UAH_ARATH
ID UAH_ARATH Reviewed; 476 AA.
AC Q8VXY9; Q9FIY0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ureidoglycolate hydrolase {ECO:0000303|PubMed:23940254};
DE Short=AtUAH {ECO:0000303|PubMed:23940254};
DE EC=3.5.1.116 {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:25020232};
DE AltName: Full=Allantoate amidohydrolase 2 {ECO:0000303|PubMed:19935661};
DE Short=AtAHH2 {ECO:0000303|PubMed:19935661};
DE AltName: Full=Ureidoglycolate amidohydrolase {ECO:0000303|PubMed:23940254};
DE Flags: Precursor;
GN Name=UAH {ECO:0000303|PubMed:23940254};
GN Synonyms=AAH2 {ECO:0000303|PubMed:19935661};
GN OrderedLocusNames=At5g43600 {ECO:0000312|Araport:AT5G43600};
GN ORFNames=K9D7.10 {ECO:0000312|EMBL:BAB11623.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19935661; DOI=10.1038/nchembio.265;
RA Werner A.K., Romeis T., Witte C.P.;
RT "Ureide catabolism in Arabidopsis thaliana and Escherichia coli.";
RL Nat. Chem. Biol. 6:19-21(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23940254; DOI=10.1104/pp.113.224261;
RA Werner A.K., Medina-Escobar N., Zulawski M., Sparkes I.A., Cao F.Q.,
RA Witte C.P.;
RT "The ureide-degrading reactions of purine ring catabolism employ three
RT amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice.";
RL Plant Physiol. 163:672-681(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 50-476 IN COMPLEX WITH SUBSTRATES
RP AND MANGANESE, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF HIS-138; ASP-149; GLU-183; GLU-184;
RP HIS-254; GLN-257; HIS-290; ASN-340; ASP-351; ARG-353; TYR-423; HIS-424 AND
RP HIS-448.
RX PubMed=25020232; DOI=10.1016/j.jmb.2014.06.017;
RA Shin I., Han K., Rhee S.;
RT "Structural insights into the substrate specificity of (s)-ureidoglycolate
RT amidohydrolase and its comparison with allantoate amidohydrolase.";
RL J. Mol. Biol. 426:3028-3040(2014).
CC -!- FUNCTION: Involved in the catabolism of purine nucleotides. Can use
CC (S)-ureidoglycolate as substrate, but not (R)-ureidoglycolate or
CC allantoate. The sequential activity of AAH, UGLYAH and UAH allows a
CC complete purine breakdown without the intermediate generation of urea.
CC {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:23940254,
CC ECO:0000269|PubMed:25020232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-ureidoglycolate + 2 H(+) + H2O = CO2 + glyoxylate + 2
CC NH4(+); Xref=Rhea:RHEA:19809, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57296; EC=3.5.1.116;
CC Evidence={ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:25020232};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25020232};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:25020232};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:25020232};
CC Note=Binds 2 manganese ions per subunit. Can also use nickel and cobalt
CC with lower activity. {ECO:0000269|PubMed:25020232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.7 uM for (S)-ureidoglycolate {ECO:0000269|PubMed:19935661};
CC KM=11.3 uM for (S)-ureidoglycolate (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:25020232};
CC Note=kcat is 1.43 sec(-1) with (S)-ureidoglycolate as substrate (at
CC pH 8.5 and 30 degrees Celsius) (PubMed:25020232). kcat is 7.9 sec(-1)
CC for (S)-ureidoglycolate (PubMed:19935661).
CC {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:25020232};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; glyoxylate
CC from (S)-ureidoglycolate: step 1/1. {ECO:0000269|PubMed:19935661,
CC ECO:0000269|PubMed:25020232}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25020232}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:23940254}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show a slight reduction of growth on a
CC medium containing allantoin as the sole nitrogen source and accumulate
CC ureidoglycolate. {ECO:0000269|PubMed:23940254}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11623.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB016875; BAB11623.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94986.1; -; Genomic_DNA.
DR EMBL; AY074343; AAL67039.1; -; mRNA.
DR EMBL; AY091387; AAM14326.1; -; mRNA.
DR EMBL; AK230338; BAF02137.1; -; mRNA.
DR RefSeq; NP_199173.2; NM_123726.4.
DR PDB; 4PXB; X-ray; 1.90 A; A/B=50-476.
DR PDB; 4PXC; X-ray; 1.89 A; A/B=50-476.
DR PDB; 4PXE; X-ray; 1.45 A; A/B=50-476.
