ID G8YC09_PICSO Unreviewed; 1114 AA.
AC G8YC09;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000256|HAMAP-Rule:MF_03182};
DE EC=3.1.13.4 {ECO:0000256|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000256|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182};
GN Name=Piso0_002217 {ECO:0000313|EMBL:CCE82490.1};
GN Synonyms=PAN2 {ECO:0000256|HAMAP-Rule:MF_03182};
GN ORFNames=GNLVRS01_PISO0J07225g {ECO:0000313|EMBL:CCE82490.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE82490.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC turnover. PAN specifically shortens poly(A) tails of RNA and the
CC activity is stimulated by poly(A)-binding protein PAB1. PAN
CC deadenylation is followed by rapid degradation of the shortened mRNA
CC tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC two alternative mechanisms, namely exosome-mediated 3'-5'
CC exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be
CC involved in post-transcriptional maturation of mRNA poly(A) tails.
CC {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03182};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03182};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000256|HAMAP-Rule:MF_03182};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC PAN3. {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC regulatory subunit PAN3 to form the poly(A)-nuclease (PAN)
CC deadenylation complex. {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC is predicted to be catalytically inactive because it lacks the active
CC site catalytic triad characteristic of thiol proteases, with residues
CC at the equivalent structural positions that are incompatible with
CC catalysis, and it cannot bind ubiquitin. It functions as a structural
CC scaffold for intra- and intermolecular interactions in the complex.
CC {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC repeats and the pseudo-UCH domain mediates interaction with PAN3.
CC {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03182}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03182}.
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DR EMBL; FO082050; CCE82490.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YC09; -.
DR STRING; 559304.G8YC09; -.
DR eggNOG; KOG1275; Eukaryota.
DR HOGENOM; CLU_002369_1_0_1; -.
DR InParanoid; G8YC09; -.
DR OMA; YEELLWS; -.
DR Proteomes; UP000005222; Chromosome J.
DR GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:UniProtKB-UniRule.
DR CDD; cd06143; PAN2_exo; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR048841; PAN2_N.
DR InterPro; IPR028881; PAN2_UCH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15728; DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR PANTHER; PTHR15728:SF0; PAN2-PAN3 DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR Pfam; PF20770; PAN2_N; 1.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03182};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_03182}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03182};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03182};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_03182};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03182};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 513..852
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT BINDING 911
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 913
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 1020
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 1073
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
SQ SEQUENCE 1114 AA; 126053 MW; ABD890314EE86844 CRC64;
MESWGEVSRV VATASPASGE ASKISTLMFD AQYNLLWCGD AAGHTRSFTP SSSTLGTPYS
GVQLSQYTKF KTSGGDTEVI QFLNHSKGVL SLSRDSVNLN NRRGVSQLVV NSTTLDEPRF
GGLSAMSFNA SSSNEIVVAG DRLFKVDLAK PNQASALSHD GNVSHMSNAS KLLVLGLSSG
EVELFDPLSN QSVNTFHGHN GFLSDMDVQG NYILSCGNST RVRRTTHVQT SSVVDPLVNI
YDIRMMRPLA PIPFSPGASF AKFHAKLPNM IVIASPSGQI QFVDRYDQSK IYVYQADLKT
YGGKNRSSAL NNNIGNFVAS GNGEYIAFSD DYNLHLWSLL GNTSTNFSNF PSNLEQPDQI
APFSQNNIGV DKMVPLSCVG MPYFKDLLLS NYGHDHYFTK ELSKVPNSID IDLLEAYGTL
SYFPYDSAKY GHRNIYEGYK SVKDNFDSKQ NLIPKFISEK TGDEHISYGD NEAFNYKSED
SSIPNCYSNL KIHYSRFGVD DFDFSFYNRT KYSGLENHLD NSYVNPLIQI YKYCSIFQNF
VIKQSLKEWL PTDLDTVVNK GNESGSSLVT ELGYLFDMMD KSVGKNCIIT NFSKVLSTKQ
EANKQGLINE DECKSLNALD LRNIIIKLNR YLLDCCDSEL REQYSTSLDN IMRCIYSIET
RSNGCGIADR SYASSLYIDL TEIPYNRAKI NGFNRSLTIV DSIEHSMQQF KTIPCQYCDK
NYKHLLEIRR TLVKYPPILS INISLSVQDT TFIKEQNGWL SKEFFLLSEN GRSFITAKEE
NGFNKYELFG YVCEINHGSE LARGAHNLVT YIKIEEKWLL FNDFLVMQIP EEEVFDISPA
WKKPVIALYQ LSKPEKFEQF RKETFHQLSG LNDTILYRDH FMEGIREGMK KEYELLTRDE
APQVGSLLAI DAEFVVLNSE KVEIDCDGTR TLVKPRKISL ARISAIRGKG KMRSTPFIDD
YIVHTGYIDD YLTKFSGIQP GDLYPTESSK SLTTLQTAYR KLWLLLNLGC VFVGHGLQND
FRCINLHVPK SQIRDTAELF YLADFKRKLS LKFLAYILLK EKVQTGNHDS IEDALTALLL
YEKYLQLTST GEFNQALYRM YVEGQYLRYR VPDS
//
