SRFR1_ARATH
ID SRFR1_ARATH Reviewed; 1052 AA.
AC F4JS25; Q8GYX1; Q9SZU6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Suppressor of RPS4-RLD 1 {ECO:0000303|PubMed:15469494};
DE AltName: Full=Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 5 {ECO:0000303|PubMed:20862316};
DE Short=AtSNC5 {ECO:0000303|PubMed:20862316};
GN Name=SRFR1 {ECO:0000303|PubMed:15469494};
GN Synonyms=SNC5 {ECO:0000303|PubMed:20862316};
GN OrderedLocusNames=At4g37460 {ECO:0000312|Araport:AT4G37460};
GN ORFNames=F6G17.110 {ECO:0000312|EMBL:CAB38213.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP FUNCTION.
RC STRAIN=cv. RLD;
RX PubMed=15469494; DOI=10.1111/j.1365-313x.2004.02213.x;
RA Kwon S.I., Koczan J.M., Gassmann W.;
RT "Two Arabidopsis srfr (suppressor of rps4-RLD) mutants exhibit avrRps4-
RT specific disease resistance independent of RPS4.";
RL Plant J. 40:366-375(2004).
RN [6]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. RLD;
RX PubMed=18774967; DOI=10.1111/j.1365-313x.2008.03669.x;
RA Kwon S.I., Kim S.H., Bhattacharjee S., Noh J.J., Gassmann W.;
RT "SRFR1, a suppressor of effector-triggered immunity, encodes a conserved
RT tetratricopeptide repeat protein with similarity to transcriptional
RT repressors.";
RL Plant J. 57:109-119(2009).
RN [7]
RP FUNCTION.
RC STRAIN=cv. RLD;
RX PubMed=19649196; DOI=10.4161/psb.4.2.7682;
RA Kim S.H., Kwon S.I., Bhattacharjee S., Gassmann W.;
RT "Regulation of defense gene expression by Arabidopsis SRFR1.";
RL Plant Signal. Behav. 4:149-150(2009).
RN [8]
RP FUNCTION.
RX PubMed=19525323; DOI=10.1104/pp.109.139238;
RA Kim S.H., Kwon S.I., Saha D., Anyanwu N.C., Gassmann W.;
RT "Resistance to the Pseudomonas syringae effector HopA1 is governed by the
RT TIR-NBS-LRR protein RPS6 and is enhanced by mutations in SRFR1.";
RL Plant Physiol. 150:1723-1732(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH SGT1.
RX PubMed=20862316; DOI=10.1371/journal.ppat.1001111;
RA Li Y., Li S., Bi D., Cheng Y.T., Li X., Zhang Y.;
RT "SRFR1 negatively regulates plant NB-LRR resistance protein accumulation to
RT prevent autoimmunity.";
RL PLoS Pathog. 6:E1001111-E1001111(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SNC1 AND RPS4.
RX PubMed=21079790; DOI=10.1371/journal.ppat.1001172;
RA Kim S.H., Gao F., Bhattacharjee S., Adiasor J.A., Nam J.C., Gassmann W.;
RT "The Arabidopsis resistance-like gene SNC1 is activated by mutations in
RT SRFR1 and contributes to resistance to the bacterial effector AvrRps4.";
RL PLoS Pathog. 6:E1001172-E1001172(2010).
RN [11]
RP FUNCTION, INTERACTION WITH EDS1, AND SUBCELLULAR LOCATION.
RX PubMed=22158819; DOI=10.1126/science.1211592;
RA Bhattacharjee S., Halane M.K., Kim S.H., Gassmann W.;
RT "Pathogen effectors target Arabidopsis EDS1 and alter its interactions with
RT immune regulators.";
RL Science 334:1405-1408(2011).
RN [12]
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 [13]
RP INTERACTION WITH TCP8; TCP14; TCP15; TCP20; TCP22 AND TCP23.
RX PubMed=24689742; DOI=10.1111/tpj.12527;
RA Kim S.H., Son G.H., Bhattacharjee S., Kim H.J., Nam J.C., Nguyen P.D.,
RA Hong J.C., Gassmann W.;
RT "The Arabidopsis immune adaptor SRFR1 interacts with TCP transcription
RT factors that redundantly contribute to effector-triggered immunity.";
RL Plant J. 78:978-989(2014).
CC -!- FUNCTION: Negative regulator of effector-triggered immunity associated
CC with the EDS1 resistance pathway (PubMed:15469494, PubMed:18774967,
CC PubMed:19649196, PubMed:19525323, PubMed:20862316, PubMed:21079790).
CC May localize its interactors to a microsomal membrane
CC (PubMed:22158819). May therefore negatively regulate RPS4 and SNC1
CC translocation to the nucleus (PubMed:21079790). Contributes to the
CC regulation of RPS2 and RPS4 protein levels and negatively regulates
CC SNC1 stability (PubMed:20862316). {ECO:0000269|PubMed:15469494,
CC ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:19525323,
CC ECO:0000269|PubMed:19649196, ECO:0000269|PubMed:20862316,
CC ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22158819}.
CC -!- SUBUNIT: Multimer (PubMed:18774967). Interacts with EDS1
CC (PubMed:22158819). Interacts with SNC1 and RPS4 (PubMed:21079790).
CC Interacts (via TPR domain) with SGT1 (via TPR domain)
CC (PubMed:20862316). Interacts with the TCP transcription factors TCP8,
CC TCP14, TCP15, TCP20, TCP22 and TCP23 (PubMed:24689742).
