GLH1_CAEEL
ID GLH1_CAEEL Reviewed; 763 AA.
AC P34689; Q22873; Q7KQH5; Q9TXH4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ATP-dependent RNA helicase glh-1;
DE EC=3.6.4.13;
DE AltName: Full=Germline helicase 1;
GN Name=glh-1 {ECO:0000312|WormBase:T21G5.3};
GN ORFNames=T21G5.3 {ECO:0000312|WormBase:T21G5.3};
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=8415696; DOI=10.1073/pnas.90.20.9300;
RA Roussell D.L., Bennett K.L.;
RT "glh-1, a germ-line putative RNA helicase from Caenorhabditis, has four
RT zinc fingers.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9300-9304(1993).
RN [2]
RP SEQUENCE REVISION TO 83-138; 275; 288 AND 398.
RA Roussell D.L., McCrone J.S., Smith P.A., Gruidl M.E., Bennett K.L.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=8943022; DOI=10.1073/pnas.93.24.13837;
RA Gruidl M.E., Smith P.A., Kuznicki K.A., McCrone J.S., Kirchner J.,
RA Roussell D.L., Strome S., Bennett K.L.;
RT "Multiple potential germ-line helicases are components of the germ-line-
RT specific P granules of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13837-13842(1996).
RN [4]
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 [5]
RP INTERACTION WITH CSN-5 AND ZYX-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 [6]
RP INTERACTION WITH KGB-1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY KGB-1,
RP MOTIF, AND MUTAGENESIS OF LYS-581; LEU-588 AND LEU-589.
RX PubMed=17699606; DOI=10.1242/dev.005181;
RA Orsborn A.M., Li W., McEwen T.J., Mizuno T., Kuzmin E., Matsumoto K.,
RA Bennett K.L.;
RT "GLH-1, the C. elegans P granule protein, is controlled by the JNK KGB-1
RT and by the COP9 subunit CSN-5.";
RL Development 134:3383-3392(2007).
RN [7]
RP FUNCTION.
RX PubMed=18234720; DOI=10.1242/dev.015552;
RA Spike C.A., Bader J., Reinke V., Strome S.;
RT "DEPS-1 promotes P-granule assembly and RNA interference in C. elegans germ
RT cells.";
RL Development 135:983-993(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, 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 [9]
RP INTERACTION WITH PAN-1.
RX PubMed=22342905; DOI=10.1016/j.ydbio.2012.02.006;
RA Gao G., Deeb F., Mercurio J.M., Parfenova A., Smith P.A., Bennett K.L.;
RT "PAN-1, a P-granule component important for C. elegans fertility, has dual
RT roles in the germline and soma.";
RL Dev. Biol. 364:202-213(2012).
RN [10]
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 [11]
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).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28533440; DOI=10.1534/genetics.116.198812;
RA Spracklin G., Fields B., Wan G., Vijayendran D., Wallig A., Shukla A.,
RA Kennedy S.;
RT "Identification and characterization of Caenorhabditis elegans RNAi
RT inheritance machinery.";
RL Genetics 206:1403-1416(2017).
CC -!- FUNCTION: Probable ATP-binding RNA helicase (PubMed:8415696). May act
CC redundantly with the P-granule component glh-4 to regulate the
CC formation of the granular structure of P-granules in embryos
CC (PubMed:21402787, PubMed:24746798). Plays a role in positively
CC regulating the localization of pgl-1 to P-granules (PubMed:18234720).
CC May play a role in transgenerational epigenetic inheritance
CC (PubMed:28533440). May protect somatic cells from excessive apoptosis
CC during normal development (PubMed:27650246).
CC {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246,
CC ECO:0000305|PubMed:28533440, ECO:0000305|PubMed:8415696}.
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 with csn-5; this may prevent glh-1 degradation
CC induced by kgb-1 (PubMed:12435362, PubMed:17699606). Interacts with
CC zyx-1 (PubMed:12435362). Interacts (via the N-terminal region
CC containing the four CCHC zinc fingers) with pan-1 (PubMed:22342905).
CC Interacts with kgb-1; this may promote glh-1 degradation by the
CC proteasome (PubMed:17699606). {ECO:0000269|PubMed:12435362,
CC ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:22342905,
CC ECO:0000303|PubMed:17699606}.
CC -!- INTERACTION:
CC P34689; P91001: csn-5; NbExp=3; IntAct=EBI-1571791, EBI-313007;
CC P34689; O01836: glh-3; NbExp=2; IntAct=EBI-1571791, EBI-1571750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17699606,
CC ECO:0000269|PubMed:21402787}. Cytoplasmic granule
CC {ECO:0000269|PubMed:17699606}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17699606}. Note=Perinuclear localization in germ
CC cells but disperses into particles in cellularized oocytes. Component
CC of P granules. {ECO:0000269|PubMed:17699606}.
CC -!- DEVELOPMENTAL STAGE: First expressed during the L3-L4 stages of larval
CC development, coinciding with germline proliferation.
CC {ECO:0000269|PubMed:8415696}.
CC -!- PTM: Phosphorylated by kgb-1 (in vitro); this may be responsible for
CC its degradation by the proteasome. {ECO:0000269|PubMed:17699606}.
