TSN1_ARATH
ID TSN1_ARATH Reviewed; 991 AA.
AC Q8VZG7; F4K6N0; Q9LY25;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Ribonuclease TUDOR 1 {ECO:0000303|PubMed:20396901};
DE Short=AtTudor1 {ECO:0000303|PubMed:20396901};
DE Short=TUDOR-SN protein 1 {ECO:0000303|PubMed:20396901};
DE EC=3.1.-.- {ECO:0000269|PubMed:25736060};
GN Name=TSN1 {ECO:0000303|PubMed:20396901};
GN OrderedLocusNames=At5g07350 {ECO:0000312|Araport:AT5G07350};
GN ORFNames=T2I1.60 {ECO:0000312|EMBL:CAB87924.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-970; SER-975 AND THR-980, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=20396901; DOI=10.1007/s00425-010-1167-0;
RA Liu S., Jia J., Gao Y., Zhang B., Han Y.;
RT "The AtTudor2, a protein with SN-Tudor domains, is involved in control of
RT seed germination in Arabidopsis.";
RL Planta 232:197-207(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND PHOSPHORYLATION AT 975.
RC STRAIN=cv. Wassilewskija;
RX PubMed=20484005; DOI=10.1105/tpc.109.070680;
RA Frei dit Frey N., Muller P., Jammes F., Kizis D., Leung J.,
RA Perrot-Rechenmann C., Bianchi M.W.;
RT "The RNA binding protein Tudor-SN is essential for stress tolerance and
RT stabilizes levels of stress-responsive mRNAs encoding secreted proteins in
RT Arabidopsis.";
RL Plant Cell 22:1575-1591(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25205572; DOI=10.1093/jxb/eru334;
RA Yan C., Yan Z., Wang Y., Yan X., Han Y.;
RT "Tudor-SN, a component of stress granules, regulates growth under salt
RT stress by modulating GA20ox3 mRNA levels in Arabidopsis.";
RL J. Exp. Bot. 65:5933-5944(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DOMAIN, AND ACTIVITY
RP REGULATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=25736060; DOI=10.1105/tpc.114.134494;
RA Gutierrez-Beltran E., Moschou P.N., Smertenko A.P., Bozhkov P.V.;
RT "Tudor staphylococcal nuclease links formation of stress granules and
RT processing bodies with mRNA catabolism in Arabidopsis.";
RL Plant Cell 27:926-943(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26237081; DOI=10.1080/15592324.2015.1071005;
RA Gutierrez-Beltran E., Bozhkov P.V., Moschou P.N.;
RT "Tudor staphylococcal nuclease plays two antagonistic roles in RNA
RT metabolism under stress.";
RL Plant Signal. Behav. 10:E1071005-E1071005(2015).
CC -!- FUNCTION: Cytoprotective ribonuclease (RNase) required for resistance
CC to abiotic stresses, acting as a positive regulator of mRNA decapping
CC during stress (PubMed:25736060). Essential for the integrity and
CC function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes
CC called stress granules (SGs) and processing bodies (PBs), sites of
CC post-transcriptional gene regulation during stress (e.g. salt and heat)
CC (PubMed:25736060). Involved in gibberellic acid (GA) biosynthesis
CC (PubMed:25205572). Essential for stress tolerance, probably by
CC regulating mRNAs entering the secretory pathway (PubMed:20484005).
CC Component of stress granules (SGs) that regulates growth under salt
CC stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA
CC (PubMed:25205572). May inhibit the degradation of mRNAs involved in
CC stress adaptation (PubMed:26237081). {ECO:0000269|PubMed:20484005,
CC ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060,
CC ECO:0000269|PubMed:26237081}.
CC -!- ACTIVITY REGULATION: Repressed by the specific inhibitor 3',5'-
CC deoxythymidine bisphosphate (pdTp); this RNase activity inhibition
CC impairs subcellular relocation upon abiotic stress and leads to reduced
CC stress resistance. {ECO:0000269|PubMed:25736060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20484005,
CC ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasmic
CC granule {ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:20484005}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:20484005}. Note=Accumulates
CC heterogeneously in the cytosol, in patches around the nucleus and in
CC the cell periphery, and relocates transiently to a diffuse pattern in
CC response to salt stress (PubMed:20484005). Accumulates in cytoplasmic
CC stress granules (SGs) and processing bodies (PBs) in response to
CC abiotic stresses (e.g. salt and heat) (PubMed:25205572,
CC PubMed:25736060). {ECO:0000269|PubMed:20484005,
CC ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZG7-2; Sequence=VSP_058574;
CC -!- TISSUE SPECIFICITY: Expressed in seeds, leaves, flowers, roots and
CC siliques (at protein level) (PubMed:20396901, PubMed:20484005).
CC Accumulates in the cap and elongation zone of the root apices (at
CC protein level) (PubMed:20484005). {ECO:0000269|PubMed:20396901,
CC ECO:0000269|PubMed:20484005}.
CC -!- INDUCTION: Accumulates after salt treatment.
CC {ECO:0000269|PubMed:25205572}.
CC -!- DOMAIN: TNase-like domains are required for relocation to cytoplasmic
CC foci upon abiotic stresses. {ECO:0000269|PubMed:25736060}.
CC -!- DISRUPTION PHENOTYPE: Normal vegetative growth, flowering time and
CC flower morphology (PubMed:20396901). Reduced expression of enzyme
CC involved in GA biosynthesis leading to reduced levels of GA-4 (e.g.
