PAN2_HUMAN
ID PAN2_HUMAN Reviewed; 1202 AA.
AC Q504Q3; O75189; Q76E12; Q8IVE1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
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=KIAA0710, USP52;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH PAN3 AND POLYADENYLATE-BINDING
RP PROTEIN, MUTAGENESIS OF ASP-1087, AND VARIANT LEU-179.
RC TISSUE=Cervix carcinoma;
RX PubMed=14583602; DOI=10.1074/jbc.m309125200;
RA Uchida N., Hoshino S., Katada T.;
RT "Identification of a human cytoplasmic poly(A) nuclease complex stimulated
RT by poly(A)-binding protein.";
RL J. Biol. Chem. 279:1383-1391(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-179.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ASN-32 AND LEU-179.
RC TISSUE=Eye, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP LACK OF UBIQUITIN CARBOXYL TERMINAL HYDROLASE ACTIVITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16284618; DOI=10.1038/nsmb1016;
RA Yamashita A., Chang T.-C., Yamashita Y., Zhu W., Zhong Z., Chen C.-Y.A.,
RA Shyu A.-B.;
RT "Concerted action of poly(A) nucleases and decapping enzyme in mammalian
RT mRNA turnover.";
RL Nat. Struct. Mol. Biol. 12:1054-1063(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18625844; DOI=10.1083/jcb.200801196;
RA Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.;
RT "Deadenylation is prerequisite for P-body formation and mRNA decay in
RT mammalian cells.";
RL J. Cell Biol. 182:89-101(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23398456; DOI=10.1042/bj20130026;
RA Bett J.S., Ibrahim A.F., Garg A.K., Kelly V., Pedrioli P., Rocha S.,
RA Hay R.T.;
RT "The P-body component USP52/PAN2 is a novel regulator of HIF1A mRNA
RT stability.";
RL Biochem. J. 451:185-194(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH PAN3.
RX PubMed=23932717; DOI=10.1016/j.molcel.2013.07.011;
RA Christie M., Boland A., Huntzinger E., Weichenrieder O., Izaurralde E.;
RT "Structure of the PAN3 pseudokinase reveals the basis for interactions with
RT the PAN2 deadenylase and the GW182 proteins.";
RL Mol. Cell 51:360-373(2013).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-1201.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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. Also
CC acts as an important regulator of the HIF1A-mediated hypoxic response.
CC Required for HIF1A mRNA stability independent of poly(A) tail length
CC regulation. {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:16284618,
CC ECO:0000269|PubMed:23398456}.
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 ECO:0000269|PubMed:14583602};
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 (PubMed:14583602, PubMed:23932717). Interacts
CC with ZFP36 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:23932717}.
CC -!- INTERACTION:
CC Q504Q3; Q58A45: PAN3; NbExp=6; IntAct=EBI-1058976, EBI-2513054;
CC Q504Q3; Q9HCJ0: TNRC6C; NbExp=7; IntAct=EBI-1058976, EBI-6507625;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14583602,
CC ECO:0000269|PubMed:16284618}. Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03182, ECO:0000269|PubMed:18625844,
CC ECO:0000269|PubMed:23398456}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:16284618}. Note=Shuttles between nucleus and
CC cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:16284618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q504Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q504Q3-2; Sequence=VSP_023749;
CC Name=3;
CC IsoId=Q504Q3-3; Sequence=VSP_023748;
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA31685.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB107585; BAD02263.1; -; mRNA.
DR EMBL; AB014610; BAA31685.2; ALT_INIT; mRNA.
DR EMBL; BC024043; AAH24043.1; -; mRNA.
DR EMBL; BC094885; AAH94885.1; -; mRNA.
