GLH4_CAEEL
ID GLH4_CAEEL Reviewed; 1156 AA.
AC O76743; O44758;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent RNA helicase glh-4;
DE EC=3.6.4.13;
DE AltName: Full=Germline helicase 4;
GN Name=glh-4 {ECO:0000312|WormBase:T12F5.3};
GN ORFNames=T12F5.3 {ECO:0000312|WormBase:T12F5.3};
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].
RC STRAIN=Bristol N2;
RX PubMed=10851135; DOI=10.1242/dev.127.13.2907;
RA Kuznicki K.A., Smith P.A., Leung-Chiu W.M., Estevez A.O., Scott H.C.,
RA Bennett K.L.;
RT "Combinatorial RNA interference indicates GLH-4 can compensate for GLH-1;
RT these two P granule components are critical for fertility in C. elegans.";
RL Development 127:2907-2916(2000).
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 INTERACTION WITH KGB-1.
RX PubMed=12435362; DOI=10.1006/dbio.2002.0832;
RA Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K.,
RA Gressman-Coberly E., Mutapcic L., Bennett K.;
RT "The GLH proteins, Caenorhabditis elegans P granule components, associate
RT with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a
RT predicted cytoskeletal protein.";
RL Dev. Biol. 251:333-347(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21402787; DOI=10.1083/jcb.201010106;
RA Hanazawa M., Yonetani M., Sugimoto A.;
RT "PGL proteins self associate and bind RNPs to mediate germ granule assembly
RT in C. elegans.";
RL J. Cell Biol. 192:929-937(2011).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24746798; DOI=10.1016/j.cub.2014.03.015;
RA Updike D.L., Knutson A.K., Egelhofer T.A., Campbell A.C., Strome S.;
RT "Germ-granule components prevent somatic development in the C. elegans
RT germline.";
RL Curr. Biol. 24:970-975(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27650246; DOI=10.1038/srep33884;
RA Al-Amin M., Min H., Shim Y.H., Kawasaki I.;
RT "Somatically expressed germ-granule components, PGL-1 and PGL-3, repress
RT programmed cell death in C. elegans.";
RL Sci. Rep. 6:33884-33884(2016).
CC -!- FUNCTION: Probable ATP-binding RNA helicase. May act redundantly with
CC the P-granule component glh-1 to regulate the formation of the granular
CC structure of P-granules in embryos (PubMed:21402787, PubMed:24746798).
CC May protect somatic cells from excessive apoptosis during normal
CC development (PubMed:27650246). {ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246, ECO:0000305}.
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=3.6.4.13;
CC -!- SUBUNIT: Interacts (via C-terminus) with kgb-1.
CC {ECO:0000269|PubMed:12435362}.
CC -!- DEVELOPMENTAL STAGE: During germline proliferation.
CC -!- DISRUPTION PHENOTYPE: Knockout with RNAi-mediated knockdown of glh-1
CC results in smaller P-granules and irregular cytoplasmic localization of
CC the P-granule component pgl-3 in embryos (PubMed:21402787). Quadruple
CC RNAi-mediated knockdown with glh-1, pgl-1 and pgl-3 results in
CC offspring that display 27-89% sterility, abnormal oocytes and do not
CC have embryos in the uterus (PubMed:24746798). These sterile offspring
CC still produce sperm (PubMed:24746798). Furthermore, these offspring may
CC have compromised P-granule integrity as there is diffuse cytoplasmic
CC localization of the P-granule component deps-1, which may cause germ
CC cells to initiate somatic reprogramming (PubMed:24746798). RNAi-
CC mediated knockdown in a double ced-1 and hpl-2 mutant background
CC rescues the reduced somatic cell apoptotic cell defect in the ced-1 and
CC hpl-2 double knockout (PubMed:27650246). {ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF079508; AAC28387.1; -; mRNA.
DR EMBL; FO081191; CCD69784.1; -; Genomic_DNA.
DR PIR; T32759; T32759.
DR PIR; T43326; T43326.
DR RefSeq; NP_491207.3; NM_058806.4.
DR AlphaFoldDB; O76743; -.
DR SMR; O76743; -.
DR BioGRID; 37415; 1.
DR IntAct; O76743; 1.
DR STRING; 6239.T12F5.3.1; -.
DR iPTMnet; O76743; -.
