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Database: UniProt
Entry: O76743
LinkDB: O76743
Original site: O76743 
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   11-DEC-2019, entry version 148.
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;
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}.
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   SMR; O76743; -.
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   EnsemblMetazoa; T12F5.3.2; T12F5.3.2; 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   eggNOG; ENOG410XNTI; LUCA.
DR   InParanoid; O76743; -.
DR   OMA; TEQEYES; -.
DR   OrthoDB; 1670303at2759; -.
DR   PRO; PR:O76743; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00001601; Expressed in 2 organ(s), highest expression level in adult organism.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005730; C:nucleolus; 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:0008432; F:JUN kinase binding; IPI:WormBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0042127; P:regulation of cell population proliferation; IMP:WormBase.
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; 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   NP_BIND         780..787
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           736..764
FT                   /note="Q motif"
FT   MOTIF           897..900
FT                   /note="DEAD box"
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
//
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