CC -!- DISRUPTION PHENOTYPE: Mortal germline (Mrt) phenotype in which there is
CC a progressive decline in fertility with each generation at 25 degrees
CC Celsius (PubMed:28533440). RNAi-mediated knockdown in a glh-4 mutant
CC background results in smaller P-granules and irregular cytoplasmic
CC localization of the P-granule component pgl-3 in embryos
CC (PubMed:21402787). Quadruple RNAi-mediated knockdown with glh-4, pgl-1
CC and pgl-3 results in offspring that display 27-89% sterility, abnormal
CC oocytes and do not have embryos in the uterus (PubMed:24746798). These
CC sterile offspring still produce sperm (PubMed:24746798). Furthermore,
CC these offspring may have compromised P-granule integrity as there is
CC diffuse cytoplasmic localization of the P-granule component deps-1,
CC which may cause germ cells to initiate somatic reprogramming
CC (PubMed:24746798). RNAi-mediated knockdown in a double ced-1 and hpl-2
CC mutant background rescues the reduced somatic cell apoptotic cell
CC defect in the ced-1 and hpl-2 double knockout (PubMed:27650246).
CC {ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:28533440}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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; L19948; AAC27384.1; -; mRNA.
DR EMBL; U62772; AAB04136.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD67591.1; -; Genomic_DNA.
DR PIR; A48686; A48686.
DR PIR; C87818; C87818.
DR PIR; T15132; T15132.
DR RefSeq; NP_491963.1; NM_059562.5.
DR AlphaFoldDB; P34689; -.
DR SMR; P34689; -.
DR BioGRID; 37860; 416.
DR IntAct; P34689; 4.
DR STRING; 6239.T21G5.3; -.
DR iPTMnet; P34689; -.
DR EPD; P34689; -.
DR PaxDb; P34689; -.
DR PeptideAtlas; P34689; -.
DR PRIDE; P34689; -.
DR EnsemblMetazoa; T21G5.3.1; T21G5.3.1; WBGene00001598.
DR GeneID; 172414; -.
DR KEGG; cel:CELE_T21G5.3; -.
DR UCSC; T21G5.3; c. elegans.
DR CTD; 172414; -.
DR WormBase; T21G5.3; CE25121; WBGene00001598; glh-1.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; P34689; -.
DR OMA; FKCSEPK; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; P34689; -.
DR SignaLink; P34689; -.
DR PRO; PR:P34689; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001598; Expressed in germ line (C elegans) and 4 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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0008432; F:JUN kinase binding; IPI:WormBase.
DR GO; GO:0043621; F:protein self-association; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0016070; P:RNA metabolic process; ISS: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; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 4.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 4.
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; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..763
FT /note="ATP-dependent RNA helicase glh-1"
FT /id="PRO_0000055089"
FT REPEAT 24..33
FT /note="1"
FT REPEAT 34..43
FT /note="2"
FT REPEAT 44..53
FT /note="3"
FT REPEAT 54..63
FT /note="4"
FT REPEAT 64..73
FT /note="5"
FT REPEAT 74..83
FT /note="6"
FT REPEAT 84..93
FT /note="7"
FT DOMAIN 372..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 592..739
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 158..175
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 183..200
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 242..259
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 262..279
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 24..93
FT /note="7 X 10 AA tandem repeats, Gly-rich"
FT REGION 193..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 341..369
FT /note="Q motif"
FT MOTIF 423..427
FT /note="Phosphodegron"
FT /evidence="ECO:0000303|PubMed:17699606"
FT MOTIF 499..502
FT /note="DEAD box"
FT BINDING 385..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 581
FT /note="K->N: Partially abolishes the interaction with kgb-
FT 1; when associated with W-588. No effect on the interaction
FT with kgb-1; when associated with W-589."
FT /evidence="ECO:0000269|PubMed:17699606"
FT MUTAGEN 588
FT /note="L->W: Partially abolishes the interaction with kgb-
FT 1; when associated with N-581."
FT /evidence="ECO:0000269|PubMed:17699606"
FT MUTAGEN 589
FT /note="L->W: No effect on the interaction with kgb-1; when
FT associated with N-581."
FT /evidence="ECO:0000269|PubMed:17699606"
FT CONFLICT 69
FT /note="T -> A (in Ref. 3; AAB04136)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="T -> I (in Ref. 1; AAC27384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 79780 MW; 956CADE2937A1725 CRC64;
MSDGWSDSES AAKAKTGFGS GGGFGGGNNG GSGFGGGKNG GTGFGGGNTG GSGFGGGNTG
GSGFGGGKTG GSGFGGGNTC GSGFGGGSTG GSPYGGASSG FGGSTATSGF GSGEKSSAFG
GSGGFGGSAT GFGSGGGSFG GGNSGFGEGG HGGGERNNNC FNCQQPGHRS SDCPEPRKER
EPRVCYNCQQ PGHTSRECTE ERKPREGRTG GFGGGAGFGN NGGNDGFGGD GGFGGGEERG
PMKCFNCKGE GHRSAECPEP PRGCFNCGEQ GHRSNECPNP AKPREGVEGE GPKATYVPVE
DNMEDVFNMQ KISEGLMFNK FFDAEVKLTS SEKTVGIKPC KTFAEANLTE TMQKNVAHAG
YSKTTPIQQY ALPLVHQGYD IMACAQTGSG KTAAFLLPIM TRLIDDNNLN TAGEGGCYPR
CIILTPTREL ADQIYNEGRK FAYQTMMEIK PVYGGLAVGY NKGQIEKGAT IIVGTVGRIK
HFCEEGTIKL DKCRFFVLDE ADRMIDAMGF GTDIETIVNY DSMPRKENRQ TLMFSATFPD
SVQEAARAFL RENYVMIAID KIGAANKCVL QEFERCERSE KKDKLLELLG IDIDSYTTEK
SAEVYTKKTM VFVSQRAMAD TLASILSSAQ VPAITIHGAR EQRERSEALR QFRNGSKPVL
IATAVAERGL DIKGVDHVIN YDMPDNIDDY IHRIGRTGRV GNSGRATSFI SEDCSLLSEL
VGVLADAQQI VPDWMQGAAG GNYGASGFGS SVPTQVPQDE EGW