DR PDBsum; 4PXB; -.
DR PDBsum; 4PXC; -.
DR PDBsum; 4PXE; -.
DR AlphaFoldDB; Q8VXY9; -.
DR SMR; Q8VXY9; -.
DR BioGRID; 19630; 1.
DR STRING; 3702.AT5G43600.1; -.
DR PaxDb; Q8VXY9; -.
DR PRIDE; Q8VXY9; -.
DR ProteomicsDB; 228616; -.
DR EnsemblPlants; AT5G43600.1; AT5G43600.1; AT5G43600.
DR GeneID; 834380; -.
DR Gramene; AT5G43600.1; AT5G43600.1; AT5G43600.
DR KEGG; ath:AT5G43600; -.
DR Araport; AT5G43600; -.
DR TAIR; locus:2158342; AT5G43600.
DR eggNOG; ENOG502QPR4; Eukaryota.
DR HOGENOM; CLU_024588_6_0_1; -.
DR InParanoid; Q8VXY9; -.
DR OMA; IWPHGRW; -.
DR OrthoDB; 529725at2759; -.
DR PhylomeDB; Q8VXY9; -.
DR BioCyc; ARA:AT5G43600-MON; -.
DR BioCyc; MetaCyc:AT5G43600-MON; -.
DR BRENDA; 3.5.1.116; 399.
DR UniPathway; UPA00395; UER00656.
DR PRO; PR:Q8VXY9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VXY9; baseline and differential.
DR Genevisible; Q8VXY9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004848; F:ureidoglycolate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0000256; P:allantoin catabolic process; IDA:TAIR.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IDA:TAIR.
DR GO; GO:0010136; P:ureide catabolic process; IDA:TAIR.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..476
FT /note="Ureidoglycolate hydrolase"
FT /id="PRO_0000423446"
FT REGION 276..391
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:25020232"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 184
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 423..424
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 448
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC,
FT ECO:0007744|PDB:4PXE"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25020232,
FT ECO:0007744|PDB:4PXB, ECO:0007744|PDB:4PXC"
FT SITE 299
FT /note="Necessary for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q53389"
FT MUTAGEN 138
FT /note="H->A: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 149
FT /note="D->A,N: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 183
FT /note="E->A,D,Q: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 184
FT /note="E->A: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 254
FT /note="H->A: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 257
FT /note="Q->A,E: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 257
FT /note="Q->N: Strongly reduced substrate affinity and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 290
FT /note="H->A,N: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 290
FT /note="H->Q: Strongly reduced substrate affinity and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 340
FT /note="N->A: Strongly reduced substrate affinity and
FT abolished enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 340
FT /note="N->D: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 351
FT /note="D->A: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 353
FT /note="R->A,K: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 423
FT /note="Y->A,G: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 423
FT /note="Y->F: Reduced substrate affinity and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 424
FT /note="H->N: Reduced substrate affinity and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT MUTAGEN 448
FT /note="H->A: Impaired enzyme activity."
FT /evidence="ECO:0000269|PubMed:25020232"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4PXE"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:4PXE"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 326..336
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 344..356
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 357..378
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 381..390
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:4PXE"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:4PXE"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:4PXE"
FT HELIX 456..475
FT /evidence="ECO:0007829|PDB:4PXE"
SQ SEQUENCE 476 AA; 51487 MW; CBAEB842B3B0BC0F CRC64;
MESLKRFLCS IALLLISLLL PSSLAQQQQH ESIRTMEDFS GYPIHEPGQF GSINLASSLS
VDAPGLQNQI DELSSFSDAP SPSVTRVLYT DKDVSARRYV KNLMALAGLT VREDAVGNIF
GKWDGLEPNL PAVATGSHID AIPYSGKYDG VVGVLGAIEA INVLKRSGFK PKRSLEIILF
TSEEPTRFGI SCLGSRLLAG SKELAEALKT TVVDGQNVSF IEAARSAGYA EDKDDDLSSV
FLKKGSYFAF LELHIEQGPI LEDEGLDIGV VTAIAAPASL KVEFEGNGGH AGAVLMPYRN
DAGLAAAELA LAVEKHVLES ESIDTVGTVG ILELHPGAIN SIPSKSHLEI DTRDIDEARR
NTVIKKIQES ANTIAKKRKV KLSEFKIVNQ DPPALSDKLV IKKMAEAATE LNLSHKMMIS
RAYHDSLFMA RISPMGMIFI PCYKGYSHKP EEYSSPEDMA NGVKVLSLTL AKLSLD
