ISS1_ARATH
ID ISS1_ARATH Reviewed; 394 AA.
AC Q9C969;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aromatic aminotransferase ISS1 {ECO:0000303|PubMed:26163189};
DE EC=2.6.1.27 {ECO:0000269|PubMed:26163189};
DE EC=2.6.1.5 {ECO:0000269|PubMed:26163189};
DE EC=2.6.1.88 {ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189};
DE AltName: Full=Methionine aminotransferase ISS1 {ECO:0000305};
DE AltName: Full=Phenylalanine aminotransferase ISS1 {ECO:0000305};
DE AltName: Full=Protein INDOLE SEVERE SENSITIVE 1 {ECO:0000303|PubMed:26163189};
DE AltName: Full=Protein REVERSAL OF SAV3 PHENOTYPE 1 {ECO:0000303|PubMed:23377040};
DE AltName: Full=Tryptophan aminotransferase ISS1 {ECO:0000305};
DE AltName: Full=Tyrosine aminotransferase ISS1 {ECO:0000305};
GN Name=ISS1 {ECO:0000303|PubMed:26163189};
GN Synonyms=VAS1 {ECO:0000303|PubMed:23377040};
GN OrderedLocusNames=At1g80360 {ECO:0000312|Araport:AT1G80360};
GN ORFNames=F5I6.11 {ECO:0000312|EMBL:AAG52437.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-66; LEU-77; GLY-179;
RP CYS-219 AND ALA-269, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=23377040; DOI=10.1038/nchembio.1178;
RA Zheng Z., Guo Y., Novak O., Dai X., Zhao Y., Ljung K., Noel J.P., Chory J.;
RT "Coordination of auxin and ethylene biosynthesis by the aminotransferase
RT VAS1.";
RL Nat. Chem. Biol. 9:244-246(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-362, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=26163189; DOI=10.1534/genetics.115.180356;
RA Pieck M., Yuan Y., Godfrey J., Fisher C., Zolj S., Vaughan D., Thomas N.,
RA Wu C., Ramos J., Lee N., Normanly J., Celenza J.L.;
RT "Auxin and tryptophan homeostasis are facilitated by the ISS1/VAS1 aromatic
RT aminotransferase in Arabidopsis.";
RL Genetics 201:185-199(2015).
CC -!- FUNCTION: Coordinates and prevents auxin (IAA) and ethylene
CC biosynthesis, thus regulating auxin homeostasis in young seedlings
CC (PubMed:23377040, PubMed:26163189). Shows aminotransferase activity
CC with methionine; can use the ethylene biosynthetic intermediate L-
CC methionine (L-Met) as an amino donor and the auxin biosynthetic
CC intermediate, indole-3-pyruvic acid (3-IPA) as an amino acceptor to
CC produce L-tryptophan (L-Trp) and 2-oxo-4-methylthiobutyric acid (KMBA)
CC (PubMed:23377040). Can also use tryptophan (Trp), phenylalanine (Phe),
CC and tyrosine (Tyr) as substrates. Regulates tryptophan (Trp)
CC homeostasis and catabolism in mature plants. Also possibly involved in
CC the metabolism of other aromatic amino acids and phenylpropanoid
CC homeostasis (PubMed:26163189). {ECO:0000269|PubMed:23377040,
CC ECO:0000269|PubMed:26163189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-methionine = 4-methylsulfanyl-2-
CC oxobutanoate + an L-alpha-amino acid; Xref=Rhea:RHEA:31763,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:35179, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59869; EC=2.6.1.88;
CC Evidence={ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:14093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:29985, ChEBI:CHEBI:57912; EC=2.6.1.27;
CC Evidence={ECO:0000269|PubMed:26163189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC Evidence={ECO:0000269|PubMed:26163189};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00509};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for indole-3-pyruvic acid (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:23377040};
CC KM=630 uM for L-Met (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:23377040};
CC KM=2600 uM for L-Phe (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:23377040};
CC Vmax=1 umol/min/ug enzyme with indole-3-pyruvic acid as substrate (at
CC pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:23377040};
CC Vmax=0.82 umol/min/ug enzyme with L-Met as substrate (at pH 8 and 23
CC degrees Celsius) {ECO:0000269|PubMed:23377040};
CC Vmax=0.14 umol/min/ug enzyme with L-Phe as substrate (at pH 8 and 23
CC degrees Celsius) {ECO:0000269|PubMed:23377040};
CC Note=kcat is 2.5 min(-1) with indole-3-pyruvic acid as substrate.
