| IED ID | IndEnz0002008545 |
| Enzyme Type ID | protease008545 |
| Protein Name |
PAN2-PAN3 deadenylation complex catalytic subunit PAN2 EC 3.1.13.4 PAB1P-dependent poly A -specific ribonuclease Poly A -nuclease deadenylation complex subunit 2 PAN deadenylation complex subunit 2 |
| Gene Name | PAN2 YGL094C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MNNWQHFFNNPVDLSEHLKKPYFRFDNRDKEITAISFDEKANLIWSGDSYGCISSYDPTFQLYTRYRGHIGGNSVKDILSHRDGILSISEDSLHFANRRGVTKLNLTSIDIAAFSELNTMCYSPHSLKNNIYCGGDNTNWGIASIDLNRGCLDSLLNYSSKVKLMCSNNKVLSIGRQTGTVDLLDPTSNRTIKSFNAHSASISAMDLRDNTLVTVGKSKRFYNLYADPFVNVYDLRTMRQLPPVSFSKGTTMGSGGADFVQLHPLLPTVMIVASSSGSFDFIDLSNPTLRTQYVHPCQSIKKLCLSPNGDVLGILEADNHLDTWRRSSNNMGMFTNTPEMLAYPDYFNDITSDGPISVDDETYPLSSVGMPYYLDKLLSAWPPVVFKSEGTIPQLTGKSPLPSSGKLKSNLAVISSQNEKLSTQEFPLLRYDRTKYGMRNAIPDYVCLRDIRKQITSGLETSDIQTYTSINKYEVPPAYSRLPLTSGRFGTDNFDFTPFNNTEYSGLDPDVDNHYTNAIIQLYRFIPEMFNFVVGCLKDENFETTLLTDLGYLFDMMERSHGKICSSSNFQASLKSLTDKRQLENGEPQEHLEEYLESLCIRESIEDFNSSESIKRNMPQKFNRFLLSQLIKEEAQTVNHNITLNQCFGLETEIRTECSCDHYDTTVKLLPSLSISGINKTVIKQLNKKSNGQNILPYIEYAMKNVTQKNSICPTCGKTETITQECTVKNLPSVLSLELSLLDTEFSNIRSSKNWLTSEFYGSIIKNKAVLRSTASELKGTSHIFKYELNGYVAKITDNNNETRLVTYVKKYNPKENCFKWLMFNDYLVVEITEEEALKMTYPWKTPEIIIYCDAEELRKPFFSVDTYSINYDILFRDYFANGIRDTARREYKLLTHDEAPKSGTLVAIDAEFVSLQSELCEIDHQGIRSIIRPKRTALARISIIRGEEGELYGVPFVDDYVVNTNHIEDYLTRYSGILPGDLDPEKSTKRLVRRNVVYRKVWLLMQLGCVFVGHGLNNDFKHININVPRNQIRDTAIYFLQGKRYLSLRYLAYVLLGMNIQEGNHDSIEDAHTALILYKKYLHLKEKAIFEKVLNSVYEEGRAHNFKVPETSKG |
| Enzyme Length | 1115 |
| Uniprot Accession Number | P53010 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by the regulatory subunit PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited under stress conditions. Inhibition of deadenylation under stress increases mRNA stability, which may be a mechanism to retain the majority of the cytoplasmic pool of mRNAs for later reuse and recovery from stress. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:16940550, ECO:0000269|PubMed:8816488}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:24880344}; |
| DNA Binding | |
| EC Number | 3.1.13.4 |
| Enzyme Function | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:11239395, ECO:0000269|PubMed:11953437, ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:15630021, ECO:0000269|PubMed:15894541, ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8550599, ECO:0000269|PubMed:8816488, ECO:0000269|PubMed:9774670}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (30); Chain (1); Domain (2); Helix (27); Metal binding (8); Mutagenesis (2); Region (1); Repeat (5); Turn (9) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Exonuclease;Hydrolase;Metal-binding;Nuclease;Reference proteome;Repeat;WD repeat;mRNA processing |
| Interact With | P36102 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (9) |
| Cross Reference PDB | 4Q8G; 4Q8H; 4XR7; 6R5K; 6R9I; 6R9J; 6R9M; 6R9O; 6R9P; 6R9Q; |
| Mapped Pubmed ID | 10669874; 11343902; 11805826; 12271148; 15044470; 15901499; 16429126; 16554755; 17572691; 18056425; 18467557; 18554525; 18657639; 18719252; 19034519; 19487562; 19536198; 19734957; 20498834; 20659020; 21118121; 21912624; 22266130; 22484098; 22785621; 23337855; 23416749; 23938393; 24992224; 25154419; 25255440; 25673754; 31104843; 31110294; 8852902; 9742129; |
| Motif | |
| Gene Encoded By | |
| Mass | 127,039 |
| Kinetics | |
| Metal Binding | METAL 660; /note="Zinc"; /evidence="ECO:0000269|PubMed:24880344, ECO:0007744|PDB:4Q8G"; METAL 662; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000269|PubMed:24880344, ECO:0007744|PDB:4Q8G"; METAL 713; /note="Zinc"; /evidence="ECO:0000269|PubMed:24880344, ECO:0007744|PDB:4Q8G"; METAL 716; /note="Zinc"; /evidence="ECO:0000269|PubMed:24880344, ECO:0007744|PDB:4Q8G"; METAL 910; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305|PubMed:24880344"; METAL 912; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305|PubMed:24880344"; METAL 1020; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1071; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305|PubMed:24880344" |
| Rhea ID | |
| Cross Reference Brenda |