GLD3_CAEEL
ID GLD3_CAEEL Reviewed; 969 AA.
AC Q95ZK7; Q95ZK6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Defective in germ line development protein 3 {ECO:0000303|PubMed:12431376};
DE AltName: Full=Germline development defective 3 {ECO:0000303|PubMed:12431376};
GN Name=gld-3 {ECO:0000312|WormBase:T07F8.3a}; ORFNames=T07F8.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), ALTERNATIVE SPLICING,
RP FUNCTION, INTERACTION WITH FBF-1 AND FBF-2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12431376; DOI=10.1016/s1534-5807(02)00322-2;
RA Eckmann C.R., Kraemer B., Wickens M., Kimble J.;
RT "GLD-3, a bicaudal-C homolog that inhibits FBF to control germline sex
RT determination in C. elegans.";
RL Dev. Cell 3:697-710(2002).
RN [2] {ECO:0000312|EMBL:CCD65918.1}
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] {ECO:0000305}
RP INTERACTION WITH GLD-2.
RX PubMed=12239571; DOI=10.1038/nature01039;
RA Wang L., Eckmann C.R., Kadyk L.C., Wickens M., Kimble J.;
RT "A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans.";
RL Nature 419:312-316(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GLD-2, AND DISRUPTION PHENOTYPE.
RX PubMed=15454534; DOI=10.1534/genetics.104.029264;
RA Eckmann C.R., Crittenden S.L., Suh N., Kimble J.;
RT "GLD-3 and control of the mitosis/meiosis decision in the germline of
RT Caenorhabditis elegans.";
RL Genetics 168:147-160(2004).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GLS-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-327.
RX PubMed=19461891; DOI=10.1371/journal.pgen.1000494;
RA Rybarska A., Harterink M., Jedamzik B., Kupinski A.P., Schmid M.,
RA Eckmann C.R.;
RT "GLS-1, a novel P granule component, modulates a network of conserved RNA
RT regulators to influence germ cell fate decisions.";
RL PLoS Genet. 5:E1000494-E1000494(2009).
RN [6] {ECO:0000305, ECO:0000312|PDB:3N89}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 88-460, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH GLD-2.
RX PubMed=20823118; DOI=10.1261/rna.2315010;
RA Nakel K., Hartung S.A., Bonneau F., Eckmann C.R., Conti E.;
RT "Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a
RT globular structural platform.";
RL RNA 16:2058-2067(2010).
CC -!- FUNCTION: Required maternally for germline survival and embryogenesis.
CC Forms a complex with gls-1 which promotes the oogenic cell fate by
CC freeing the translational repressor fbf to repress sperm promoting
CC factors. Promotes maturation of primary spermatocytes to mature sperm.
CC Required during hermaphrodite development to promote sperm fate, which
CC is critical for determining the normal number of sperm. Promotion of
CC sperm fate is at the expense of oogenesis, possibly through the
CC negative regulation of fbf. Required during male development for the
CC continued production of sperm and inhibition of oogenesis. Together
CC with gld-2, promotes the transition from mitosis to meiosis.
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:15454534,
CC ECO:0000269|PubMed:19461891}.
CC -!- SUBUNIT: Interacts (via its KH1 domain) with gld-2. Isoform A but not
CC isoform B interacts specifically with fbf-1 and fbf-2 in an RNA-
CC independent manner. Isoform A interacts with gls-1 isoform C.
CC {ECO:0000269|PubMed:12239571, ECO:0000269|PubMed:12431376,
CC ECO:0000269|PubMed:15454534, ECO:0000269|PubMed:19461891,
CC ECO:0000269|PubMed:20823118}.
CC -!- INTERACTION:
CC Q95ZK7; O17087: gld-2; NbExp=2; IntAct=EBI-317828, EBI-2420017;
CC Q95ZK7-1; Q9N5M6: fbf-1; NbExp=2; IntAct=EBI-14989519, EBI-1569950;
CC Q95ZK7-1; Q8I4M5: gls-1; NbExp=3; IntAct=EBI-14989519, EBI-322416;
CC Q95ZK7-1; Q8I4M5-3: gls-1; NbExp=6; IntAct=EBI-14989519, EBI-14989623;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12431376,
CC ECO:0000269|PubMed:19461891}. Cytoplasmic granule
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:12431376,
CC ECO:0000269|PubMed:19461891}. Note=Localizes to P granules. Found also
CC in particles near but not coincident with P granules.
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Experimental confirmation
CC may be lacking for some isoforms. {ECO:0000305};
CC Name=a {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:9851916};
CC Synonyms=GLD-3L {ECO:0000303|PubMed:12431376};
CC IsoId=Q95ZK7-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:9851916};
CC Synonyms=GLD-3S {ECO:0000303|PubMed:12431376};
CC IsoId=Q95ZK7-2; Sequence=VSP_043966;
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level). In
CC adult hermaphrodites, first detected in the transition zone (TZ),
CC weakly expressed in the early mitotic region and in pachytene germ
CC cells, and becomes more abundantly expressed as germ cells enter
CC diakinesis (at protein level). Expressed in primary spermatocytes, but
CC not in secondary spermatocytes or adult sperm (at protein level).
