NXF3_HUMAN
ID NXF3_HUMAN Reviewed; 531 AA.
AC Q9H4D5; B4DYS7; Q5H9I1; Q9H1A9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Nuclear RNA export factor 3;
DE AltName: Full=TAP-like protein 3;
DE Short=TAPL-3;
GN Name=NXF3; Synonyms=TAPL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11073998; DOI=10.1128/mcb.20.23.8996-9008.2000;
RA Herold A., Suyama M., Rodrigues J.P., Braun I.C., Kutay U.,
RA Carmo-Fonseca M., Bork P., Izaurralde E.;
RT "TAP (NXF1) belongs to a multigene family of putative RNA export factors
RT with a conserved modular architecture.";
RL Mol. Cell. Biol. 20:8996-9008(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS.
RC TISSUE=Testis;
RX PubMed=11545741; DOI=10.1016/s1097-2765(01)00303-3;
RA Yang J., Bogerd H.P., Wang P.J., Page D.C., Cullen B.R.;
RT "Two closely related human nuclear export factors utilize entirely distinct
RT export pathways.";
RL Mol. Cell 8:397-406(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-531 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11566096; DOI=10.1016/s0960-9822(01)00419-5;
RA Jun L., Frints S., Duhamel H., Herold A., Abad-Rodrigues J., Dotti C.,
RA Izaurralde E., Marynen P., Froyen G.;
RT "NXF5, a novel member of the nuclear RNA export factor family, is lost in a
RT male patient with a syndromic form of mental retardation.";
RL Curr. Biol. 11:1381-1391(2001).
CC -!- FUNCTION: May function as a tissue-specific nuclear mRNA export factor.
CC -!- SUBUNIT: Interacts with NXT1, NXT2, E1B-AP5 and CRM1 nuclear export
CC factor.
CC -!- INTERACTION:
CC Q9H4D5; Q9UKK6: NXT1; NbExp=16; IntAct=EBI-750038, EBI-301889;
CC Q9H4D5; Q9NPJ8: NXT2; NbExp=8; IntAct=EBI-750038, EBI-752122;
CC Q9H4D5; Q9NPJ8-3: NXT2; NbExp=9; IntAct=EBI-750038, EBI-10698339;
CC Q9H4D5; P12757: SKIL; NbExp=3; IntAct=EBI-750038, EBI-2902468;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4D5-2; Sequence=VSP_057068, VSP_057069, VSP_057070;
CC -!- TISSUE SPECIFICITY: Expressed at high level in testis and at low level
CC in a small number of tissues.
CC -!- DOMAIN: Lacks C-terminal domain that mediates direct interactions with
CC nucleoporins.
CC -!- DOMAIN: Contains a novel CRM1-dependent nuclear export signal that
CC compensates in cis for the loss of the nuclear pore targeting domain.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC20434.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ277527; CAC16589.1; -; mRNA.
DR EMBL; AF346619; AAL07564.1; -; mRNA.
DR EMBL; AK302586; BAG63839.1; -; mRNA.
DR EMBL; Z75746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471190; EAW54722.1; -; Genomic_DNA.
DR EMBL; BC031616; AAH31616.1; -; mRNA.
DR EMBL; AJ277660; CAC20434.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14503.1; -. [Q9H4D5-1]
DR RefSeq; NP_071335.1; NM_022052.1. [Q9H4D5-1]
DR AlphaFoldDB; Q9H4D5; -.
DR SMR; Q9H4D5; -.
DR BioGRID; 121025; 8.
DR ComplexPortal; CPX-2436; mRNA nuclear export factor complex, NXF3-NXT1.
DR ComplexPortal; CPX-2612; mRNA nuclear export factor NXF3-NXT2.
DR IntAct; Q9H4D5; 3.
DR MINT; Q9H4D5; -.
DR STRING; 9606.ENSP00000378504; -.
DR iPTMnet; Q9H4D5; -.
DR PhosphoSitePlus; Q9H4D5; -.
DR BioMuta; NXF3; -.
DR DMDM; 20455187; -.
DR EPD; Q9H4D5; -.
DR MassIVE; Q9H4D5; -.
DR PaxDb; Q9H4D5; -.
DR PeptideAtlas; Q9H4D5; -.
DR PRIDE; Q9H4D5; -.
DR ProteomicsDB; 80824; -. [Q9H4D5-1]
DR Antibodypedia; 526; 189 antibodies from 31 providers.
DR DNASU; 56000; -.