DR EPD; O76743; -.
DR PaxDb; O76743; -.
DR PeptideAtlas; O76743; -.
DR PRIDE; O76743; -.
DR EnsemblMetazoa; T12F5.3.1; T12F5.3.1; WBGene00001601.
DR GeneID; 171941; -.
DR KEGG; cel:CELE_T12F5.3; -.
DR UCSC; T12F5.3.1; c. elegans.
DR CTD; 171941; -.
DR WormBase; T12F5.3; CE29052; WBGene00001601; glh-4.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_008559_0_0_1; -.
DR InParanoid; O76743; -.
DR OMA; FPTKETS; -.
DR OrthoDB; 1670303at2759; -.
DR SignaLink; O76743; -.
DR PRO; PR:O76743; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001601; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008432; F:JUN kinase binding; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; ISS:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00098; zf-CCHC; 5.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 5.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50158; ZF_CCHC; 5.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1156
FT /note="ATP-dependent RNA helicase glh-4"
FT /id="PRO_0000055092"
FT DOMAIN 767..951
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 986..1139
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 570..587
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 593..610
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 616..633
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 639..656
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 665..682
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 736..764
FT /note="Q motif"
FT MOTIF 897..900
FT /note="DEAD box"
FT COMPBIAS 58..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 780..787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 136
FT /note="L -> P (in Ref. 1; AAC28387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1156 AA; 120641 MW; 698829D125F81064 CRC64;
MSFSDDGWGA EAEVKVAEDV PEKNVPPPVE PPRAPQSTAI KTEPERNSDE PSAGFGIDPI
TTSKTFGSQT TPKTEFGGAP SLSGFGGNAA AAAANKTSFD QQGNGFGGAA KHGFGGVGGA
PSSFGANVIP VNKPSLGHKT TGFGGEPKHV SGGAFSSANN FDQQDKGFGG AASSGFGNGS
MLTNQKVGLE NQTTGVGASE VPTSKPSSFG QQPAVVSGFG GAAKMGFGGS SSSGFGGQKA
GATESSGFPT KETSTSQPGF GGDSSTGFGS GLKAGFGGHG AGAAENSGLP TETTGFGGKL
PSAGFGASSS NESAFGQQSK GFGGATKNGF GGDSSSSFGS GSKAGFGGTS SSGIGGQKPG
ATESSGFPTK ETSTSGGTFG SGFGGKPTST GFGAPSTTDS SSGQQTAGFG GASKPGFGGD
SSTGFGSGLK AGFGGHRAST AENSGLPTET TGFGGKLPPA GFGASSSNES AFGQQSKGFG
GATKNGFGGD SSNSFGKRDS GFGGPQDQGF GDTDAPSKSG LGSFNTGGGA VKSAFGAAGF
GSSSNFGNGN TFGEPSDNQR GNWDGGERPR GCHNCGEEGH ISKECDKPKV PRFPCRNCEQ
LGHFASDCDQ PRVPRGPCRN CGIEGHFAVD CDQPKVPRGP CRNCGQEGHF AKDCQNERVR
MEPTEPCRRC AEEGHWGYEC PTRPKDLQGN FLESYDFVFT PDDKMFEDAV NNDDKIDFDQ
KVVASTGKVE IPDMASFDGF KILPQDLHDN LKRMKMNRPT PIQRASFFPI MHGNDVVACA
HTGSGKTLAF LIPFVIKLME EFEKDRDVTD EKPSPRLLIV APTRELVNQT FTTARQLTYE
TGLKCGLAFG GYSRNANVQH LRSFSQLNIL VATMGRLQDF VNAGEVSLSK MKYIVLDEAD
RMVDSNDFGE EVSKIIGSPG ERTQQTVLFS ASFSEDLQSD DLPKFVKEGY TMLQVDKFGT
ANEKIDQKIL PVPRTEKRDA IYKLLGIDEN TVTLLPDAPI EKQKTLIFVN SVKFCDTLAA
LISSAGVSTI SMHSYQNQEQ RDRTLDDFRR GKYQCMVASN VCARGLNIAG LDHVVNYDMP
DKNGFDEYVN RIGRTGRAGF TGTSTAFVDV ENDTDIIPCL VSILNEAKKE VPEWLTEGAG
HQEEGGDDWN EQEQEW
