NASP1_CAEEL
ID NASP1_CAEEL Reviewed; 382 AA.
AC Q17886;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein NASP homolog 1 {ECO:0000305};
GN Name=nasp-1 {ECO:0000312|WormBase:C09H10.6};
GN ORFNames=C09H10.6 {ECO:0000312|WormBase:C09H10.6};
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, AND INTERACTION WITH TRA-4 AND HDA-1.
RX PubMed=17011494; DOI=10.1016/j.devcel.2006.07.015;
RA Grote P., Conradt B.;
RT "The PLZF-like protein TRA-4 cooperates with the Gli-like transcription
RT factor TRA-1 to promote female development in C. elegans.";
RL Dev. Cell 11:561-573(2006).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-53 AND ASP-307.
RX PubMed=23918784; DOI=10.1128/iai.00700-13;
RA Iatsenko I., Sinha A., Roedelsperger C., Sommer R.J.;
RT "New role for DCR-1/dicer in Caenorhabditis elegans innate immunity against
RT the highly virulent bacterium Bacillus thuringiensis DB27.";
RL Infect. Immun. 81:3942-3957(2013).
CC -!- FUNCTION: Promotes normal hermaphrodite (XX) development, in concert
CC with zinc finger protein tra-4 and histone deacetylase hda-1, perhaps
CC as components of a complex (PubMed:17011494). May act redundantly with
CC nasp-2 (PubMed:17011494). Involved in innate immune response to
CC B.thuringiensis strain DB27 and S.aureus bacteria (PubMed:23918784).
CC May play a role in the uptake or spreading of dsRNA (PubMed:23918784).
CC {ECO:0000269|PubMed:17011494, ECO:0000269|PubMed:23918784}.
CC -!- SUBUNIT: May interact with zinc finger protein tra-4 and histone
CC deacetylase hda-1. {ECO:0000269|PubMed:17011494}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown by injection leads to
CC strong resistance to B. thuringiensis-mediated killing.
CC {ECO:0000269|PubMed:23918784}.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90441.1; -; Genomic_DNA.
DR PIR; T19166; T19166.
DR RefSeq; NP_496380.1; NM_063979.5.
DR AlphaFoldDB; Q17886; -.
DR SMR; Q17886; -.
DR DIP; DIP-24701N; -.
DR IntAct; Q17886; 2.
DR STRING; 6239.C09H10.6; -.
DR EPD; Q17886; -.
DR PaxDb; Q17886; -.
DR PeptideAtlas; Q17886; -.
DR EnsemblMetazoa; C09H10.6.1; C09H10.6.1; WBGene00007500.
DR GeneID; 174697; -.
DR KEGG; cel:CELE_C09H10.6; -.
DR UCSC; C09H10.6; c. elegans.
DR CTD; 174697; -.
DR WormBase; C09H10.6; CE03007; WBGene00007500; nasp-1.
DR eggNOG; KOG4563; Eukaryota.
DR GeneTree; ENSGT00390000016650; -.
DR HOGENOM; CLU_010162_2_0_1; -.
DR InParanoid; Q17886; -.
DR OMA; QTYILMA; -.
DR OrthoDB; 1176629at2759; -.
DR PhylomeDB; Q17886; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007500; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Immunity; Innate immunity; Nucleus; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..382
FT /note="Protein NASP homolog 1"
FT /id="PRO_0000452696"
FT REPEAT 42..75
FT /note="TPR 1"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 191..224
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 233..266
FT /note="TPR 3"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..304
FT /evidence="ECO:0000255"
FT COMPBIAS 103..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53
FT /note="L->S: In tu439; strong resistance to
FT B.thuringiensis-mediated killing. Resistant to infection by
FT S.aureus. Reduced life span. RNAi-mediated knockdown of
FT pmk-1 (by injection) abolishes resistance to
FT B.thuringiensis. Deficient for RNAi-mediated knockdown by
FT feeding; in association with N-307."
FT /evidence="ECO:0000269|PubMed:23918784"
FT MUTAGEN 307
FT /note="D->N: In tu439; strong resistance to B.
FT thuringiensis-mediated killing. Resistant to infection by
FT S.aureus. Reduced life span. RNAi-mediated knockdown of
FT pmk-1 (by injection) abolishes resistance to
FT B.thuringiensis. Deficient for RNAi-mediated knockdown by
FT feeding; in association with S-53."
FT /evidence="ECO:0000269|PubMed:23918784"
SQ SEQUENCE 382 AA; 42213 MW; 149EDD9232895A19 CRC64;
MDTENIADAS DIRVKDASGD SDEKGNGTTT EEETVEQKEK RLAELLAAGR RALKVNDIDK
ASDSLSEATE LSSEIYGENH ENTFDSLYYY GMATLELAKE ESQLLKGPGE KESGDEEQAG
NSDDKTDEEN GETEKEDGEE SGEEEDDDDD TMKLSWEILE TARCIAAAKI EALEAEQSGI
SAIEEWNLKL ADVLVLLGEH GISDGKYTQA FEDLDRALNI QRNVLPPSSR KIAQTYILIG
NACASDANYD ETVQYFGKTK DVLIARQTEL KHELERGVDD KEKKSEFENE LKELEEMMPG
VEEMIADAVH SAAQVEETKK AIKAQFEGFT QVLAKLPQEA GDQKEANDIS SLVRRPAKRA
VDAPTDNQAV KKEKEEEGTT SI
