GLTB1_ARATH
ID GLTB1_ARATH Reviewed; 1622 AA.
AC Q9ZNZ7; P93649;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial {ECO:0000305};
DE EC=1.4.7.1 {ECO:0000269|PubMed:19223513};
DE AltName: Full=Fd-GOGAT 1 {ECO:0000303|PubMed:9596633};
DE Flags: Precursor;
GN Name=GLU1 {ECO:0000303|PubMed:9596633};
GN Synonyms=GLS1 {ECO:0000303|PubMed:9596633};
GN OrderedLocusNames=At5g04140 {ECO:0000312|Araport:AT5G04140};
GN ORFNames=F21E1_60 {ECO:0000312|EMBL:CAC05496.1};
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 [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=9057836; DOI=10.1111/j.1432-1033.1997.00708.x;
RA Suzuki A., Rothstein S.;
RT "Structure and regulation of ferredoxin-dependent glutamase synthase from
RT Arabidopsis thaliana. Cloning of cDNA expression in different tissues of
RT wild-type and gltS mutant strains, and light induction.";
RL Eur. J. Biochem. 243:708-718(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY LIGHT AND SUGAR.
RC STRAIN=cv. Columbia;
RX PubMed=9596633; DOI=10.2307/3870661;
RA Coschigano K.T., Melo-Oliveira R., Lim J., Coruzzi G.M.;
RT "Arabidopsis gls mutants and distinct Fd-GOGAT genes. Implications for
RT photorespiration and primary nitrogen assimilation.";
RL Plant Cell 10:741-752(1998).
RN [3]
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 [4]
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 [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19555410; DOI=10.1111/j.1742-4658.2009.07114.x;
RA Potel F., Valadier M.H., Ferrario-Mery S., Grandjean O., Morin H.,
RA Gaufichon L., Boutet-Mercey S., Lothier J., Rothstein S.J., Hirose N.,
RA Suzuki A.;
RT "Assimilation of excess ammonium into amino acids and nitrogen
RT translocation in Arabidopsis thaliana--roles of glutamate synthases and
RT carbamoylphosphate synthetase in leaves.";
RL FEBS J. 276:4061-4076(2009).
RN [6]
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 [7]
RP INTERACTION WITH SHM1, SUBCELLULAR LOCATION, DUAL TARGETING, FUNCTION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-1270, AND DISRUPTION PHENOTYPE.
RX PubMed=19223513; DOI=10.1105/tpc.108.063289;
RA Jamai A., Salome P.A., Schilling S.H., Weber A.P., McClung C.R.;
RT "Arabidopsis photorespiratory serine hydroxymethyltransferase activity
RT requires the mitochondrial accumulation of ferredoxin-dependent glutamate
RT synthase.";
RL Plant Cell 21:595-606(2009).
RN [8]
RP FUNCTION.
RX PubMed=19468822; DOI=10.1007/s00726-009-0303-2;
RA Ishizaki T., Ohsumi C., Totsuka K., Igarashi D.;
RT "Analysis of glutamate homeostasis by overexpression of Fd-GOGAT gene in
RT Arabidopsis thaliana.";
RL Amino Acids 38:943-950(2010).
RN [9]
RP INDUCTION BY GATA21/GNC AND GATA22/CGA1.
RX PubMed=22102866; DOI=10.1371/journal.pone.0026765;
RA Hudson D., Guevara D., Yaish M.W., Hannam C., Long N., Clarke J.D.,
RA Bi Y.-M., Rothstein S.J.;
RT "GNC and CGA1 modulate chlorophyll biosynthesis and glutamate synthase
RT (GLU1/Fd-GOGAT) expression in Arabidopsis.";
RL PLoS ONE 6:E26765-E26765(2011).
CC -!- FUNCTION: Involved in glutamate biosynthesis in leaf. Required for the
CC reassimilation of ammonium ions generated during photorespiration.
CC {ECO:0000269|PubMed:19223513, ECO:0000269|PubMed:19468822,
CC ECO:0000269|PubMed:19555410, ECO:0000269|PubMed:9596633}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-
CC oxoglutarate + 2 H(+) + L-glutamine + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:12128, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58359; EC=1.4.7.1;
CC Evidence={ECO:0000269|PubMed:19223513};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12130;
CC Evidence={ECO:0000269|PubMed:19223513};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:Q43155};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q43155};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P09831};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q43155};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC route): step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with SHM1. {ECO:0000269|PubMed:19223513}.
