId=Q8BZR9-3; Sequence=VSP_029000, VSP_029003;
CC -!- SIMILARITY: Belongs to the NCBP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27625.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28111.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK004766; BAB23546.2; -; mRNA.
DR EMBL; AK011450; BAB27625.1; ALT_INIT; mRNA.
DR EMBL; AK033682; BAC28428.1; -; mRNA.
DR EMBL; AK017496; BAB30775.2; -; mRNA.
DR EMBL; AK020130; BAB32004.1; -; mRNA.
DR EMBL; AK032983; BAC28111.1; ALT_INIT; mRNA.
DR EMBL; AK163780; BAE37488.1; -; mRNA.
DR EMBL; AK153152; BAE31762.1; -; mRNA.
DR EMBL; AK153241; BAE31833.1; -; mRNA.
DR EMBL; AK165317; BAE38135.1; -; mRNA.
DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098495; AAH98495.1; -; mRNA.
DR EMBL; BC118943; AAI18944.1; -; mRNA.
DR CCDS; CCDS24994.1; -. [Q8BZR9-1]
DR RefSeq; NP_080094.3; NM_025818.3. [Q8BZR9-1]
DR AlphaFoldDB; Q8BZR9; -.
DR BioGRID; 211780; 7.
DR ComplexPortal; CPX-3661; Alternative nuclear cap-binding complex.
DR STRING; 10090.ENSMUSP00000021135; -.
DR iPTMnet; Q8BZR9; -.
DR PhosphoSitePlus; Q8BZR9; -.
DR EPD; Q8BZR9; -.
DR jPOST; Q8BZR9; -.
DR MaxQB; Q8BZR9; -.
DR PaxDb; Q8BZR9; -.
DR PeptideAtlas; Q8BZR9; -.
DR PRIDE; Q8BZR9; -.
DR ProteomicsDB; 286155; -. [Q8BZR9-1]
DR ProteomicsDB; 286156; -. [Q8BZR9-2]
DR ProteomicsDB; 286157; -. [Q8BZR9-3]
DR Antibodypedia; 64617; 43 antibodies from 13 providers.
DR DNASU; 66874; -.
DR Ensembl; ENSMUST00000021135; ENSMUSP00000021135; ENSMUSG00000020783. [Q8BZR9-1]
DR GeneID; 66874; -.
DR KEGG; mmu:66874; -.
DR UCSC; uc007jzu.2; mouse. [Q8BZR9-3]
DR UCSC; uc007jzv.2; mouse. [Q8BZR9-1]
DR CTD; 55421; -.
DR MGI; MGI:1914124; Ncbp3.
DR VEuPathDB; HostDB:ENSMUSG00000020783; -.
DR eggNOG; ENOG502QRX4; Eukaryota.
DR GeneTree; ENSGT00390000005712; -.
DR HOGENOM; CLU_488838_0_0_1; -.
DR InParanoid; Q8BZR9; -.
DR OMA; DANEDKS; -.
DR OrthoDB; 535499at2759; -.
DR PhylomeDB; Q8BZR9; -.
DR TreeFam; TF331339; -.
DR BioGRID-ORCS; 66874; 6 hits in 40 CRISPR screens.
DR ChiTaRS; Ncbp3; mouse.
DR PRO; PR:Q8BZR9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BZR9; protein.
DR Bgee; ENSMUSG00000020783; Expressed in rostral migratory stream and 244 other tissues.
DR Genevisible; Q8BZR9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISO:MGI.
DR GO; GO:0005846; C:nuclear cap binding complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006408; P:snRNA export from nucleus; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; Isopeptide bond;
KW mRNA capping; mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transport; Ubl conjugation.
FT CHAIN 1..615
FT /note="Nuclear cap-binding protein subunit 3"
FT /id="PRO_0000308583"
FT REGION 15..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..187
FT /note="RNA recognition motif (RRM) domain"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT REGION 182..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..158
FT /note="WLDD motif; essential for 7-methylguanosine-
FT containing mRNA cap binding"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT COMPBIAS 187..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53F19"
FT VAR_SEQ 119..161
FT /note="AIPKVRLETIYICGVDEMSTQDIFSYFKEYPPAHIEWLDDTSC -> GTVCL
FT GEIFHPGSRVTFPAVVSRSFWLCPVCPVVIQIPKRKGF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029000"
FT VAR_SEQ 119..121
FT /note="AIP -> VVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029001"
FT VAR_SEQ 122..615
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029002"
FT VAR_SEQ 162..615
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029003"
FT CONFLICT 73
FT /note="S -> I (in Ref. 1; BAB30775)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="K -> E (in Ref. 3; AAH98495)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="R -> S (in Ref. 1; BAB27625)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="K -> Q (in Ref. 1; BAB23546)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="K -> Q (in Ref. 1; BAB23546)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="S -> R (in Ref. 1; BAB27625)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="R -> K (in Ref. 1; BAB27625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 70043 MW; 67033DB16255889F CRC64;
MAAVRGLRVS VKAEAPAGPA LGLPSPEVES GLERGEPEPM EVEEGELEIV PVRRSLKELL
PDTSRRYENK AGSFITGIDV TSKEAIEKKE QRAKRFHFRA EVNLAQRNVA LDRDMMKKAI
PKVRLETIYI CGVDEMSTQD IFSYFKEYPP AHIEWLDDTS CNVVWLDEMT ATRALINMSS
LPAQDKMRSR DASEDKSSEK NKKDKQEDSS DDDETEEGEV EDENSSDVEL DTLSQVEEES
LLRNDLRPAN KLAKGNRLFM RFATKDDKKE LGAARRSQYY MKYGNPNYGG MKGILSNSWK
RRYHSRRIQR DVIKKRALIG DDVGLTSYKH RHSGLVNVPE EPIEEEEEEE EEEEDQDMDA
DDRVVVEYHE ELPGLKQPRE RSLSRRSSAS SSDSDEMDYD LELKMISTPS PKKSMKMTMY
ADEVESQLKS IRNPMRADSI STSNIKNRIG NKLPPEKFAD VRHLLDEKRQ HSCPRPAVSS
TKPDIRQRLG KRPYSPEKAF SSNQVVRREP SSDVHSRLGV PRQDVKGLYS DTRERKSGGL
WTRLGSTPKT KEKNTKKVDH RASGAEEDDS ELQRAWGALI KEKEESRQKK SRLDSLPSLQ
IEVSRESSSG SEAES