DR Ensembl; ENST00000395065.8; ENSP00000378504.3; ENSG00000147206.17. [Q9H4D5-1]
DR GeneID; 56000; -.
DR KEGG; hsa:56000; -.
DR MANE-Select; ENST00000395065.8; ENSP00000378504.3; NM_022052.2; NP_071335.1.
DR UCSC; uc004eju.5; human. [Q9H4D5-1]
DR CTD; 56000; -.
DR DisGeNET; 56000; -.
DR GeneCards; NXF3; -.
DR HGNC; HGNC:8073; NXF3.
DR HPA; ENSG00000147206; Tissue enhanced (fallopian tube, testis).
DR MIM; 300316; gene.
DR neXtProt; NX_Q9H4D5; -.
DR OpenTargets; ENSG00000147206; -.
DR PharmGKB; PA31860; -.
DR VEuPathDB; HostDB:ENSG00000147206; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_011280_2_1_1; -.
DR InParanoid; Q9H4D5; -.
DR OMA; MQAHFFV; -.
DR OrthoDB; 1051093at2759; -.
DR PhylomeDB; Q9H4D5; -.
DR TreeFam; TF314566; -.
DR PathwayCommons; Q9H4D5; -.
DR SignaLink; Q9H4D5; -.
DR BioGRID-ORCS; 56000; 18 hits in 699 CRISPR screens.
DR ChiTaRS; NXF3; human.
DR GenomeRNAi; 56000; -.
DR Pharos; Q9H4D5; Tbio.
DR PRO; PR:Q9H4D5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9H4D5; protein.
DR Bgee; ENSG00000147206; Expressed in right uterine tube and 106 other tissues.
DR ExpressionAtlas; Q9H4D5; baseline and differential.
DR Genevisible; Q9H4D5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0042272; C:nuclear RNA export factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR CDD; cd00780; NTF2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR030216; NXF3.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR015245; Tap_RNA-bd.
DR PANTHER; PTHR10662; PTHR10662; 1.
DR PANTHER; PTHR10662:SF12; PTHR10662:SF12; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF09162; Tap-RNA_bind; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA transport; Nucleus;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..531
FT /note="Nuclear RNA export factor 3"
FT /id="PRO_0000220534"
FT DOMAIN 113..192
FT /note="RRM"
FT DOMAIN 344..494
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT REGION 33..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057068"
FT VAR_SEQ 297..322
FT /note="NSILELFPKLLCLDGQQSPRATLCGT -> KSVVPSVTTWDPDLCLIAPFCR
FT RRQH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057069"
FT VAR_SEQ 323..531
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057070"
FT VARIANT 186
FT /note="N -> I (in dbSNP:rs2301387)"
FT /id="VAR_050419"
FT MUTAGEN 300
FT /note="L->R: Inactivates CRM1 binding; when associated with
FT R-302."
FT /evidence="ECO:0000269|PubMed:11545741"
FT MUTAGEN 302
FT /note="L->R: Inactivates CRM1 binding; when associated with
FT R-300."
FT /evidence="ECO:0000269|PubMed:11545741"
SQ SEQUENCE 531 AA; 60102 MW; 3A47C7D35FC396B9 CRC64;
MSLPSGHTTG HTDQVVQRRA RCWDIYQRRF SSRSEPVNPG MHSSSHQQQD GDAAMHGAHM
DSPVRYTPYT ISPYNRKGSF RKQDQTHVNM EREQKPPERR MEGNMPDGTL GSWFKITVPF
GIKYNEKWLL NLIQNECSVP FVPVEFHYEN MHASFFVENA SIAYALKNVS GKIWDEDNEK
ISIFVNPAGI PHFVHRELKS EKVEQIKLAM NQQCDVSQEA LDIQRLPFYP DMVNRDTKMA
SNPRKCMAAS LDVHEENIPT VMSAGEMDKW KGIEPGEKCA DRSPVCTTFS DTSSNINSIL
ELFPKLLCLD GQQSPRATLC GTEAHKRLPT CKGSFFGSEM LKNLVLQFLQ QYYLIYDSGD
RQGLLSAYHD EACFSLSIPF NPEDSAPSSF CKFFKDSRNI KILKDPYLRG ELLKHTKLDI
VDSLSALPKT QHDLSSFLVD MWYQTEWMLC FSVNGVFKEV EGQSQGSVLA FTRTFIATPG
SSSSLCIVND KLFVRDTSHQ GTQSALFTLV PTAFSSSVPA FSQEQQKMLP S
