PAN2_CANAL
ID PAN2_CANAL Reviewed; 1190 AA.
AC Q5APK0; A0A1D8PEH7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=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};
GN OrderedLocusNames=CAALFM_C109070WA; ORFNames=CaO19.12228, CaO19.4764;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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: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 {ECO:0000255|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: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}.
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DR EMBL; CP017623; AOW26541.1; -; Genomic_DNA.
DR RefSeq; XP_723450.2; XM_718357.2.
DR AlphaFoldDB; Q5APK0; -.
DR SMR; Q5APK0; -.
DR STRING; 237561.Q5APK0; -.
DR GeneID; 3634773; -.
DR KEGG; cal:CAALFM_C109070WA; -.
DR CGD; CAL0000194881; orf19.12228.
DR VEuPathDB; FungiDB:C1_09070W_A; -.
DR HOGENOM; CLU_002369_1_0_1; -.
DR InParanoid; Q5APK0; -.
DR OrthoDB; 128953at2759; -.
DR PRO; PR:Q5APK0; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW Nuclease; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1190
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000295340"
FT REPEAT 24..63
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 129..166
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 167..207
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 222..264
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 266..306
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 322..361
FT /note="WD 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 512..924
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 988..1158
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 364..511
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 991
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 993
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 1097
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 1150
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 1190 AA; 136495 MW; 8308C393E925AA91 CRC64;
MDGWSEVLRI PSSVFATDNY NNPTTIVNIT SLQFDSVQNF IWCGDSRGYT RSFTGSFATN
SLYGNLQLYP YTKFHTSDVN YNNPIKQILS HREGILSLSN NAISFNSRRG LSKLQVTSKT
FNNNATTENK FNNLQAMTFN CNSFNDVVVG TDTSMMKFDL NKPNVLSSFD HQGGISLLNN
LGKFLTIANS NGSLDIFDPV SNSTMKTFSA HNGFISNLDV RGNYIATCGY SIKPKRYYHN
QPAEYIVDPL VNIYDTRIMR AIAPVPFPAG AASVKFHPKL PNIIIIASTS GQMQFVDIFD
QTNVYLYQAD LAIPTTTTTT INNKPRMSNL EISENGDFLV FNDNCDNMHL WSISPSSKDF
VNFPQPVEQP DIIDSNFEII DIDANVPLSI VGMPYYKELL LSNYPNDLRF VKETAKLPEP
IDIELILENE TRNNGTKKFF PYDKLKYGPG NVYKPYQSLK DNKENKEISI PKFISERSTT
TTTTTKELKA DNDGKFIDDS IFQYKFQGKL NKVPNCYSRL QIQYSKFGIK DFDFSYYNKT
KECCGLENHT DNSYINSLLQ LYRFQSSIYN QVVGSLSKEW LPNDITTIIT TNNPEGSSIL
NELGYLFDMM FKAQSNNVKI YNLSQVLNHH PNAQKLLNNN ELLNLNSQQV RDLVIEFNNF
LLTTLHQDFQ TQFQENFNLT ELKYEIEIKG NGTSCPMYDK HQGSMFSLEL ITPPSNMLNK
MSILINNNNN NNNPQYQPEP ISSLDNIRRN LNILTYLEYS MNQYKTIPCQ QHNHSYPHNL
EIQTSIVHLP SVLTINVNLS NPEFKIINNF TQWLVPEFYA VKSKSISGKN GYSFKEIDHP
TPNSATQESG KYKYKYELLG YVCEINHQSD IVSGAHNLVA FIKVNNNGGW YLFNDFLVMP
IPEEEVFDLQ PSWKKPIVIM YQQTNQPSFN YLTTTTTTTT TTTTFSNAGK YDDSILYRDH
FAEGIRKGHQ LEYELLTRKE SPQPGSLVAI DAEFVMLKPE ELEIHYDGYK KLIKPKQLSL
ARISVLRENG IPFIDDYIVH TSDIYDYLTN FSGIEPNDLN LTLSNRENLV TLQTAYRKLW
LLLNLGVIFV GHGLYNDFRT INLQVPERQI RDTAVIYYKS DFKRQLSLKF LAYVMLKEKV
QSGNHDSIED ANTALLLYKK YQNLYNKEDF ESILNYIYSE GQQLRFKVPE