CC GA20OX3). Slower growth in salt conditions (PubMed:25205572). The
CC double mutant tsn1 tsn2 exhibits severe alteration in germination,
CC growth, and survival under high salinity stress. Reduced levels of
CC stress-regulated mRNAs encoding secreted proteins (PubMed:20484005).
CC Abnormal stress granules (SGs) and processing bodies (PBs) assembly
CC accompanied by reduced uncapped RNAs levels in heat-stressed double
CC mutant tsn1 tsn2 (PubMed:25736060). The double mutant tsn1 tsn2 is also
CC showing enriched uncapping and subsequent degradation of mRNAs involved
CC in stress adaptation (PubMed:26237081). {ECO:0000269|PubMed:20396901,
CC ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572,
CC ECO:0000269|PubMed:25736060, ECO:0000269|PubMed:26237081}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87924.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AL163912; CAB87924.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91140.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91141.1; -; Genomic_DNA.
DR EMBL; AY064975; AAL57629.1; -; mRNA.
DR PIR; T49874; T49874.
DR RefSeq; NP_001154697.2; NM_001161225.2. [Q8VZG7-2]
DR RefSeq; NP_196352.2; NM_120817.3. [Q8VZG7-1]
DR AlphaFoldDB; Q8VZG7; -.
DR SMR; Q8VZG7; -.
DR IntAct; Q8VZG7; 1.
DR STRING; 3702.AT5G07350.2; -.
DR iPTMnet; Q8VZG7; -.
DR PRIDE; Q8VZG7; -.
DR ProteomicsDB; 234592; -. [Q8VZG7-1]
DR EnsemblPlants; AT5G07350.1; AT5G07350.1; AT5G07350. [Q8VZG7-1]
DR EnsemblPlants; AT5G07350.2; AT5G07350.2; AT5G07350. [Q8VZG7-2]
DR GeneID; 830626; -.
DR Gramene; AT5G07350.1; AT5G07350.1; AT5G07350. [Q8VZG7-1]
DR Gramene; AT5G07350.2; AT5G07350.2; AT5G07350. [Q8VZG7-2]
DR KEGG; ath:AT5G07350; -.
DR Araport; AT5G07350; -.
DR TAIR; locus:2183359; AT5G07350.
DR eggNOG; KOG2039; Eukaryota.
DR HOGENOM; CLU_005966_2_0_1; -.
DR OMA; EAREYTH; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q8VZG7; -.
DR BRENDA; 3.1.31.1; 399.
DR PRO; PR:Q8VZG7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZG7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0010372; P:positive regulation of gibberellin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00565; SNase; 4.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 5.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Hydrolase; Nuclease; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..991
FT /note="Ribonuclease TUDOR 1"
FT /id="PRO_0000437883"
FT DOMAIN 8..151
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 186..364
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 378..557
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 587..714
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 782..847
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 227..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 970
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 980
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 990..991
FT /note="RR -> LEIRGSLNHAYKQKKSRD (in isoform 2)"
FT /id="VSP_058574"
SQ SEQUENCE 991 AA; 108235 MW; 4192E2F57B896010 CRC64;
MATGAENQWL KGRVKAVTSG DCLVITALSH NRAGPPPEKT ITFSSLMAPK MARRGGIDEP
FAWESKEFLR KLCIGKEVAF KVDYKVEAIA GREFGSVFLG NENLAKLVVK TGWAKVREPG
QQNQDKVSPY IKELLQLEEL AKQEGYGRWS KVPGAAEASI RNLPPSAIGD SAGFDAMGLL
AANKGKPMEG IVEQVRDGST IRVYLLPEFQ FVQVFVAGVQ APSMGRRTTN GSVVETVPDE
PNGDVSAESR GPLTTAQRLA ASAASSVEVS SDPFATEAKY FTEHRVLSRD VRIVLEGVDK
FNNLIGSVHY SDGETVKDLG LELVENGLAK FVEWSANMME EEAKKKLKAA ELQCKKDKVK
MWANYVPPAT NSKAIHDQNF TGKVVEVVSG DCLIVADDAV PFGSPAAERR VCLSSIRSPK
MGNPRREEKP APYAREAREF LRQRLIGKQV IVQMEYSRKV TQGDGPTTSG AADRFMDFGS
VFLPSAAKAD SDEVTAPPAA AIAGSQPVGV NIAELVLVRG FGNVVRHRDF EERSNHYDAL
LAAEARALAG KKGIHSAKES PAMHITDLTV SAAKKAKDFL PSLQRIRRIP AVVEYVLSGH
RFKLYIPKIT CSIAFSFSGV RCPGRGEPYS EEAISVMRRR IMQRDVEIEV ETVDRTGTFL
GSMWESRTNV ATVLLEAGLA KMQTSFGADR IAEAHLLEQA ERSAKNQKLK IWENYVEGEE
VSNGNTNTVE TRQKETLKVV VTEVLGGGRF YVQSAGDQKI ASIQNQLASL SIKDAPIIGS
FNPKRGDIVL AQFSLDNSWN RAMIVTAPRA AVQSPDEKFE VFYIDYGNQE TVPYSAIRPI
DPSVSAAPGL AQLCRLAYIK VPSLEDDFGP EAGEYLHTVT LGSGKEFKAV IEERDTSGGK
VKGQGTGTEF VVTLIAVDDE ISVNAAMLQE GIARMEKRQK WGHKGKQAAL DALEKFQEEA
RKSRIGIWQY GDIESDDEDT GPARKPAGGR R
