RBM8A_CAEEL
ID RBM8A_CAEEL Reviewed; 142 AA.
AC Q21832;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=RNA-binding protein rnp-4 {ECO:0000305};
DE AltName: Full=RNA-binding protein 8A {ECO:0000255|RuleBase:RU361239};
DE AltName: Full=RNA-binding protein Y14 {ECO:0000250|UniProtKB:Q9Y5S9};
DE AltName: Full=Ribonucleoprotein rnp-4 {ECO:0000305};
GN Name=rnp-4 {ECO:0000312|WormBase:R07E5.14};
GN Synonyms=RBM8 {ECO:0000312|EMBL:AHX83804.1},
GN Y14 {ECO:0000312|EMBL:AHX83804.1};
GN ORFNames=R07E5.14 {ECO:0000312|WormBase:R07E5.14};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AHX83804.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=24416299; DOI=10.1371/journal.pone.0084842;
RA Gong P., Zhao M., He C.;
RT "Slow co-evolution of the MAGO and Y14 protein families is required for the
RT maintenance of their obligate heterodimerization mode.";
RL PLoS ONE 9:E84842-E84842(2014).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP INTERACTION WITH RSR-1.
RX PubMed=12944400; DOI=10.1074/jbc.m306856200;
RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
RT "An evolutionarily conserved role for SRm160 in 3'-end processing that
RT functions independently of exon junction complex formation.";
RL J. Biol. Chem. 278:44153-44160(2003).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MAG-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=14706697; DOI=10.1016/j.mod.2003.11.003;
RA Kawano T., Kataoka N., Dreyfuss G., Sakamoto H.;
RT "Ce-Y14 and MAG-1, components of the exon-exon junction complex, are
RT required for embryogenesis and germline sexual switching in Caenorhabditis
RT elegans.";
RL Mech. Dev. 121:27-35(2004).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE EXON JUNCTION COMPLEX, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23149939; DOI=10.1128/mcb.01298-12;
RA Shiimori M., Inoue K., Sakamoto H.;
RT "A specific set of exon junction complex subunits is required for the
RT nuclear retention of unspliced RNAs in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 33:444-456(2013).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30279189; DOI=10.1534/g3.118.200744;
RA Gauvin T.J., Han B., Sun M.J., Griffin E.E.;
RT "PIE-1 Translation in the Germline Lineage Contributes to PIE-1 Asymmetry
RT in the Early Caenorhabditis elegans Embryo.";
RL G3 (Bethesda) 8:3791-3801(2018).
CC -!- FUNCTION: RNA-binding protein which binds to pre-mRNA, spliced mRNA and
CC spliceosomal snRNAs (PubMed:14706697, PubMed:23149939). Preferentially
CC binds to the spliceosomal snRNP U2 (PubMed:23149939). Core component of
CC the splicing-dependent multiprotein exon junction complex (EJC)
CC deposited at splice junctions on mRNAs (By similarity). Positively
CC regulates the nuclear export of spliced mRNAs including the sex
CC determination gene tra-2 (PubMed:23149939). Promotes oogenesis by
CC repressing germline masculinization and spermatogenesis
CC (PubMed:14706697). Required for embryonic development, possibly through
CC positively regulating the expression of pie-1 (PubMed:14706697,
CC PubMed:30279189). Not required for the spatial patterning of pie-1 in
CC embryos (PubMed:30279189). {ECO:0000255|RuleBase:RU361239,
CC ECO:0000269|PubMed:14706697, ECO:0000269|PubMed:23149939,
CC ECO:0000269|PubMed:30279189}.
CC -!- SUBUNIT: Heterodimer with mag-1/MAGOH (PubMed:14706697). Part of the
CC mRNA splicing-dependent exon junction complex (EJC) complex; the core
CC complex contains CASC3, EIF4A3, mag-1/MAGOH and rnp-4/RBM8A (Probable).
CC Interacts with rsr-1/SRm160 (PubMed:12944400).
CC {ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14706697,
CC ECO:0000305|PubMed:23149939}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14706697}. Nucleus
CC {ECO:0000269|PubMed:14706697}. Nucleus speckle
CC {ECO:0000255|RuleBase:RU361239}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic cells and germline cells.
