RAE1_CAEEL
ID RAE1_CAEEL Reviewed; 373 AA.
AC Q93454;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=mRNA export factor rae-1 {ECO:0000312|WormBase:F10G8.3};
DE AltName: Full=Nuclear pore complex protein 17;
DE AltName: Full=Nucleoporin-17;
GN Name=rae-1 {ECO:0000312|WormBase:F10G8.3};
GN Synonyms=npp-17 {ECO:0000312|WormBase:F10G8.3};
GN ORFNames=F10G8.3 {ECO:0000312|WormBase:F10G8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-10; 71-103; 163-196; 200-218; 231-264 AND 302-310,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT MET-1.
RA Bienvenut W.V.;
RL Submitted (SEP-2005) to UniProtKB.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA Galy V., Mattaj I.W., Askjaer P.;
RT "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT of nuclear pore complex size exclusion in vivo.";
RL Mol. Biol. Cell 14:5104-5115(2003).
RN [4]
RP FUNCTION, INTERACTION WITH RPM-1, AND TISSUE SPECIFICITY.
RX PubMed=22357847; DOI=10.1523/jneurosci.2901-11.2012;
RA Grill B., Chen L., Tulgren E.D., Baker S.T., Bienvenut W., Anderson M.,
RA Quadroni M., Jin Y., Garner C.C.;
RT "RAE-1, a novel PHR binding protein, is required for axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL J. Neurosci. 32:2628-2636(2012).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC (PubMed:12937276). NPC components, collectively referred to as
CC nucleoporins (NUPs), can play the role of both NPC structural
CC components and of docking or interaction partners for transiently
CC associated nuclear transport factors (By similarity). It is
CC specifically important for nuclear mRNA export (PubMed:12937276). Has a
CC role in neuronal development, where it acts downstream of rpm-1 to
CC control axon termination and synapse formation in anterior lateral
CC microtubule (ALM) and posterior lateral microtubule (PLM)
CC mechanosensory neurons (PubMed:22357847).
CC {ECO:0000250|UniProtKB:P40066, ECO:0000269|PubMed:12937276,
CC ECO:0000269|PubMed:22357847}.
CC -!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive means
CC of nucleocytoplasmic transport (By similarity). NPCs allow the passive
CC diffusion of ions and small molecules and the active, nuclear transport
CC receptor-mediated bidirectional transport of macromolecules such as
CC proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits
CC across the nuclear envelope (By similarity). Interacts with rpm-1
CC (PubMed:22357847). {ECO:0000250|UniProtKB:P40066,
CC ECO:0000269|PubMed:22357847}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12937276}. Nucleus {ECO:0000269|PubMed:22357847}.
CC Cell projection, axon {ECO:0000269|PubMed:22357847}. Synapse
CC {ECO:0000269|PubMed:22357847}.
CC -!- TISSUE SPECIFICITY: Expressed along the ventral and dorsal nerve cords.
CC {ECO:0000269|PubMed:22357847}.
CC -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
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DR EMBL; Z80216; CAB02280.1; -; Genomic_DNA.
DR PIR; T20723; T20723.
DR RefSeq; NP_492650.1; NM_060249.3.
DR AlphaFoldDB; Q93454; -.
DR SMR; Q93454; -.
DR BioGRID; 38286; 16.
DR IntAct; Q93454; 1.
DR STRING; 6239.F10G8.3.2; -.
DR EPD; Q93454; -.
DR PaxDb; Q93454; -.
DR PeptideAtlas; Q93454; -.
DR EnsemblMetazoa; F10G8.3.1; F10G8.3.1; WBGene00003803.
DR EnsemblMetazoa; F10G8.3.2; F10G8.3.2; WBGene00003803.
DR GeneID; 172864; -.
DR KEGG; cel:CELE_F10G8.3; -.
DR UCSC; F10G8.3.1; c. elegans.
DR CTD; 172864; -.
DR WormBase; F10G8.3; CE09338; WBGene00003803; rae-1.
DR eggNOG; KOG0647; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_1_0_1; -.
DR InParanoid; Q93454; -.
DR OMA; EAMDQSI; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; Q93454; -.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-191859; snRNP Assembly.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR SignaLink; Q93454; -.
DR PRO; PR:Q93454; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003803; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037631; Gle2/RAE1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10971:SF11; PTHR10971:SF11; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Direct protein sequencing; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Synapse; Translocation; Transport; WD repeat.
FT CHAIN 1..373
FT /note="mRNA export factor rae-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000051107"
FT REPEAT 40..82
FT /note="WD 1"
FT REPEAT 87..126
FT /note="WD 2"
FT REPEAT 128..169
FT /note="WD 3"
FT REPEAT 276..315
FT /note="WD 4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 373 AA; 41413 MW; B0B151DB47FC3526 CRC64;
MFGSSGFGNK SMFGGSNIST STTTPAANTT QNDDFLVDGA PEDTIQVIKF SPTPQDKPML
ACGSWDGTIR VWMFNDANTF EGKAQQNIPA PILDIAWIED SSKIFIACAD KEARLWDLAS
NQVAVVGTHD GPVKTCHWIN GNNYQCLMTG SFDKTLRFWD MKNLPNQTQM AQIQLPERVY
AADVLYPMAV VALANKHIKV YNLENGPTEV KDIESQLKFQ IRCISIFKDK SNQNPAGFAL
GSIEGRVAVQ YVDVANPKDN FTFKCHRSAE LVNGFQEIYA VNDICFHPQH GTLVTIGSDG
RYSMWDKDAR TKLKTSEPHP MPLTCCDVHS SGAFLVYALG YDWSRGHEGN TQPGSKIVIH
KCIEDMKPRP TKK
