GLD4_CAEEL
ID GLD4_CAEEL Reviewed; 845 AA.
AC G5EFL0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Poly(A) RNA polymerase gld-4 {ECO:0000303|PubMed:19339688};
DE EC=2.7.7.19 {ECO:0000269|PubMed:19339688};
DE AltName: Full=Defective in germ line development protein 4;
DE AltName: Full=Germline development defective-4 {ECO:0000303|PubMed:19339688};
GN Name=gld-4 {ECO:0000312|WormBase:ZK858.1}; ORFNames=ZK858.1;
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, ECO:0000312|EMBL:ACO95123.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP GLS-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-139.
RX PubMed=19339688; DOI=10.1101/gad.494009;
RA Schmid M., Kuchler B., Eckmann C.R.;
RT "Two conserved regulatory cytoplasmic poly(A) polymerases, GLD-4 and GLD-2,
RT regulate meiotic progression in C. elegans.";
RL Genes Dev. 23:824-836(2009).
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).
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. The
CC enzymatic activity is enhanced by its interaction with gls-1. Required,
CC together with gld-2, for early meiotic progression in male and female
CC germ cells and for gld-1 protein accumulation in the hermaphrodite
CC germline. In the germline, forms a complex with gls-1 which directly
CC binds to gld-1 mRNA and prevents its degradation.
CC {ECO:0000269|PubMed:19339688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:19339688};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O17087};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O17087};
CC -!- SUBUNIT: Interacts with gls-1 isoform C. {ECO:0000269|PubMed:19339688}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19339688}.
CC Cytoplasmic granule {ECO:0000269|PubMed:19339688}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:19339688}. Note=Localizes to P
CC granules. This association is less apparent during pachytene, becomes
CC obvious in maturing oocytes and is most prominently visible in
CC developing embryos. {ECO:0000269|PubMed:19339688}.
CC -!- TISSUE SPECIFICITY: Germline-specific. {ECO:0000269|PubMed:19339688}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout embryonic development and in adult hermaphrodites.
CC {ECO:0000269|PubMed:19339688}.
CC -!- DOMAIN: In contrast to other poly(A) RNA polymerases, lacks any RNA-
CC binding domain. {ECO:0000269|PubMed:19339688}.
CC -!- DISRUPTION PHENOTYPE: High embryonic lethality. Hermaphrodite animals
CC are partially fertile and those that produce sperm and oocytes have
CC reduced brood sizes and display smaller germlines. Hermaphrodite gld-4
CC and gld-2 double mutants are fully sterile and display either an
CC earlier meiotic arrest than gld-2 single mutant or a failure to commit
CC to meiotic progression and a return to mitosis.
CC {ECO:0000269|PubMed:19339688}.
CC -!- MISCELLANEOUS: The gld-4 locus produces a single transcript that is SL-
CC 1 trans-spliced. {ECO:0000269|PubMed:19339688}.
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DR EMBL; FJ610054; ACO95123.1; -; mRNA.
DR EMBL; Z79759; CAB02138.3; -; Genomic_DNA.
DR RefSeq; NP_492446.3; NM_060045.4.
DR AlphaFoldDB; G5EFL0; -.
DR SMR; G5EFL0; -.
DR BioGRID; 38166; 2.
DR IntAct; G5EFL0; 1.
DR STRING; 6239.ZK858.1; -.
DR EPD; G5EFL0; -.
DR PaxDb; G5EFL0; -.
DR PeptideAtlas; G5EFL0; -.
DR EnsemblMetazoa; ZK858.1.1; ZK858.1.1; WBGene00014115.
DR GeneID; 172735; -.
DR KEGG; cel:CELE_ZK858.1; -.
DR CTD; 172735; -.
DR WormBase; ZK858.1; CE42850; WBGene00014115; gld-4.
DR eggNOG; KOG1906; Eukaryota.
DR GeneTree; ENSGT00940000169468; -.
DR HOGENOM; CLU_320096_0_0_1; -.
DR InParanoid; G5EFL0; -.
DR OMA; KISMFGS; -.
DR OrthoDB; 720205at2759; -.
DR PRO; PR:G5EFL0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00014115; Expressed in adult organism and 4 other tissues.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:WormBase.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:WormBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Developmental protein; Magnesium; Manganese;
KW Meiosis; Metal-binding; mRNA processing; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..845
FT /note="Poly(A) RNA polymerase gld-4"
FT /id="PRO_0000419046"
FT DOMAIN 276..335
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O17087, ECO:0000305"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O17087, ECO:0000305"
FT MUTAGEN 139
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19339688"
SQ SEQUENCE 845 AA; 94310 MW; C4836B6F8E7CC372 CRC64;
MNEDSRLSSS QQPSTSTPRS SIPSTMNSDE PNTCRRLSQS QEQPSTSRTC KSETPEFGYS
DSLPFAPWRR KRYGLNIQGL HEEIVDMYHW IKPNEIESRL RTKVFEKVRD SVLRRWKQKT
IKISMFGSLR TNLFLPTSDI DVLVECDDWV GTPGDWLAET ARGLEADNIA ESVMVYGGAF
VPIVKMVDRD TRLSIDISFN TVQGVRAASY IAKVKEEFPL IEPLVLLLKQ FLHYRNLNQT
FTGGLSSYGL VLLLVNFFQL YALNMRSRTI YDRGVNLGHL LLRFLELYSL EFNFEEMGIS
PGQCCYIPKS ASGARYGHKQ AQPGNLALED PLLTANDVGR STYNFSSIAN AFGQAFQILL
VAVTLRERKG KNHVAMRAYK GSLLHLIMPF TSKELTYRNW LMSGVLSMPG QEAPASYDLN
QLHNTLVSPM VDLSRYAWLR KAPAKAEKRD SRPLTIVNPA DDRQTLAQQL KKQILEQTEA
KKSLEKMPAC DDNKKEEELV ATRETDVELE AEDTESEGHH NGENDLILTG PPLPTSTQSV
NTSATVSTAA SISEREDTDS PGLSSSMGNQ SSEEDEDNGI NNRNNSAVPV QFKKPFNEVV
AQPARESKRT QTTSEDKMQD QFHFNGYSYP PPSRYAAGTA APSHKHRNAH PQRQRPSIRN
LSQGSDGSDE YNVESWNNNI RQGRRASSNS PSPSRQQTNT RNCGPTNNIP YDSFRSQNKN
STLDGSNNSS EEPITMYADV VKKKSSITTS TNTSTADVNV TNGNPIPANG IIPQSMAVVN
VGRGSYRNAL TTSPMTPPSA HTSMQKQHHL RKDNECGFDN NSATSSTDLS HHQPQLVPPV
NRLQR
