ATRX_CAEEL
ID ATRX_CAEEL Reviewed; 1359 AA.
AC Q9U7E0; O02061;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Transcriptional regulator ATRX homolog;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase xnp-1;
DE AltName: Full=X-linked nuclear protein 1;
GN Name=xnp-1 {ECO:0000312|WormBase:B0041.7};
GN ORFNames=B0041.7 {ECO:0000312|WormBase:B0041.7};
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 [MRNA].
RX PubMed=10433961; DOI=10.1016/s0378-1119(99)00279-6;
RA Villard L., Fontes M., Ewbank J.J.;
RT "Characterization of xnp-1, a Caenorhabditis elegans gene similar to the
RT human XNP/ATR-X gene.";
RL Gene 236:13-19(1999).
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, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-1130.
RX PubMed=15328017; DOI=10.1016/j.ydbio.2004.06.009;
RA Bender A.M., Wells O., Fay D.S.;
RT "lin-35/Rb and xnp-1/ATR-X function redundantly to control somatic gonad
RT development in C. elegans.";
RL Dev. Biol. 273:335-349(2004).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15649460; DOI=10.1016/j.ydbio.2004.10.014;
RA Cardoso C., Couillault C., Mignon-Ravix C., Millet A., Ewbank J.J.,
RA Fontes M., Pujol N.;
RT "XNP-1/ATR-X acts with RB, HP1 and the NuRD complex during larval
RT development in C. elegans.";
RL Dev. Biol. 278:49-59(2005).
CC -!- FUNCTION: Required for embryonic development and gonadogenesis. Also,
CC functions redundantly with the transcriptional repressor lin-35 to
CC regulate somatic gonad development. {ECO:0000269|PubMed:15328017,
CC ECO:0000269|PubMed:15649460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed in most cells during embryonic
CC development (PubMed:15328017, PubMed:15649460). First expressed at
CC around the 100-200 cell stage of embryogenesis (PubMed:15328017,
CC PubMed:15649460). Expression was absent or reduced in intestinal cell
CC lineages during this time. Highly expressed in neuronal cells of the
CC head, ventral nerve cord and tail during the late stages of
CC embryogenesis (PubMed:15328017). Highly expressed in all dividing cells
CC after hatching (PubMed:15649460). Highly expressed in the P lineage
CC during the L1 stage of larval development (PubMed:15649460). During
CC larval development, mainly expressed in the neurons, but there is also
CC high expression in the junctional cells of the spermatheca and uterus,
CC and weak expression in cells of the somatic gonad including the distal
CC tip cells (PubMed:15328017). {ECO:0000269|PubMed:15328017,
CC ECO:0000269|PubMed:15649460}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive with 38% embryonic
CC lethality at 25 degrees Celsius (PubMed:15649460). A large proportion
CC of surviving animals are sterile. Surviving animals also have gonad
CC developmental defects such as defective gonadal arm growth and as a
CC result irregular distal tip cell migration, and 24% of animals had a
CC protruding vulva phenotype (PubMed:15649460). Reduced brood size
CC (PubMed:15328017). Double knockout with lin-35 results in 43% embryonic
CC lethality (PubMed:15328017). Surviving animals develop slowly, are
CC small, sterile and display male and female gonad developmental defects
CC characterized by shorter gonadal arms, fewer germ cells, an everted
CC vulva phenotype, and failed formation of sheath and spermathecal cells
CC (PubMed:15328017). RNAi-mediated knockdown of lin-35 or hpl-2 results
CC in larval arrest at 25 degrees Celsius in an xpn-1 mutant background
CC (PubMed:15649460). {ECO:0000269|PubMed:15328017,
CC ECO:0000269|PubMed:15649460}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF134186; AAD55361.1; -; mRNA.
DR EMBL; FO080106; CCD61253.1; -; Genomic_DNA.
DR PIR; T34036; T34036.
DR RefSeq; NP_001020958.1; NM_001025787.2.
DR AlphaFoldDB; Q9U7E0; -.
DR BioGRID; 37541; 1.
DR STRING; 6239.B0041.7; -.
DR iPTMnet; Q9U7E0; -.
DR EPD; Q9U7E0; -.
DR PaxDb; Q9U7E0; -.
DR PeptideAtlas; Q9U7E0; -.
DR PRIDE; Q9U7E0; -.
DR EnsemblMetazoa; B0041.7.1; B0041.7.1; WBGene00006961.