CC -!- INTERACTION:
CC Q9ZNZ7; Q9SZJ5: SHM1; NbExp=2; IntAct=EBI-2292564, EBI-2292536;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19223513}. Mitochondrion matrix
CC {ECO:0000269|PubMed:19223513}. Note=Dual targeting is supposed to
CC depend on alternative initiation: MET-1 or MET-3 for chloroplast or
CC mitochondrion location, respectively. {ECO:0000269|PubMed:19223513}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Short;
CC IsoId=Q9ZNZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q9ZNZ7-2; Sequence=VSP_046513;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. High expression in the
CC leaf mesophyll and phloem companion cell-sieve element complex.
CC {ECO:0000269|PubMed:19555410, ECO:0000269|PubMed:9596633}.
CC -!- INDUCTION: Up-regulated by GATA21/GNC and GATA22/CGA1. Induced by light
CC or sucrose. {ECO:0000269|PubMed:22102866, ECO:0000269|PubMed:9596633}.
CC -!- DISRUPTION PHENOTYPE: Displays photorespiratory chlorosis when grown at
CC ambient CO2. {ECO:0000269|PubMed:19223513}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; Y09667; CAA70862.1; -; mRNA.
DR EMBL; U39287; AAC78551.1; -; mRNA.
DR EMBL; AL391716; CAC05496.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90703.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90704.1; -; Genomic_DNA.
DR RefSeq; NP_568134.1; NM_120496.3. [Q9ZNZ7-1]
DR RefSeq; NP_850763.1; NM_180432.2. [Q9ZNZ7-2]
DR AlphaFoldDB; Q9ZNZ7; -.
DR SMR; Q9ZNZ7; -.
DR BioGRID; 15572; 14.
DR IntAct; Q9ZNZ7; 2.
DR STRING; 3702.AT5G04140.2; -.
DR MEROPS; C44.951; -.
DR iPTMnet; Q9ZNZ7; -.
DR MetOSite; Q9ZNZ7; -.
DR PaxDb; Q9ZNZ7; -.
DR PRIDE; Q9ZNZ7; -.
DR ProteomicsDB; 248543; -. [Q9ZNZ7-1]
DR EnsemblPlants; AT5G04140.1; AT5G04140.1; AT5G04140. [Q9ZNZ7-1]
DR EnsemblPlants; AT5G04140.2; AT5G04140.2; AT5G04140. [Q9ZNZ7-2]
DR GeneID; 830292; -.
DR Gramene; AT5G04140.1; AT5G04140.1; AT5G04140. [Q9ZNZ7-1]
DR Gramene; AT5G04140.2; AT5G04140.2; AT5G04140. [Q9ZNZ7-2]
DR KEGG; ath:AT5G04140; -.
DR Araport; AT5G04140; -.
DR TAIR; locus:2146718; AT5G04140.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; Q9ZNZ7; -.
DR OMA; LKTGWDV; -.
DR OrthoDB; 126283at2759; -.
DR BioCyc; ARA:AT5G04140-MON; -.
DR BRENDA; 1.4.7.1; 399.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR PRO; PR:Q9ZNZ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZNZ7; baseline and differential.
DR Genevisible; Q9ZNZ7; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IDA:TAIR.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IBA:GO_Central.
DR GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009853; P:photorespiration; IMP:TAIR.
DR GO; GO:0080114; P:positive regulation of glycine hydroxymethyltransferase activity; IDA:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Alternative splicing; Amino-acid biosynthesis; Chloroplast; FAD;
KW Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..105
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 106..1622
FT /note="Ferredoxin-dependent glutamate synthase 1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000011614"
FT DOMAIN 106..505
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 106
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1184..1241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1237
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1243
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1248
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT VAR_SEQ 92
FT /note="Q -> QVRFFTDINFTNTQRAKFHPLWGSFKQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9057836"
FT /id="VSP_046513"
FT MUTAGEN 1270
FT /note="L->F: In glu1-201; Abolishes interaction with SHM1.
FT Displays photorespiratory chlorosis when grown at ambient
FT CO2."