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development and in adult hermaphrodites and males (at
CC protein level). {ECO:0000269|PubMed:12431376,
CC ECO:0000269|PubMed:19461891}.
CC -!- DISRUPTION PHENOTYPE: Loss of both maternal and zygotic expression
CC causes variable lethality, ranging from arrest during embryonic
CC development to soon after hatching, and sterility due to early germline
CC defects. In these animals the germline precursor cells Z2 and Z3 are
CC smaller, divide more slowly and their descendants remain small and
CC indistinct compared to their wild-type counterparts. In addition, some
CC of these animals show somatic defects, including a protruding vulva,
CC multiple vulvae or a reduction in animal size. In zygotic mutant adult
CC hermaphrodites, most spermatogenic cells are blocked as primary
CC spermatocytes, the number of spermatocytes appears lower than normal
CC and spermatogenesis is delayed by several hours. Zygotic mutant
CC homozygous adult males produce some spermatogenic cells, although these
CC sperm are less well defined morphologically than normal. In addition,
CC loss of maternal and zygotic expression results in adult males that
CC produce enlarged granular cells that appear oocyte-like and show
CC chromosomal bivalents typical of oocytes. In zygotic mutants the
CC mitotic region is longer and has more nuclei than normal, the mitotic
CC region/TZ boundary is shifted from 20 to an average of 27 or 28 nuclei
CC and the boundaries between mitotic region and TZ and TZ and pachytene
CC region are not sharp as in wild-type. {ECO:0000269|PubMed:12431376,
CC ECO:0000269|PubMed:15454534}.
CC -!- MISCELLANEOUS: The deletion mutant gld-3 (q730) makes no detectable
CC GLD-3; it is predicted to generate an mRNA with a premature stop codon,
CC which should be subject to NMD. The deletion mutant gld-3 (q741)
CC removes the fbf-binding site from isoform A, but leaves the gld-2-
CC binding site intact. Animals homozygous for gld-3 (7q41) enter meiosis,
CC but are feminized. In addition, gld-3 protein that retains its gld-2-
CC binding region, does not have the dramatic mitosis/meiosis delay seen
CC in gld-3 null mutants. By contrast, sex determination was not normal;
CC gld-3 (q741) males produced oocytes. Therefore, promotes meiosis
CC primarily via its interaction with gld-2 whereas the sperm/oocyte
CC decision relies on its interaction with fbf.
CC {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:15454534}.
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DR EMBL; BX284602; CCD65916.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD65918.1; -; Genomic_DNA.
DR RefSeq; NP_495479.2; NM_063078.3. [Q95ZK7-1]
DR RefSeq; NP_495480.1; NM_063079.5.
DR PDB; 3N89; X-ray; 2.79 A; A/B=88-460.
DR PDB; 4ZRL; X-ray; 2.28 A; B=13-88.
DR PDBsum; 3N89; -.
DR PDBsum; 4ZRL; -.
DR AlphaFoldDB; Q95ZK7; -.
DR SMR; Q95ZK7; -.
DR BioGRID; 39510; 17.
DR ComplexPortal; CPX-1132; gls-1-gld-3 complex.
DR ComplexPortal; CPX-1214; GLD-2-GLD-3 complex.
DR DIP; DIP-25960N; -.
DR IntAct; Q95ZK7; 10.
DR STRING; 6239.T07F8.3a; -.
DR EPD; Q95ZK7; -.
DR PaxDb; Q95ZK7; -.
DR PeptideAtlas; Q95ZK7; -.
DR PRIDE; Q95ZK7; -.
DR EnsemblMetazoa; T07F8.3a.1; T07F8.3a.1; WBGene00001597. [Q95ZK7-1]
DR EnsemblMetazoa; T07F8.3b.1; T07F8.3b.1; WBGene00001597.
DR GeneID; 174174; -.
DR KEGG; cel:CELE_T07F8.3; -.
DR UCSC; T07F8.3a; c. elegans.
DR CTD; 174174; -.
DR WormBase; T07F8.3a; CE42163; WBGene00001597; gld-3. [Q95ZK7-1]
DR WormBase; T07F8.3b; CE28652; WBGene00001597; gld-3.
DR eggNOG; ENOG502T0PW; Eukaryota.
DR HOGENOM; CLU_307611_0_0_1; -.
DR InParanoid; Q95ZK7; -.
DR OMA; QLPRIHE; -.
DR OrthoDB; 581884at2759; -.
DR SignaLink; Q95ZK7; -.
DR EvolutionaryTrace; Q95ZK7; -.
DR PRO; PR:Q95ZK7; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001597; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030880; C:RNA polymerase complex; EXP:ComplexPortal.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; IPI:WormBase.
