SART3_CAEEL
ID SART3_CAEEL Reviewed; 836 AA.
AC Q17430;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Nuclear RNA-binding protein sart-3 {ECO:0000305};
DE AltName: Full=U4/U6 snRNA-associated-splicing factor {ECO:0000305};
GN Name=sart-3 {ECO:0000303|PubMed:25753661, ECO:0000312|WormBase:B0035.12};
GN ORFNames=B0035.12 {ECO:0000312|WormBase:B0035.12};
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|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 [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH USIP-1 AND U6 SNRNA,
RP IDENTIFICATION IN A COMPLEX WITH U4 SNRNP AND U6 SNRNP COMPLEXES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25753661; DOI=10.1093/nar/gkv196;
RA Rueegger S., Miki T.S., Hess D., Grosshans H.;
RT "The ribonucleotidyl transferase USIP-1 acts with SART3 to promote U6 snRNA
RT recycling.";
RL Nucleic Acids Res. 43:3344-3357(2015).
CC -!- FUNCTION: U6 snRNP-binding protein that functions as a recycling factor
CC of the splicing machinery (PubMed:25753661). Promotes the initial
CC reassembly of U4 and U6 snRNPs following their ejection from the
CC spliceosome during its maturation (PubMed:25753661).
CC {ECO:0000269|PubMed:25753661}.
CC -!- SUBUNIT: Forms a complex composed of sart-3, terminal
CC uridylyltransferase usip-1 and U6 snRNA; complex formation is mediated
CC by usip-1 and sart-3 binding to U6 snRNA (PubMed:25753661). Associates
CC with U4 and U6 snRNP complexes, probably by interacting with U4 and U6
CC snRNAs (PubMed:25753661). {ECO:0000269|PubMed:25753661}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000305|PubMed:25753661}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:25753661}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
CC {ECO:0000269|PubMed:25753661}.
CC -!- DISRUPTION PHENOTYPE: Lethal at the young adult stage due to a ruptured
CC vulva (PubMed:25753661). RNAi-mediated knockdown causes a partial
CC reduction in the number of hatched embryos (PubMed:25753661). RNAi-
CC mediated knockdown in a usip-1 (tm1897) mutant background causes
CC complete embryonic lethality (PubMed:25753661).
CC {ECO:0000269|PubMed:25753661}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284604; CAA97405.1; -; Genomic_DNA.
DR PIR; T18650; T18650.
DR RefSeq; NP_502136.1; NM_069735.5.
DR AlphaFoldDB; Q17430; -.
DR SMR; Q17430; -.
DR STRING; 6239.B0035.12.1; -.
DR EPD; Q17430; -.
DR PaxDb; Q17430; -.
DR PeptideAtlas; Q17430; -.
DR EnsemblMetazoa; B0035.12.1; B0035.12.1; WBGene00007111.
DR EnsemblMetazoa; B0035.12.2; B0035.12.2; WBGene00007111.
DR GeneID; 178053; -.
DR KEGG; cel:CELE_B0035.12; -.
DR UCSC; B0035.12.1; c. elegans.
DR CTD; 178053; -.
DR WormBase; B0035.12; CE05167; WBGene00007111; sart-3.
DR eggNOG; KOG0128; Eukaryota.
DR GeneTree; ENSGT00900000141107; -.
DR HOGENOM; CLU_007172_1_1_1; -.
DR InParanoid; Q17430; -.
DR OMA; PRQMYGA; -.
DR OrthoDB; 867827at2759; -.
DR PhylomeDB; Q17430; -.
DR PRO; PR:Q17430; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007111; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0034057; F:RNA strand-exchange activity; IBA:GO_Central.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:WormBase.
DR GO; GO:0097010; P:eukaryotic translation initiation factor 4F complex assembly; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12391; RRM1_SART3; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR008669; LSM_interact.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034217; SART3_RRM1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF05391; Lsm_interact; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00386; HAT; 5.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..836
FT /note="Nuclear RNA-binding protein sart-3"
FT /id="PRO_0000449386"
FT REPEAT 127..163
FT /note="HAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 296..329
FT /note="HAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 331..367
FT /note="HAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 418..451
FT /note="HAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 453..486
FT /note="HAT 5"
FT /evidence="ECO:0000255"
FT DOMAIN 593..668
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 683..760
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 507..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 95487 MW; 999122BF7436C0D2 CRC64;
MSDVDMESGS DDSGMEDLDE EIQKIKQKMI DDSQSVVLAN QLLILLRKNG DFDELDIKRR
QFVEWAPLNP LNWKNWIEDF QNRKPEPSVA EVEEMFEKAL FDENDVTIWV ERAMYAYKVA
NDKNKKEDFK FCRDVCSKAL ENLGTRYDSG GHIWLIFLEY EMSYLKNSMN APDYQRLADQ
VFALFERALH CPTDQLEDVY VLAEQFCTEF KQHHKLEELK KTYNSTMRQK EQLSKFEELI
QQEETKKQGL KQFFDHEKKS GIPSRIKMAH ERLVSELDDD EEAWIAYGAW ADIELKLPQV
AVKVYSRALR HCPYSFVLHQ QALLAFERDR RPNEEIDALW ERARSNVINS AEEGRSLYRT
YAFLLRRRIH LTGSSDYSPM AEVFDEGAAL LREWFSMAWD TTADYRQMQA YFYASLMKNM
DKCRNIWNDI LASGFGRFAG KWIEAVRLER QFGDKENARK YLNKALNSVS DNINEIYMYY
VQFEREEGTL AELDLVLEKV NSQVAHRAIR PQKKVSEKPA PAPKSKQDHI QKRTSGGEPI
VKKVKGDDGG FKAPLPPSNA KSSSAVSSSN ASSTPAPGSF AVQKAAPGTE DARTIFVSNL
DFTTTEDEIR QAIEGVASIR FARKANSDLV HRGFAYVVME NDQKAQQALL KDRVPVKGRP
MFISANDPEK RVGFKFSTTL EKSKVFVRNV HFQATDDELK ALFSKFGTVT SVRRVTHKDG
KPKGIAFVDF DTEASAQKCV ASGDKLMLRE RELEVALSNP PVKKDKSHGK PAAIGASLEE
DGPRKGHAAK LQLVPRAITN KTPQITARLD AMDVSEGTST SQPLSNDQFR KMFMKN