DR CCDS; CCDS44922.1; -. [Q504Q3-1]
DR CCDS; CCDS53802.1; -. [Q504Q3-3]
DR CCDS; CCDS8915.1; -. [Q504Q3-2]
DR RefSeq; NP_001120932.1; NM_001127460.2. [Q504Q3-1]
DR RefSeq; NP_001159751.1; NM_001166279.1. [Q504Q3-3]
DR RefSeq; NP_055686.3; NM_014871.4. [Q504Q3-2]
DR AlphaFoldDB; Q504Q3; -.
DR SMR; Q504Q3; -.
DR BioGRID; 115252; 394.
DR DIP; DIP-50708N; -.
DR IntAct; Q504Q3; 23.
DR STRING; 9606.ENSP00000401721; -.
DR MEROPS; C19.978; -.
DR iPTMnet; Q504Q3; -.
DR PhosphoSitePlus; Q504Q3; -.
DR BioMuta; PAN2; -.
DR DMDM; 296439280; -.
DR EPD; Q504Q3; -.
DR jPOST; Q504Q3; -.
DR MassIVE; Q504Q3; -.
DR MaxQB; Q504Q3; -.
DR PaxDb; Q504Q3; -.
DR PeptideAtlas; Q504Q3; -.
DR PRIDE; Q504Q3; -.
DR ProteomicsDB; 62400; -. [Q504Q3-1]
DR ProteomicsDB; 62401; -. [Q504Q3-2]
DR ProteomicsDB; 62402; -. [Q504Q3-3]
DR Antibodypedia; 28142; 138 antibodies from 24 providers.
DR DNASU; 9924; -.
DR Ensembl; ENST00000257931.9; ENSP00000257931.5; ENSG00000135473.16. [Q504Q3-3]
DR Ensembl; ENST00000425394.7; ENSP00000401721.2; ENSG00000135473.16. [Q504Q3-1]
DR Ensembl; ENST00000440411.8; ENSP00000388231.3; ENSG00000135473.16. [Q504Q3-2]
DR Ensembl; ENST00000548043.5; ENSP00000449861.1; ENSG00000135473.16. [Q504Q3-1]
DR Ensembl; ENST00000610546.4; ENSP00000481859.1; ENSG00000135473.16. [Q504Q3-1]
DR GeneID; 9924; -.
DR KEGG; hsa:9924; -.
DR MANE-Select; ENST00000440411.8; ENSP00000388231.3; NM_014871.6; NP_055686.4. [Q504Q3-2]
DR UCSC; uc001skx.3; human. [Q504Q3-1]
DR CTD; 9924; -.
DR DisGeNET; 9924; -.
DR GeneCards; PAN2; -.
DR HGNC; HGNC:20074; PAN2.
DR HPA; ENSG00000135473; Low tissue specificity.
DR MIM; 617447; gene.
DR neXtProt; NX_Q504Q3; -.
DR OpenTargets; ENSG00000135473; -.
DR PharmGKB; PA162398664; -.
DR VEuPathDB; HostDB:ENSG00000135473; -.
DR eggNOG; KOG1275; Eukaryota.
DR GeneTree; ENSGT00390000013978; -.
DR HOGENOM; CLU_002369_0_0_1; -.
DR InParanoid; Q504Q3; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 128953at2759; -.
DR PhylomeDB; Q504Q3; -.
DR TreeFam; TF105657; -.
DR BRENDA; 3.1.13.4; 2681.
DR PathwayCommons; Q504Q3; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR SignaLink; Q504Q3; -.
DR BioGRID-ORCS; 9924; 29 hits in 1098 CRISPR screens.
DR ChiTaRS; PAN2; human.
DR GeneWiki; USP52; -.
DR GenomeRNAi; 9924; -.
DR Pharos; Q504Q3; Tbio.
DR PRO; PR:Q504Q3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q504Q3; protein.
DR Bgee; ENSG00000135473; Expressed in right lobe of thyroid gland and 195 other tissues.
DR ExpressionAtlas; Q504Q3; baseline and differential.