CC {ECO:0000269|PubMed:14706697}.
CC -!- DEVELOPMENTAL STAGE: First expressed in 20-30 cell stage embryos and
CC expression continues through to adulthood.
CC {ECO:0000269|PubMed:14706697}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality due to developmental arrest during morphogenesis
CC (PubMed:30279189). RNAi-mediated knockdown at the L1 larval stage
CC results in increased sperm production and no oocyte production
CC (PubMed:14706697). RNAi-mediated knockdown at the L1 larval stage
CC results in the accumulation of unspliced mRNAs including ama-1 and ife-
CC 4 in the cytoplasm, and specifically in the production of an irregular
CC unspliced form of the sex determining protein tra-2, which accumulates
CC in the cytoplasm and inhibits the regular tra-2 isoforms a and c
CC reducing their expression and disrupting their nuclear localization
CC (PubMed:23149939). RNAi-mediated knockdown in L4 hermaphrodite larvae
CC results in 90% embryonic lethality with embryos exhibiting elongation
CC defects (PubMed:14706697). RNAi-mediated knockdown reduces the
CC expression of pie-1 in P2 blastomeres (PubMed:30279189). RNAi-mediated
CC knockdown together with nxf-2 RNAi results in severe growth
CC retardation, lethality and reduced accumulation of unspliced tra-2 in
CC the cytoplasm (PubMed:23149939). RNAi-mediated knockdown together with
CC ire-1 RNAi restores fertility, reduces the accumulation of unspliced
CC tra-2 in the cytoplasm and suppresses germ line masculinization of the
CC single rnp-4 RNAi mutant (PubMed:23149939).
CC {ECO:0000269|PubMed:14706697, ECO:0000269|PubMed:23149939,
CC ECO:0000269|PubMed:30279189}.
CC -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
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DR EMBL; KF051018; AHX83804.1; -; mRNA.
DR EMBL; BX284603; CAA83626.1; -; Genomic_DNA.
DR PIR; F88427; F88427.
DR RefSeq; NP_497891.1; NM_065490.4.
DR AlphaFoldDB; Q21832; -.
DR SMR; Q21832; -.
DR DIP; DIP-26500N; -.
DR IntAct; Q21832; 1.
DR STRING; 6239.R07E5.14.1; -.
DR EPD; Q21832; -.
DR PaxDb; Q21832; -.
DR PeptideAtlas; Q21832; -.
DR EnsemblMetazoa; R07E5.14.1; R07E5.14.1; WBGene00004387.
DR EnsemblMetazoa; R07E5.14.2; R07E5.14.2; WBGene00004387.
DR UCSC; R07E5.14.2; c. elegans.
DR WormBase; R07E5.14; CE01044; WBGene00004387; rnp-4.
DR eggNOG; KOG0130; Eukaryota.
DR GeneTree; ENSGT00730000111185; -.
DR HOGENOM; CLU_012062_18_1_1; -.
DR InParanoid; Q21832; -.
DR OMA; NVKVDWC; -.
DR OrthoDB; 1444995at2759; -.
DR PhylomeDB; Q21832; -.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004387; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0040022; P:feminization of hermaphroditic germ-line; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:1905881; P:positive regulation of oogenesis; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd12324; RRM_RBM8; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR008111; RNA-bd_8.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033744; RRM_RBM8.
DR PANTHER; PTHR45894; PTHR45894; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR01738; RNABINDINGM8.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..142
FT /note="RNA-binding protein rnp-4"
FT /id="PRO_0000453360"
FT DOMAIN 55..133
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 142 AA; 16114 MW; 4A7B461EDAB18B76 CRC64;
MSDNEVEMED VVANAERSRG RGLAQSRNRE RITYDVVDEE SSATSGAPQR SVEGWIVFVT
NIHEEATEDD VHDKFSEYGK IKNIHLNLDR RTGFLKGYAL VEYETQKEAN EAIDQSNDTD
LLGQNVKVDW CFVKGKKTSG KR
