ID   RNP1_CAEEL              Reviewed;         305 AA.
AC   Q10667;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=RNA-binding protein rnp-1;
GN   Name=rnp-1 {ECO:0000312|WormBase:ZK863.7a};
GN   ORFNames=ZK863.7 {ECO:0000312|WormBase:ZK863.7a};
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Bristol N2;
RX   PubMed=7588066; DOI=10.1242/dev.121.10.3323;
RA   Hsu D.R., Chuang P.-T., Meyer B.J.;
RT   "DPY-30, a nuclear protein essential early in embryogenesis for
RT   Caenorhabditis elegans dosage compensation.";
RL   Development 121:3323-3334(1995).
RN   [2]
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   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25261697; DOI=10.1534/genetics.114.168823;
RA   Spike C.A., Coetzee D., Nishi Y., Guven-Ozkan T., Oldenbroek M.,
RA   Yamamoto I., Lin R., Greenstein D.;
RT   "Translational control of the oogenic program by components of OMA
RT   ribonucleoprotein particles in Caenorhabditis elegans.";
RL   Genetics 198:1513-1533(2014).
CC   -!- FUNCTION: RNA-binding protein that is required for the germ line to
CC       transition from spermatogenesis to oogenesis and allow for normal
CC       oocyte development. {ECO:0000269|PubMed:25261697}.
CC   -!- TISSUE SPECIFICITY: Expressed throughout the germline.
CC       {ECO:0000269|PubMed:25261697}.
CC   -!- DISRUPTION PHENOTYPE: Hermaphrodites are sterile and produce no oocytes
CC       due to the failure of the germ line to transition from spermatogenesis
CC       to oogenesis during oocyte development. {ECO:0000269|PubMed:25261697}.
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DR   EMBL; U21302; AAA92287.1; -; Genomic_DNA.
DR   EMBL; Z78019; CAB01455.1; -; Genomic_DNA.
DR   PIR; T28063; T28063.
DR   RefSeq; NP_001256408.1; NM_001269479.1.
DR   AlphaFoldDB; Q10667; -.
DR   SMR; Q10667; -.
DR   BioGRID; 44695; 6.
DR   DIP; DIP-24668N; -.
DR   IntAct; Q10667; 5.
DR   STRING; 6239.ZK863.7a; -.
DR   EPD; Q10667; -.
DR   PaxDb; Q10667; -.
DR   PeptideAtlas; Q10667; -.
DR   EnsemblMetazoa; ZK863.7a.1; ZK863.7a.1; WBGene00004384.
DR   GeneID; 179672; -.
DR   KEGG; cel:CELE_ZK863.7; -.
DR   UCSC; ZK863.7; c. elegans.
DR   CTD; 179672; -.
DR   WormBase; ZK863.7a; CE15447; WBGene00004384; rnp-1.
DR   eggNOG; KOG0109; Eukaryota.
DR   GeneTree; ENSGT00940000172179; -.
DR   HOGENOM; CLU_922053_0_0_1; -.
DR   InParanoid; Q10667; -.
DR   OMA; TKYFYFR; -.
DR   OrthoDB; 1244727at2759; -.
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-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-CEL-72187; mRNA 3'-end processing.
DR   Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR   PRO; PR:Q10667; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00004384; Expressed in embryo and 4 other tissues.
DR   ExpressionAtlas; Q10667; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0048600; P:oocyte fate commitment; IMP:UniProtKB.
DR   GO; GO:0060282; P:positive regulation of oocyte development; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..305
FT                   /note="RNA-binding protein rnp-1"
FT                   /id="PRO_0000081809"
FT   DOMAIN          3..72
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         84..97
FT                   /note="CCHC-type"
FT   REGION          284..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33049 MW;  20C19544E58FBA2F CRC64;
     MPSKLFVGNL PDNVDSNKLK QVFQPFCKVT ECDIVKNYAF VHIEEDDVDP IITRLTGYTI
     DGKVVNIKKS TSKLRPTPGM PNRCFRCQSD EHRTPQCPQD PTNNQKTENG VQTLKFDLTS
     GAGVKRSAGD PIIDSAKRIA YGAQSVVEPE IPQPMDPDLQ ALYQEYQLSR QRYVYYRDRL
     LKEMEAKQHG STAGFALSSS STVPVPVASA PPGATQLSAA PVSYQPNAPP VIASINAPYA
     VASNLRAPYA LQSAPYASAA SAPYGSVTPA GAPSNVMTTQ QYLQQIQHQQ ATGSPAPVPA
     PPRLY