CC kcat is 1.9 min(-1) with L-Met as substrate. kcat is 3.16 min(-1)
CC with L-Phe as substrate (at pH 8.5 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:23377040};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00509}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23377040}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and flowers.
CC {ECO:0000269|PubMed:23377040}.
CC -!- DISRUPTION PHENOTYPE: Suppressor of sav3 mutant plants leading to
CC rescued hypocotyl elongation in response to shade and restored auxin
CC biosynthetic pathway. In continuous white light, elongated hypocotyls
CC and petioles, with increased leaf hyponasty, decreased leaf area, and
CC accelerated leaf senescence as well as early flowering. Increases
CC levels of auxin (IAA), indole-3-pyruvic acid (3-IPA) and the ethylene
CC precursor 1-aminocyclopropane-1-carboxylate (ACC) (PubMed:23377040).
CC Indole-dependent auxin (IAA) overproduction phenotypes including leaf
CC epinasty and adventitious rooting. In contrast to normal plants, uses
CC primarily Trp-independent (Trp-I) IAA synthesis when grown on indole-
CC supplemented medium, but uses primarily Trp-dependent (Trp-D) IAA
CC synthesis when grown on unsupplemented medium. Accumulates strongly IAA
CC and Trp when grown on indole, probably due to loss of Trp catabolism.
CC Altered phenylpropanoid profile (PubMed:26163189).
CC {ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AC018848; AAG52437.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36391.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59817.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59818.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59819.1; -; Genomic_DNA.
DR EMBL; AY093159; AAM13158.1; -; mRNA.
DR EMBL; BT008854; AAP68293.1; -; mRNA.
DR PIR; C96835; C96835.
DR RefSeq; NP_001322147.1; NM_001334979.1.
DR RefSeq; NP_001322148.1; NM_001334980.1.
DR RefSeq; NP_001322149.1; NM_001334981.1.
DR RefSeq; NP_178152.1; NM_106685.5.
DR AlphaFoldDB; Q9C969; -.
DR SMR; Q9C969; -.
DR STRING; 3702.AT1G80360.1; -.
DR iPTMnet; Q9C969; -.
DR PaxDb; Q9C969; -.
DR PRIDE; Q9C969; -.
DR ProteomicsDB; 232231; -.
DR EnsemblPlants; AT1G80360.1; AT1G80360.1; AT1G80360.
DR EnsemblPlants; AT1G80360.2; AT1G80360.2; AT1G80360.
DR EnsemblPlants; AT1G80360.3; AT1G80360.3; AT1G80360.
DR EnsemblPlants; AT1G80360.4; AT1G80360.4; AT1G80360.
DR GeneID; 844376; -.
DR Gramene; AT1G80360.1; AT1G80360.1; AT1G80360.
DR Gramene; AT1G80360.2; AT1G80360.2; AT1G80360.
DR Gramene; AT1G80360.3; AT1G80360.3; AT1G80360.
DR Gramene; AT1G80360.4; AT1G80360.4; AT1G80360.
DR KEGG; ath:AT1G80360; -.
DR Araport; AT1G80360; -.
DR TAIR; locus:2034240; AT1G80360.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_017584_4_1_1; -.
DR InParanoid; Q9C969; -.
DR OMA; YFNHEMA; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q9C969; -.
DR BioCyc; ARA:AT1G80360-MON; -.