DR Genevisible; Q504Q3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA: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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; Metal-binding;
KW mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1202
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000280521"
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..924
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 975..1147
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 BINDING 978
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 980
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 1087
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 1139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 643
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_023748"
FT VAR_SEQ 689..692
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14583602,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023749"
FT VARIANT 32
FT /note="S -> N (in dbSNP:rs11558139)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031162"
FT VARIANT 179
FT /note="I -> L (in dbSNP:rs1918496)"
FT /evidence="ECO:0000269|PubMed:14583602,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_031163"
FT VARIANT 1201
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1330054285)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036359"
FT MUTAGEN 1087
FT /note="D->A: Loss of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:14583602"
FT CONFLICT 9
FT /note="G -> E (in Ref. 4; AAH94885)"
FT /evidence="ECO:0000305"
FT CONFLICT 1091
FT /note="I -> V (in Ref. 4; AAH94885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1202 AA; 135368 MW; 579194C102FCA019 CRC64;
MNFEGLDPGL AEYAPAMHSA LDPVLDAHLN PSLLQNVELD PEGVALEALP VQESVHIMEG
VYSELHSVVA EVGVPVSVSH FDLHEEMLWV GSHGGHATSF FGPALERYSS FQVNGSDDIR
QIQSLENGIL FLTKNNLKYM ARGGLIIFDY LLDENEDMHS LLLTDSSTLL VGGLQNHIIE
IDLNTVQETQ KYAVETPGVT IMRQTNRFFF CGHTSGKVSL RDLRTFKVEH EFDAFSGSLS
DFDVHGNLLA ACGFSSRLTG LACDRFLKVY DLRMMRAITP LQVHVDPAFL RFIPTYTSRL
AIISQSGQCQ FCEPTGLANP ADIFHVNPVG PLLMTFDVSA SKQALAFGDS EGCVHLWTDS
PEPSFNPYSR ETEFALPCLV DSLPPLDWSQ DLLPLSLIPV PLTTDTLLSD WPAANSAPAP
RRAPPVDAEI LRTMKKVGFI GYAPNPRTRL RNQIPYRLKE SDSEFDSFSQ VTESPVGREE
EPHLHMVSKK YRKVTIKYSK LGLEDFDFKH YNKTLFAGLE PHIPNAYCNC MIQVLYFLEP
VRCLIQNHLC QKEFCLACEL GFLFHMLDLS RGDPCQGNNF LRAFRTIPEA SALGLILADS
DEASGKGNLA RLIQRWNRFI LTQLHQDMQE LEIPQAYRGA GGSSFCSSGD SVIGQLFSCE
MENCSLCRCG SETVRASSTL LFTLSYPDGS KSDKTGKNYD FAQVLKRSIC LDQNTQAWCD
TCEKYQPTIQ TRNIRHLPDI LVINCEVNSS KEADFWRMQA EVAFKMAVKK HGGEISKNKE
FALADWKELG SPEGVLVCPS IEELKNVWLP FSIRMKMTKN KGLDVCNWTD GDEMQWGPAR
AEEEHGVYVY DLMATVVHIL DSRTGGSLVA HIKVGETYHQ RKEGVTHQQW YLFNDFLIEP
IDKHEAVQFD MNWKVPAILY YVKRNLNSRY NLNIKNPIEA SVLLAEASLA RKQRKTHTTF
IPLMLNEMPQ IGDLVGLDAE FVTLNEEEAE LRSDGTKSTI KPSQMSVARI TCVRGQGPNE
GIPFIDDYIS TQEQVVDYLT QYSGIKPGDL DAKISSKHLT TLKSTYLKLR FLIDIGVKFV
GHGLQKDFRV INLMVPKDQV LDTVYLFHMP RKRMISLRFL AWYFLDLKIQ GETHDSIEDA
RTALQLYRKY LELSKNGTEP ESFHKVLKGL YEKGRKMDWK VPEPEGQTSP KNAAVFSSVL
AL