CC {ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:20862316,
CC ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22158819,
CC ECO:0000269|PubMed:24689742}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18774967,
CC ECO:0000269|PubMed:21079790}. Cytoplasm {ECO:0000269|PubMed:18774967}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:18774967}. Membrane
CC {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Microsome
CC {ECO:0000269|PubMed:21079790}. Note=Found in microsomes when
CC interacting with SNC1 and RPS4. {ECO:0000269|PubMed:21079790}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JS25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JS25-2; Sequence=VSP_057256, VSP_057257;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Not detected in very young flowers and
CC older siliques. {ECO:0000269|PubMed:18774967}.
CC -!- DISRUPTION PHENOTYPE: Severe stunting in cv. Columbia.
CC {ECO:0000269|PubMed:21079790}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38213.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80411.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035601; CAB38213.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161591; CAB80411.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86797.1; -; Genomic_DNA.
DR EMBL; BT005966; AAO64901.1; -; mRNA.
DR EMBL; AK117340; BAC42010.1; -; mRNA.
DR PIR; T04740; T04740.
DR RefSeq; NP_195462.3; NM_119910.4. [F4JS25-1]
DR AlphaFoldDB; F4JS25; -.
DR SMR; F4JS25; -.
DR BioGRID; 15182; 11.
DR IntAct; F4JS25; 3.
DR STRING; 3702.AT4G37460.1; -.
DR iPTMnet; F4JS25; -.
DR PaxDb; F4JS25; -.
DR PRIDE; F4JS25; -.
DR ProteomicsDB; 226870; -. [F4JS25-1]
DR EnsemblPlants; AT4G37460.1; AT4G37460.1; AT4G37460. [F4JS25-1]
DR GeneID; 829901; -.
DR Gramene; AT4G37460.1; AT4G37460.1; AT4G37460. [F4JS25-1]
DR KEGG; ath:AT4G37460; -.
DR Araport; AT4G37460; -.
DR TAIR; locus:2126347; AT4G37460.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_014101_0_0_1; -.
DR InParanoid; F4JS25; -.
DR OMA; SWHDVYS; -.
DR PRO; PR:F4JS25; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JS25; baseline and differential.
DR Genevisible; F4JS25; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:TAIR.
DR GO; GO:0060090; F:molecular adaptor activity; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR044650; SRFR1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44749; PTHR44749; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Microsome; Nucleus; Plant defense;
KW Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1052
FT /note="Suppressor of RPS4-RLD 1"
FT /id="PRO_0000431367"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 39..72
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 74..106
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 297..330
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 331..364
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 365..398
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 400..432
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 433..466
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 468..500
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REPEAT 502..534
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT REPEAT 535..567
FT /note="TPR 10"
FT /evidence="ECO:0000255"
FT REPEAT 569..591
FT /note="TPR 11"
FT /evidence="ECO:0000255"
FT REGION 131..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..136
FT /evidence="ECO:0000255"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 881..883
FT /note="KRL -> WVC (in isoform 2)"
FT /id="VSP_057256"
FT VAR_SEQ 884..1052
FT /note="Missing (in isoform 2)"
FT /id="VSP_057257"
SQ SEQUENCE 1052 AA; 118107 MW; D20D45A7068FDAEA CRC64;
MATATATSER FELAKHCSSR NWSKAIRVLD SLLAKESSIL DICNRAFCYN QLELHKHVIK
DCDKALLLEP FAIQAFILKG RALLALGRKQ EAVLVLEQGY KSALQQTADV KQLLELEELL
KDARREIDGI LKSHATESPQ ETPAYHSEKS DEKSDKLDNH ESGASSNGNS HESSSELGEQ
SKIVSFSKVA SKASKQSDGN SDLCNGSVYK EKENGKCGSQ INGYYESCKP CNGSDLHDNL
AESSDRFGEL SINGNKISIK SSKMSHKAEA RCGISDESRK NKKYTIARIS GTHSISVDFR
LSRGIAQVNE GNYTKAISIF DKVLKEEPTY PEALIGRGTA YAFQRELESA IADFTKAIQS
NPAASEAWKR RGQARAALGE YVEAVEDLTK ALVFEPNSPD VLHERGIVNF KSKDFTAAVK
DLSICLKQEK DNKSAYTYLG LAFASLGEYK KAEEAHLKSI QLDSNYLEAW LHLAQFYQEL
ADHCKALECI EQVLQVDNRV WKAYHLRGLV FHGLGEHRKA IQELSIGLSI ENTIECLYLR
GSCYHAVGEY RDAVKDYDAT VDVELDAVEK FVLQCLAFYQ KELALYTASK VSSEFLCFDI
DGDIDPMFKE YWCKRLHPKN VCEKVYRQPP LRESLKKGKL KKQDLAITKQ KANILRFADL
IGKRIQYDCP GFLPNKRQHR MAGLAVIEIA QKVSKAWRIE WRNSTKGTTK NGKKNRRRER
TNILSQNRGG AGCSSSSFSE TSTGYASLED RSSGRSILSW QDVYSPAVRW RQISEPCDPV
VWVNKLSEEF NSGFGSHTPM VLGQAKVVRY FPNYERTLTL AKSIIKDKLS VRSKKDKVID
LSKDEKIEKI MRAETCDELH NIVGEDFWVA TWCDSTGSEG KRLEGTRITC IQKPGRLGYD
FSIRTPCTPA RWSDFDEEMT SAWEALCTAY CGENYGSTEL DALETVRDAI LRMTYYWYNF
MPLARGTAVT GFVVLLGLLL AANMEFTETI PKGLQIDWEA ILNVEPGSFV DSVKSWLYPS
LKINTSWRDH TEISSAFSTT GAVVAALSTY ND