FT /evidence="ECO:0000269|PubMed:19223513"
FT CONFLICT 96
FT /note="L -> W (in Ref. 2; AAC78551)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="G -> R (in Ref. 2; AAC78551)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> C (in Ref. 1; CAA70862)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..624
FT /note="EGLV -> KVWF (in Ref. 1; CAA70862)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="A -> T (in Ref. 1; CAA70862)"
FT /evidence="ECO:0000305"
FT CONFLICT 1473..1474
FT /note="IF -> DI (in Ref. 1; CAA70862)"
FT /evidence="ECO:0000305"
FT CONFLICT 1585
FT /note="E -> K (in Ref. 2; AAC78551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1622 AA; 176752 MW; FAE7D097490F8A97 CRC64;
MAMQSLSPVP KLLSTTPSSV LSSDKNFFFV DFVGLYCKSK RTRRRLRGDS SSSSRSSSSL
SRLSSVRAVI DLERVHGVSE KDLSSPSALR PQVANLEDIL SERGACGVGF IANLDNIPSH
GVVKDALIAL GCMEHRGGCG ADNDSGDGSG LMSSIPWDFF NVWAKEQSLA PFDKLHTGVG
MIFLPQDDTF MQEAKQVIEN IFEKEGLQVL GWREVPVNVP IVGKNARETM PNIQQVFVKI
AKEDSTDDIE RELYICRKLI ERAVATESWG TELYFCSLSN QTIVYKGMLR SEALGLFYLD
LQNELYESPF AIYHRRYSTN TSPRWPLAQP MRFLGHNGEI NTIQGNLNWM QSREASLKAA
VWNGRENEIR PFGNPRGSDS ANLDSAAEIM IRSGRTPEEA LMILVPEAYK NHPTLSVKYP
EVVDFYDYYK GQMEAWDGPA LLLFSDGKTV GACLDRNGLR PARYWRTSDN FVYVASEVGV
VPVDEAKVTM KGRLGPGMMI AVDLVNGQVY ENTEVKKRIS SFNPYGKWIK ENSRFLKPVN
FKSSTVMENE EILRSQQAFG YSSEDVQMVI ESMASQGKEP TFCMGDDIPL AGLSQRPHML
YDYFKQRFAQ VTNPAIDPLR EGLVMSLEVN IGKRGNILEL GPENASQVIL SNPVLNEGAL
EELMKDQYLK PKVLSTYFDI RKGVEGSLQK ALYYLCEAAD DAVRSGSQLL VLSDRSDRLE
PTRPSIPIML AVGAVHQHLI QNGLRMSASI VADTAQCFST HHFACLVGYG ASAVCPYLAL
ETCRQWRLSN KTVAFMRNGK IPTVTIEQAQ KNYTKAVNAG LLKILSKMGI SLLSSYCGAQ
IFEIYGLGQD VVDLAFTGSV SKISGLTFDE LARETLSFWV KAFSEDTTKR LENFGFIQFR
PGGEYHSNNP EMSKLLHKAV REKSETAYAV YQQHLSNRPV NVLRDLLEFK SDRAPIPVGK
VEPAVAIVQR FCTGGMSLGA ISRETHEAIA IAMNRIGGKS NSGEGGEDPI RWKPLTDVVD
GYSPTLPHLK GLQNGDIATS AIKQVASGRF GVTPTFLVNA DQLEIKVAQG AKPGEGGQLP
GKKVSAYIAR LRSSKPGVPL ISPPPHHDIY SIEDLAQLIF DLHQINPNAK VSVKLVAEAG
IGTVASGVAK GNADIIQISG HDGGTGASPI SSIKHAGGPW ELGLTETHQT LIANGLRERV
ILRVDGGLKS GVDVLMAAAM GADEYGFGSL AMIATGCVMA RICHTNNCPV GVASQREELR
ARFPGVPGDL VNYFLYVAEE VRGILAQLGY NSLDDIIGRT ELLRPRDISL VKTQHLDLSY
LLSSVGTPSL SSTEIRKQEV HTNGPVLDDD ILADPLVIDA IENEKVVEKT VKICNVDRAA
CGRVAGVIAK KYGDTGFAGQ VNLTFLGSAG QSFGCFLIPG MNIRLIGESN DYVGKGMAGG
EIVVTPVEKI GFVPEEATIV GNTCLYGATG GQIFARGKAG ERFAVRNSLA EAVVEGTGDH
CCEYMTGGCV VVLGKVGRNV AAGMTGGLAY LLDEDDTLLP KINREIVKIQ RVTAPAGELQ
LKSLIEAHVE KTGSSKGATI LNEWEKYLPL FWQLVPPSEE DTPEASAAYV RTSTGEVTFQ
SA