DR BioCyc; MetaCyc:AT1G80360-MON; -.
DR BRENDA; 2.6.1.57; 399.
DR BRENDA; 2.6.1.99; 399.
DR PRO; PR:Q9C969; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C969; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IDA:UniProtKB.
DR GO; GO:0009851; P:auxin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
DR GO; GO:0006555; P:methionine metabolic process; IDA:UniProtKB.
DR GO; GO:0010366; P:negative regulation of ethylene biosynthetic process; IMP:TAIR.
DR GO; GO:1901997; P:negative regulation of indoleacetic acid biosynthetic process via tryptophan; IDA:TAIR.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IMP:UniProtKB.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR GO; GO:0006569; P:tryptophan catabolic process; IMP:UniProtKB.
DR GO; GO:0006568; P:tryptophan metabolic process; IDA:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Auxin biosynthesis; Cytoplasm;
KW Ethylene biosynthesis; Phenylpropanoid metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase; Tryptophan catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..394
FT /note="Aromatic aminotransferase ISS1"
FT /id="PRO_0000440181"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 64
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 98..99
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 123
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 207
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 230..232
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT MUTAGEN 66
FT /note="P->L: In vas1-4; suppressor of sav3 mutant plants
FT leading to rescued hypocotyl elongation in response to
FT shade and restored auxin biosynthetic pathway."
FT /evidence="ECO:0000269|PubMed:23377040"
FT MUTAGEN 77
FT /note="L->F: In vas1-5; suppressor of sav3 mutant plants
FT leading to rescued hypocotyl elongation in response to
FT shade and restored auxin biosynthetic pathway."
FT /evidence="ECO:0000269|PubMed:23377040"
FT MUTAGEN 179
FT /note="G->D: In vas1-2; suppressor of sav3 mutant plants
FT leading to rescued hypocotyl elongation in response to
FT shade and restored auxin biosynthetic pathway. Increases
FT levels of auxin (IAA) and indole-3-pyruvic acid (3-IPA)."
FT /evidence="ECO:0000269|PubMed:23377040"
FT MUTAGEN 219
FT /note="C->Y: In vas1-7; suppressor of sav3 mutant plants
FT leading to rescued hypocotyl elongation in response to
FT shade and restored auxin biosynthetic pathway."
FT /evidence="ECO:0000269|PubMed:23377040"
FT MUTAGEN 269
FT /note="A->T: In vas1-8; suppressor of sav3 mutant plants
FT leading to rescued hypocotyl elongation in response to
FT shade and restored auxin biosynthetic pathway."
FT /evidence="ECO:0000269|PubMed:23377040"
FT MUTAGEN 362
FT /note="R->W: In iss1-2; indole-dependent auxin (IAA)
FT overproduction phenotypes including leaf epinasty and
FT adventitious rooting."
FT /evidence="ECO:0000269|PubMed:26163189"
SQ SEQUENCE 394 AA; 43762 MW; E848C65BAB140620 CRC64;
MGSFGMLSRR TLGTDMPVMA QIRSLMAELT NPMSLAQGVV HWQPPQKALE KVKELVWDPI
ISSYGPDEGL PELRQALLKK LREENKLTNS QVMVTAGANQ AFVNLVITLC DAGDSVVMFE
PYYFNSYMAF QMTGVTNIIV GPGQSDTLYP DADWLERTLS ESKPTPKVVT VVNPGNPSGT
YVPEPLLKRI AQICKDAGCW LIVDNTYEYF MYDGLKHCCV EGDHIVNVFS FSKTYGMMGW
RLGYIAYSER LDGFATELVK IQDNIPICAA IISQRLAVYA LEEGSGWITE RVKSLVKNRD
IVKEALEPLG KENVKGGEGA IYLWAKLPEG HRDDFKVVRW LAHRHGVVVI PGCASGSPGY
LRVSFGGLQE VEMRAAAARL RKGIEELLHH GMVE
