ID A0A3B0JKW5_DROGU Unreviewed; 1240 AA.
AC A0A3B0JKW5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=PAN2 {ECO:0000256|HAMAP-Rule:MF_03182};
GN ORFNames=DGUA_6G001433 {ECO:0000313|EMBL:SPP73876.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP73876.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in general
CC and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A)
CC tails of RNA and the activity is stimulated by poly(A)-binding protein
CC (PABP). PAN deadenylation is followed by rapid degradation of the
CC shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are
CC then degraded by two alternative mechanisms, namely exosome-mediated
CC 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA
CC decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.
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, P-body {ECO:0000256|HAMAP-
CC Rule:MF_03182}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03182}.
CC Note=Shuttles between nucleus and cytoplasm. {ECO:0000256|HAMAP-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OUUW01000001; SPP73876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JKW5; -.
DR STRING; 7266.A0A3B0JKW5; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 9810at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
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 GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; 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 Nucleus {ECO:0000256|HAMAP-Rule:MF_03182}.
FT DOMAIN 505..966
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 815..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1038
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 1040
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 1147
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 1199
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 1240 AA; 139017 MW; F33AE667323E1A92 CRC64;
MDYVYCGFDQ IGASEDILNA YDGGPPRGTG HFSPSFNGFN IGTTDPDYVE LVPVLADGGE
HFGVSSVIFD DYEELLWMGN QGGHVTSYYT SSMQKYTSFQ VHASDIVRQI ATLDSGVLVL
TQTSLRHQIR RGLPKFTHKS NHMAEMVCML QLSPNRLVMA GLQEELIDFD LRTLKETRLE
HVGAAGCTVL RKNSRYLFAG DQFGTVTLRD LNSLSVQHTI KTHTNVLSDF SVQGNLLISC
GYGGRQNNLA IDRFLMVYDL RMLRLISPIQ VLIDPQMLKF LPSLTSRLAV VSSYGQVQLV
DTVELSEPRV SMYQINTNGS QCLSFDISSS SQAMAFGDQS GHINMIASVQ TPQPQFNPFS
RNTEFADVVP QLPVVSITDT NFPLSSVMLP HLTTGTQWFS DWPEELLHYR YHRPKTIEPD
VLSSMKMQGP IGYSPNPRTA RRNQIPYVIE PGGVGSTNVN GATAVTKAEN GVKIIPRRYR
KVELKYTKLG TQDFDFDQHN QTCFAGLEAT LPNSYCNSML QILYFTEPLR MKLIEHVCTK
EFCLSCELGF LFNMLDKSSA SSPCQASNFL RSFRTVPEAS ALGLILTDRS ANVNLITLIQ
NWNRFILHQM HYEIFDSSKN SSAGGTVQAR SNADSSSTVD TSGSTDLYDS ICDDTAKDDD
RERSKINVET DISKIFGTKQ ICINRCIKCH VEKSKENLLL ACNMSYPTHI KDSEQYFNFG
TILKRSLSSE KSIQAFCENC KKFSPTNQSV KVTSLPQMLA INCGLNNDKD IGFLKRHLNR
CNEKPSVEVS ASLSTSKPCR YGANCSRSDC HFMHPDRKSP SHTSQSNNSS SSPSGRQKSW
FPLTFTMTIT DQGELVVQTQ SDTEKAEQEQ QEGQKPSIKS GEINRMYALH AVVCQVDDGT
QKNLVSLINV QRQYHTMKLA ASESSEDSQH QWYIFNDFSI SPVSPQESVW FTLDWKVPCV
LFYRSIEEES DLASSPDSTE APEESQPSDE AADSPVCLSN PFLHDMVSPI SSNLSTDATL
KPLQSNEMPQ SGDLVAMDAE FVTLNPEENE IRPDGKTATT KPCHMSVARI SCIRGQGANE
GVPFMDDYIS TQEKVVDYLT QFSGIKPGDL DANFSNKRLT ALKYSYQKLK YLVDVGVIFV
GHGLKNDFRV INIYVPSEQI IDTVHLFHMP HHRMVSLRFL AWHFLGTKIQ SETHDSIEDA
RTTLQLYKHY LKLQADKKFT SALKTLYERG KQLQWKVPEE
//
