PAN2_CHICK
ID PAN2_CHICK Reviewed; 1197 AA.
AC Q5F450;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 52 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN Name=PAN2 {ECO:0000255|HAMAP-Rule:MF_03182}; Synonyms=USP52;
GN ORFNames=RCJMB04_3e13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_03182};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC PAN3. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03182}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182}.
CC Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03182}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000255|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; AJ851450; CAH65084.1; -; mRNA.
DR RefSeq; NP_001012972.1; NM_001012954.2.
DR RefSeq; XP_015155758.1; XM_015300272.1.
DR AlphaFoldDB; Q5F450; -.
DR SMR; Q5F450; -.
DR STRING; 9031.ENSGALP00000042623; -.
DR PaxDb; Q5F450; -.
DR Ensembl; ENSGALT00000058110; ENSGALP00000044566; ENSGALG00000031512.
DR Ensembl; ENSGALT00000078501; ENSGALP00000055744; ENSGALG00000031512.
DR GeneID; 429172; -.
DR KEGG; gga:429172; -.
DR CTD; 9924; -.
DR VEuPathDB; HostDB:geneid_429172; -.
DR eggNOG; KOG1275; Eukaryota.
DR GeneTree; ENSGT00390000013978; -.
DR HOGENOM; CLU_002369_0_0_1; -.
DR InParanoid; Q5F450; -.
DR OrthoDB; 128953at2759; -.
DR PhylomeDB; Q5F450; -.
DR Reactome; R-GGA-429947; Deadenylation of mRNA.
DR PRO; PR:Q5F450; -.
DR Proteomes; UP000000539; Unplaced.
DR Bgee; ENSGALG00000031512; Expressed in testis and 13 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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 Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
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 Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW Nuclease; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1197
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000280524"
FT REPEAT 153..193
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 195..231
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 244..280
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 328..367
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 486..919
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 970..1142
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 368..485
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 1176..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 973
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 975
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 1082
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 1134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
SQ SEQUENCE 1197 AA; 134863 MW; DF7BBD6401D02FE5 CRC64;
MNFEGLDPSL AEYAPTLHPA LDPVLDPHLN PSLLQNVELD PEGVPLEGIA VPESVHIVEG
MYSELHTAVS EVGVPVSVSH FDLHEEMLWV GNHGGHATSF FGPTLERYSS FQVNSSDDIR
QIQSLESGVL FLTKTNLKCM SRGGLIIFDY LMDEAEDMHS LLLTDSSTLL VGGLQNHVIE
IDLNTVQETQ KYTVEVPGIT IMRQSNRFFF CGHTSGKVSL RDLRTFVVEH EFDAYSGSLS
DFDVHGNLLV TCGFSSRMNG LACDRFLKVY DLRMMRATTP LQVHIDPFFL RFIPTYTSRL
AIISQTGQCQ FCEPTGLANP ADIFHVNTVG PLIMTFDVSA SKQALAFGDS EGCVHLWADS
PEVTFNTYSR ETDFALPCIV DTLPHLDWNQ DLVPLSLIPV PLTSETLLSD WPAANSAPAP
RRAPPVDPEI LRTMKKVGFI GYAPNPRTKL RNQIPYRLKE ADNEFDSFSQ VPESPIGREE
EPHLYMVAKK YRKVTIKYSK LGLEDFDFKH YNKTLFAGLE PHIPNAYCNC MIQVLYFLEP
VRCLVQNHLC QKEFCLGCEL GLLFHMLDLS RGDPCQGSNF LRAFRTIPEA SALGLILADS
DEATGKVNLG RLIQSWNRFI LTQLHQETQE QEGPQAYRGA GSSTFGSSGD SVIGQLFSCE
VENCSMCRCG KETVRVSSTL LFTLSYPESA EKPVKDYEFA QILKRSICLE QNTQAWCENC
EKYQPTVQTR NIRCLPDVLV INCEVNSSKE ADFWKTQAEY AFQRALMKRG GFEITKGKEI
SLGDWKELGN PEVGHSYPSV EELKNIWIPH AIKMRLTKNK ELDVCNWSES DELSPNDDPE
SVYVYDLMAT VVHILDSRTG GSLVGHIKVG ETYHQRKEGV THQQWYLFND FLIEPVDKCE
AVQFDMSWKV PAILYYARRN LNSKYNLVIK NPIEASVLLA EASLARKQRK CHATFIPLML
SEMPQAGDLV GLDAEFVTLN EEEAELRSDG TKSTIKPSQM SVARITCVRG QGPNEGVPFI
DDYISTQEQV VDYLTQYSGI KPGDLDAKIS SKHLTTLKST YLKLRFLIDV GVKFVGHGLQ
KDFRVINLMV PKDQVIDTVY LFHIPRKRMI SLRFLAWYFL DLKIQGETHD SIEDARTALQ
LYRKYLELSQ GGSEPDDFRK VLKALYEKGR KLDWKVPEPD SQSSPKHGAV FPPVLAL
