XRN2_MOUSE
ID XRN2_MOUSE Reviewed; 951 AA.
AC Q9DBR1; Q3TI26; Q3TKF2; Q3UZT9; Q61489; Q99KS7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
DE AltName: Full=Protein Dhm1;
GN Name=Xrn2; Synonyms=Dhm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=7885830; DOI=10.1093/nar/23.3.357;
RA Shobuike T., Sugano S., Yamashita T., Ikeda H.;
RT "Characterization of cDNA encoding mouse homolog of fission yeast dhp1+
RT gene: structural and functional conservation.";
RL Nucleic Acids Res. 23:357-361(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-417 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Eye, Forelimb, Lung, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-471; SER-475;
RP SER-482; SER-487; SER-499 AND SER-678, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-286, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-847; ARG-880; ARG-883; ARG-895
RP AND ARG-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote the
CC termination of transcription by RNA polymerase II. During transcription
CC termination, cleavage at the polyadenylation site liberates a 5'
CC fragment which is subsequently processed to form the mature mRNA and a
CC 3' fragment which remains attached to the elongating polymerase. The
CC processive degradation of this 3' fragment by this protein may promote
CC termination of transcription. Binds to RNA polymerase II (RNAp II)
CC transcription termination R-loops formed by G-rich pause sites (By
CC similarity). {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- SUBUNIT: Interacts with POLR2A and SMN1/SMN2. Interacts with CDKN2AIP
CC and NKRF. Interacts with CDKN2AIPNL; the interaction is direct.
CC Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By
CC similarity). Interacts with DHX34; the interaction is RNA-independent
CC (By similarity). {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBR1-2; Sequence=VSP_007235;
CC -!- TISSUE SPECIFICITY: Expressed in the spleen, testis, heart, brain,
CC lung, liver, skeletal muscle, and kidney. {ECO:0000269|PubMed:7885830}.
CC -!- MISCELLANEOUS: [Isoform 2]: May result from the retention of an intron
CC in the cDNA. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04028.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D38517; BAA07524.1; -; mRNA.
DR EMBL; AK004800; BAB23573.1; -; mRNA.
DR EMBL; AK031247; BAC27318.1; -; mRNA.
DR EMBL; AK053643; BAC35458.1; -; mRNA.
DR EMBL; AK133654; BAE21766.1; -; mRNA.
DR EMBL; AK167019; BAE39193.1; -; mRNA.
DR EMBL; AK168037; BAE40020.1; -; mRNA.
DR EMBL; BC004028; AAH04028.1; ALT_INIT; mRNA.
DR EMBL; BC054743; AAH54743.1; -; mRNA.
DR CCDS; CCDS38258.1; -. [Q9DBR1-1]
DR PIR; I49635; I49635.
DR RefSeq; NP_036047.2; NM_011917.2. [Q9DBR1-1]
DR AlphaFoldDB; Q9DBR1; -.
DR SMR; Q9DBR1; -.
DR BioGRID; 204910; 21.
DR IntAct; Q9DBR1; 2.
DR STRING; 10090.ENSMUSP00000028921; -.
DR iPTMnet; Q9DBR1; -.
DR PhosphoSitePlus; Q9DBR1; -.
DR SwissPalm; Q9DBR1; -.
DR EPD; Q9DBR1; -.
DR jPOST; Q9DBR1; -.
DR MaxQB; Q9DBR1; -.
DR PaxDb; Q9DBR1; -.
DR PeptideAtlas; Q9DBR1; -.
DR PRIDE; Q9DBR1; -.
DR ProteomicsDB; 299725; -. [Q9DBR1-1]
DR ProteomicsDB; 299726; -. [Q9DBR1-2]
DR Antibodypedia; 24812; 192 antibodies from 28 providers.
DR DNASU; 24128; -.
DR Ensembl; ENSMUST00000028921; ENSMUSP00000028921; ENSMUSG00000027433. [Q9DBR1-1]
DR GeneID; 24128; -.
DR KEGG; mmu:24128; -.