DR GeneID; 172077; -.
DR KEGG; cel:CELE_B0041.7; -.
DR UCSC; B0041.7; c. elegans.
DR CTD; 172077; -.
DR WormBase; B0041.7; CE17314; WBGene00006961; xnp-1.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR HOGENOM; CLU_000315_11_4_1; -.
DR InParanoid; Q9U7E0; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; Q9U7E0; -.
DR PRO; PR:Q9U7E0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006961; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797; PTHR45797; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1359
FT /note="Transcriptional regulator ATRX homolog"
FT /id="PRO_0000074308"
FT DOMAIN 483..685
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 951..1134
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 636..639
FT /note="DEAH box"
FT COMPBIAS 18..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 1130
FT /note="R->K: In fd2; viable. Gonad morphological defects in
FT a lin-35 RNAi background."
FT /evidence="ECO:0000269|PubMed:15328017"
FT CONFLICT 479
FT /note="C -> F (in Ref. 2; CCD61253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1359 AA; 156193 MW; EB4342547D4F4E64 CRC64;
MRVGVSESED SDGHVIEDED LEMARQIENE RKEKRAQKLK EKREREGKPP PKKRPAKKRK
ASSSEEDDDD EEESPRKSSK KSRKRAKSES ESDESDEEED RKKSKSKKKV DQKKKEKSKK
KRTTSSSEDE DSDEEREQKS KKKSKKTKKQ TSSESSEESE EERKVKKSKK NKEKSVKKRA
ETSEESDEDE KPSKKSKKGL KKKAKSESES ESEDEKEVKK SKKKSKKVVK KESESEDEAP
EKKKTEKRKR SKTSSEESSE SEKSDEEEEE KESSPKPKKK KPLAVKKLSS DEESEESDVE
VLPQKKKRGA VTLISDSEDE KDQKSESEAS DVEEKVSKKK AKKQESSESG SDSSEGSITV
NRKSKKKEKP EKKKKGIIMD SSKLQKETID AERAEKERRK RLEKKQKEFN GIVLEEGEDL
TEMLTGTSSQ RKLKSVVLDP DSSTVDEESK KPVEVHNSLV RILKPHQAHG IQFMYDCACE
SLDRLDTEGS GGILAHCMGL GKTLQVITFL HTVLMHEKIG EKCKRVLVVV PKNVIINWFK
EFQKWLVDND EELDTIDVNE LDSYKTIEDR RRALKAWHSS KTPSVMIIGY DLFRILTVED
DPKKKKPKNR NRRLEKAKED FRKYLQNPGP DMVVCDEAHK LKNDDSALSK CMVKILTKRR
ICLTGTPLQN NLMEYHCMVN FVKPGLLGTK TEFANRFVNI INRGRTKDAS PLEVSFMKRR
CHVLYDHLKK CVDRKDYRVL TEAIPPKQEY VINVRQTERQ CALYNAFLND IVGDSGLSKR
LLPDYHMFSR IWTHPYQLVL HEQRMERERV MREDAEEEAD FIDDGDGSES ESEGSFKSGS
ESDSGKSVVL SSDDEGSSKK KKNGNKPEIK KTAPQKKRKF LNSDDEDEED GEDTAMAILQ
DGIRQSKRLA GEEADLRDTD TPPEYTGWFA RLGLVKEEDR DDFALSNKLI LLVEIIKKCE
EIGDKLLVFS QSLESLTLIK RMLEYMAGTG QWFADGHEAL NAEGEETWSW LEGEDYMTID
GSVQSGKRDA VQTSFNDPLN LRARLMLIST RAGSLGTNMV AANRVIIFDA CWNPSHDTQS
LFRVYRFGQT KPVYIYRFIA QGTMEERIYK RQVTKESTSM RVVDEAQIQR HYLGNDLTEL
YQFTPSTFDP DVEISCAPPK DRLLADVIHK NQHAVVDYIE HDTLFANVED EKLTEQEMKD
AWTDYEKDKS GMPVRAQYAA PPMPGFPNGM IVGQNVQALL QNRMNQGIRV DQMQHDILFK
ELQKMRIKDA GTAVKIVLLR NLLEQILPYI PDEMRGGMSE FNTHFIRLVH ETDRKMETPA
DLLRKSLESF KTVIKMVKMI PTCREPLARM TRDYPYLFA