DR GO; GO:1990749; F:polynucleotide adenylyltransferase activator activity; IDA:WormBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0018992; P:germ-line sex determination; IMP:WormBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:WormBase.
DR GO; GO:0042006; P:masculinization of hermaphroditic germ-line; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0006378; P:mRNA polyadenylation; EXP:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; EXP:ComplexPortal.
DR GO; GO:0051100; P:negative regulation of binding; IDA:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0000280; P:nuclear division; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ComplexPortal.
DR GO; GO:0060903; P:positive regulation of meiosis I; EXP:ComplexPortal.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:WormBase.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; EXP:ComplexPortal.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0043631; P:RNA polyadenylation; IDA:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR041194; GLD-3_KH5.
DR Pfam; PF17905; KH_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Meiosis; Reference proteome; Repeat.
FT CHAIN 1..969
FT /note="Defective in germ line development protein 3"
FT /id="PRO_0000418087"
FT DOMAIN 34..109
FT /note="KH 1"
FT /evidence="ECO:0000269|PubMed:20823118"
FT DOMAIN 113..187
FT /note="KH 2"
FT /evidence="ECO:0000269|PubMed:20823118"
FT DOMAIN 189..259
FT /note="KH 3"
FT /evidence="ECO:0000269|PubMed:20823118"
FT DOMAIN 270..342
FT /note="KH 4"
FT /evidence="ECO:0000269|PubMed:20823118"
FT DOMAIN 344..419
FT /note="KH 5"
FT /evidence="ECO:0000269|PubMed:20823118"
FT REGION 34..81
FT /note="gld-2-binding"
FT /evidence="ECO:0000269|PubMed:19461891"
FT REGION 57..471
FT /note="gls-1-binding"
FT /evidence="ECO:0000269|PubMed:19461891"
FT REGION 459..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..969
FT /note="gls-1-binding"
FT /evidence="ECO:0000269|PubMed:19461891"
FT REGION 860..949
FT /note="fbf-1-binding"
FT /evidence="ECO:0000269|PubMed:12431376"
FT REGION 950..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 575..753
FT /note="VSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRN
FT MGNRPSSSTGSYYPSTTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYER
FT QYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHRDVRNSNEYDFHVGNSGPAKRSPSL
FT EQVQLQMTH -> GARYSSNIYPFSYIVPQNFNFLNGNFG (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12431376,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_043966"
FT MUTAGEN 327
FT /note="G->R: Abolishes binding to gls-1."
FT /evidence="ECO:0000269|PubMed:19461891"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3N89"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3N89"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3N89"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:3N89"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:3N89"
SQ SEQUENCE 969 AA; 110324 MW; CA1DB3F2D68143C8 CRC64;
MGEQSHEKDH DEAHSYNPFV RSAVEYDADT RLQMAENAAS ARKLFVSSAL KDIIVNPENF
YHDFQQSAQM AEDANQRRQV SYNTKREAHI HQLKAQGLPL PSNIPMIEIN PTRVTLNMEF
ESQYYSLMTS DNGDHENVAS IMAETNTLIQ LPDRSVGGTT PDPFAQQVTI TGYFGDVDRA
RMLMRRNCHF TVFMALSKMK MPLHELQAHV RQNPIQNVEM SFVDAPEKNG IVTTYLRITA
REKNQHELIE AAKRLNEILF RESPAPENNF TLHFTLSTYY VDQVLGSSST AQLMPVIERE
TTTIISYPCY NNRNETRGNI YEIKVVGNID NVLKARRYIM DLLPISMCFN IKNTDMAEPS
RVSDRNIHMI IDESGIILKM TPSVYEPADL LSGEVPLNCA SLRSKEFNIK KLYTAYQKVL
SKKFDFIAPQ PNDYDNSIWH HSLPANFLKN FNMPCRGELS DGSNGRRHRS SSIASSRSKH
SYMSKGKQFS ESSGGPSRSH TRVSSFSENS STVPIMQFPT PHFAPPMLTP HHHMLKYVYL
QQHQQAQTFL KGAAGLHPGT HIMFPPPIIV DGSFVSALPF ADPVVFDGFP YVHGLFPVNE
AEQHRNHRES SPSLRSTQEI RKPSRNMGNR PSSSTGSYYP STTPRQRVYE QVREDDLRSH
IGSRRTSVNG DDQNVESMHD QGYERQYPRQ HQRLQKDDQQ RWKTGSRGDI HSSRTINVHR
DVRNSNEYDF HVGNSGPAKR SPSLEQVQLQ MTHHLKLKSN DVDLDHEKLY MHESPHNDSD
TTVSASGFGN DLMDGDFVQR FLSNANINES GRRPRTVSCF TEKDGQSARY IDSDGAYSVV
DHASTHQSRS YDSFRKVGDN GVTKTILEPR ARVEKDYGKI SLEHKTKYSN EYGDEEKSAE
NDTSSLGSRQ YRIDPMKLIA SVRESSEQLP RIHERQFSDV LNEKEKEIAD KSIESTVTQD
LSLDETSTY