DR UCSC; uc008msq.1; mouse. [Q9DBR1-2]
DR UCSC; uc008msr.1; mouse. [Q9DBR1-1]
DR CTD; 22803; -.
DR MGI; MGI:894687; Xrn2.
DR VEuPathDB; HostDB:ENSMUSG00000027433; -.
DR eggNOG; KOG2044; Eukaryota.
DR GeneTree; ENSGT00670000098098; -.
DR HOGENOM; CLU_006038_1_2_1; -.
DR InParanoid; Q9DBR1; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 685597at2759; -.
DR PhylomeDB; Q9DBR1; -.
DR TreeFam; TF105977; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 24128; 23 hits in 107 CRISPR screens.
DR ChiTaRS; Xrn2; mouse.
DR PRO; PR:Q9DBR1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DBR1; protein.
DR Bgee; ENSMUSG00000027433; Expressed in ectoplacental cone and 245 other tissues.
DR Genevisible; Q9DBR1; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0007017; P:microtubule-based process; TAS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016070; P:RNA metabolic process; IGI:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Exonuclease; Hydrolase;
KW Metal-binding; Methylation; mRNA processing; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..951
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000071397"
FT ZN_FING 262..278
FT /note="CCHC-type"
FT REGION 408..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 824
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 847
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 847
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 851
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 851
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 880
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 883
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 883
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 895
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 947
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 947
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT VAR_SEQ 931..951
FT /note="GYPREGRKYPLPPPSGRYSWN -> VISTMWAVEGKQHTAHC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:7885830"
FT /id="VSP_007235"
FT CONFLICT 122..124
FT /note="SKE -> IKG (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="H -> Q (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> P (in Ref. 2; BAE40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="I -> N (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="V -> E (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="P -> H (in Ref. 2; BAE40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="P -> Q (in Ref. 2; BAE40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="K -> R (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="Y -> L (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="P -> H (in Ref. 2; BAC27318)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="T -> K (in Ref. 2; BAC27318)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="P -> L (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="Q -> K (in Ref. 1; BAA07524)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="P -> H (in Ref. 2; BAC27318)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="D -> G (in Ref. 2; BAE40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="Q -> QV (in Ref. 2; BAC27318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 108687 MW; CF57479291DD18B9 CRC64;
MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN LYLDMNGIIH
PCTHPEDKPA PKNEDEMMVA IFEYIDRLFN IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
ASKEGMEAAV EKQRVREEIL AKGGFLPPEE IKERFDSNCI TPGTEFMDNL AKCLRYYIAD
RLNNDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG
LATHEPNFTI IREEFKPNKP KPCALCNQFG HEVKDCEGLP REKKGKHDEL ADSLPCAEGE
FIFLRLNVLR EYLERELTMA SLPFPFDVER SIDDWVFMCF FVGNDFLPHL PSLEIREGAI
DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE DSIFKKRKDD EDSFRRRQKE
KRKRMKRDQP AFTPSGILTP HALGSRNSPG CQVASNPRQA AYEMRMQRNS SPSISPNTSF
ASDGSPSPLG GIKRKAEDSD SEPEPEDNVR LWEAGWKQRY YKNKFDVDAA DEKFRRKVVQ
SYVEGLCWVL RYYYQGCASW KWYYPFHYAP FASDFEGIAD MSSEFEKGTK PFKPLEQLMG
VFPAASGNFL PPTWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL PFVDERRLRA
ALEEVYPDLT PEENRRNSLG GDVLFVGKLH PLRDFILELY QTGSTEPVDV PPELCHGIQG
TFSLDEEAIL PDQTVCSPVP MLRDLTQNTA VSINFKDPQF AEDYVFKAAM LPGARKPATV
LKPGDWEKSS NGRQWKPQLG FNRDRRPVHL DQAAFRTLGH VTPRGSGTSV YTNTALPPAN
YQGNNYRPLL RGQAQIPKLM SNMRPQDSWR GPPPLFQQHR FERSVGAEPL LPWNRMIQNQ
NAAFQPNQYQ MLGGPGGYPP RRDDHRGGRQ GYPREGRKYP LPPPSGRYSW N
