PAN3_CAEEL
ID PAN3_CAEEL Reviewed; 632 AA.
AC P34653;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE Short=PAN deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN Name=panl-3 {ECO:0000312|WormBase:ZK632.7};
GN Synonyms=PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN ORFNames=ZK632.7 {ECO:0000312|WormBase:ZK632.7};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
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 AIN-1.
RX PubMed=22402495; DOI=10.1093/nar/gks218;
RA Kuzuoglu-Ozturk D., Huntzinger E., Schmidt S., Izaurralde E.;
RT "The Caenorhabditis elegans GW182 protein AIN-1 interacts with PAB-1 and
RT subunits of the PAN2-PAN3 and CCR4-NOT deadenylase complexes.";
RL Nucleic Acids Res. 40:5651-5665(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23843623; DOI=10.1242/jcs.132936;
RA Nousch M., Techritz N., Hampel D., Millonigg S., Eckmann C.R.;
RT "The Ccr4-Not deadenylase complex constitutes the main poly(A) removal
RT activity in C. elegans.";
RL J. Cell Sci. 126:4274-4285(2013).
CC -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC involved in general and miRNA-mediated mRNA turnover. PAN specifically
CC shortens poly(A) tails of RNA and the activity is stimulated by
CC poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid
CC degradation of the shortened mRNA tails by the CCR4-NOT complex.
CC Deadenylated mRNAs are then degraded by two alternative mechanisms,
CC namely exosome-mediated 3'-5' exonucleolytic degradation, or
CC deadenylation-dependent mRNA decaping and subsequent 5'-3'
CC exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator
CC for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its
CC interaction with RNA and PABP, and to miRNA targets via its interaction
CC with GW182 family proteins. Within the PAN complex, may positively
CC regulate fertility (PubMed:23843623). {ECO:0000255|HAMAP-Rule:MF_03181,
CC ECO:0000269|PubMed:23843623}.
CC -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2
CC to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts
CC (via PAM-2 motif) with poly(A)-binding protein (via PABC domain),
CC conferring substrate specificity of the enzyme complex (By similarity).
CC Interacts with the GW182 family protein ain-1 (PubMed:22402495).
CC {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:22402495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- TISSUE SPECIFICITY: Highly expressed in germ cells.
CC {ECO:0000269|PubMed:23843623}.
CC -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain is
CC predicted to be catalytically inactive because some of the residues
CC important for catalytic activity are substituted and it lacks the
CC equivalent of the binding site for a peptide substrate. However, it has
CC retained an ATP-binding site and ATP-binding is required for mRNA
CC degradation, stimulating the activity of the PAN2 nuclease in vitro.
CC The nucleotide-binding site is juxtaposed to the RNase active site of
CC PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA
CC rather than ATP, feeding the poly(A)-tail to the active site of the
CC deadenylase and thus increasing the efficiency with which this
CC distributive enzyme degrades oligo(A) RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal
CC knob domain (CK) form a structural unit (PKC) that forms an extensive
CC high-affinity interaction surface for PAN2. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
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DR EMBL; BX284603; CAA80184.3; -; Genomic_DNA.
DR PIR; S40939; S40939.
DR RefSeq; NP_499177.3; NM_066776.5.
DR AlphaFoldDB; P34653; -.
DR SMR; P34653; -.
DR BioGRID; 41585; 2.
DR ComplexPortal; CPX-653; Pan complex.
DR DIP; DIP-24759N; -.
DR IntAct; P34653; 2.
DR MINT; P34653; -.
DR STRING; 6239.ZK632.7; -.
DR EPD; P34653; -.
DR PaxDb; P34653; -.
DR PeptideAtlas; P34653; -.
DR EnsemblMetazoa; ZK632.7.1; ZK632.7.1; WBGene00014015.
DR EnsemblMetazoa; ZK632.7.2; ZK632.7.2; WBGene00014015.
DR GeneID; 176391; -.
DR KEGG; cel:CELE_ZK632.7; -.
DR UCSC; ZK632.7; c. elegans.
DR CTD; 176391; -.
DR WormBase; ZK632.7; CE37601; WBGene00014015; panl-3.
DR eggNOG; KOG3741; Eukaryota.
DR GeneTree; ENSGT00390000001504; -.
DR HOGENOM; CLU_016423_3_1_1; -.
DR InParanoid; P34653; -.
DR OMA; IGPHSQN; -.
DR OrthoDB; 1515085at2759; -.
DR PhylomeDB; P34653; -.
DR PRO; PR:P34653; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00014015; Expressed in embryo and 4 other tissues.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR HAMAP; MF_03181; PAN3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030844; PAN3.
DR InterPro; IPR041332; Pan3_PK.
DR PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; mRNA processing; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..632
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000065524"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..494
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 534..632
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 495..533
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 321..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 397..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 632 AA; 71201 MW; 10062FC84AA29C1F CRC64;
MQPGEGYHYD SGPNNAVHPH QLPAGSRLNQ YLANNNRQGP SFGPGTPINV NAPVFVPKHQ
QPQPAQVAAP PPMVNQFAQL SIHDVPHQMI PFGQINGPPT FGPGQHMNHR ASHHHQSPQM
AQQPPTLQQS AYDRYQLENR GGTTYFYTEP TEAGPDDEQY TEAEAPDGSI LVNTPGAFGY
NAPLPISHMA RFRGKANANL QTQFISPEIR MELINRQLAY DTKADSAIIG DIPHSVEHFS
NLVPLEIAGI QSQTTYKAFS CRDGNYYCLR RIHGNRIQHP GKQTHLVEQW KKLVHGNVVP
LREVLINCRA FDDSSLIFAY DYYPLAGTLM EKHFDTKSGT FFDPNNGFRI SSPMNVSMPI
SGTGAHETLI WSYIIQIAAA LRAIHSSGLA CRTLDLNKII TYGNKIMISF CGIQDVLDPD
PTTIQQQQNE DLNMFGNLIV ALATGRANGW RKDLYQQLKK FIEDTYSMDL RNVIGFLHNN
STRKTINEIM PMIGGRFFTV MENMQAKTDV LEAELSREME NGRLFRLVAK MNTVLERVEH
GTDDAWSETG DRFMLKLFRD YVFHQVTDQG KAWLDMAHIV QCLNKLDCGS QEKIEMVSRS
GDTQIIIDYA TLKRCLDKSF RDLLGTNMML HR
