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Database: UniProt/SWISS-PROT
Entry: PARK7_CHICK
LinkDB: PARK7_CHICK
Original site: PARK7_CHICK 
ID   PARK7_CHICK             Reviewed;         189 AA.
AC   Q8UW59;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.124 {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE   AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            Short=DJ-1;
DE   Flags: Precursor;
GN   Name=PARK7 {ECO:0000250|UniProtKB:Q99497};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15976810; DOI=10.1038/sj.cdd.4401704;
RA   Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,
RA   Seino C., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full
RT   activities.";
RL   Cell Death Differ. 13:96-108(2006).
CC   -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC       deglycation of the Maillard adducts formed between amino groups of
CC       proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus,
CC       functions as a protein deglycase that repairs methylglyoxal- and
CC       glyoxal-glycated proteins, and releases repaired proteins and lactate
CC       or glycolate, respectively. Deglycates cysteine, arginine and lysine
CC       residues in proteins, and thus reactivates these proteins by reversing
CC       glycation by glyoxals. Acts on early glycation intermediates
CC       (hemithioacetals and aminocarbinols), preventing the formation of
CC       advanced glycation endproducts (AGE) that cause irreversible damage.
CC       Also functions as a nucleotide deglycase able to repair glycated
CC       guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA
CC       and RNA. Is thus involved in a major nucleotide repair system named
CC       guanine glycation repair (GG repair), dedicated to reversing
CC       methylglyoxal and glyoxal damage via nucleotide sanitization and direct
CC       nucleic acid repair. Also displays an apparent glyoxalase activity that
CC       in fact reflects its deglycase activity. Plays an important role in
CC       cell protection against oxidative stress and cell death acting as
CC       oxidative stress sensor and redox-sensitive chaperone and protease. It
CC       is involved in neuroprotective mechanisms as well as cell growth and
CC       transformation. Its involvement in protein repair could also explain
CC       other unrelated functions. Eliminates hydrogen peroxide and protects
CC       cells against hydrogen peroxide-induced cell death. Required for
CC       correct mitochondrial morphology and function as well as for autophagy
CC       of dysfunctional mitochondria. Regulates astrocyte inflammatory
CC       responses, may modulate lipid rafts-dependent endocytosis in astrocytes
CC       and neuronal cells. Binds to a number of mRNAs containing multiple
CC       copies of GG or CC motifs and partially inhibits their translation but
CC       dissociates following oxidative stress. Metal-binding protein able to
CC       bind copper as well as toxic mercury ions, enhances the cell protection
CC       mechanism against induced metal toxicity (By similarity).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] =
CC         H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:131708; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) +
CC         L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:131709; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) +
CC         L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:131710; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] =
CC         glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:141553; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC         glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:141554; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC         glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:141555; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate;
CC         Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate;
CC         Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate;
CC         Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate +
CC         H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC         H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC         H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC         H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a
CC         guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-
CC         COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141580; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O
CC         = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300,
CC         Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445,
CC         ChEBI:CHEBI:141578; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC         guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-
CC         COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141581; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O
CC         = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC         Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- COFACTOR:
CC       Note=Deglycase activity does not require glutathione as a cofactor,
CC       however, glycated glutathione constitutes a PARK7 substrate.
CC       {ECO:0000250|UniProtKB:Q99497};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88767};
CC       Lipid-anchor {ECO:0000250|UniProtKB:O88767}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99497}. Nucleus {ECO:0000250|UniProtKB:Q99497}.
CC       Membrane raft {ECO:0000250|UniProtKB:O88767}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q99497}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- PTM: Sumoylated on Lys-130; which is essential for cell-growth
CC       promoting activity and transforming activity.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
CC       activation of protease activity in response to oxidative stress.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- CAUTION: Glyoxylase activity previously reported may reflect in fact
CC       its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CAUTION: The protein deglycation activity has been ascribed to a TRIS
CC       buffer artifact by a publication, which has then been rebutted by clear
CC       biochemical experiments showing that PARK7 is a bona fide deglycase.
CC       Deglycase activity is even strengthened by a novel article that reports
CC       nucleotide deglycation activity. {ECO:0000250|UniProtKB:Q99497}.
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DR   EMBL; AB076264; BAB79527.1; -; mRNA.
DR   RefSeq; NP_989916.1; NM_204585.1.
DR   AlphaFoldDB; Q8UW59; -.
DR   SMR; Q8UW59; -.
DR   BioGRID; 675570; 1.
DR   STRING; 9031.ENSGALP00000048532; -.
DR   MEROPS; C56.971; -.
DR   PaxDb; 9031-ENSGALP00000041756; -.
DR   GeneID; 395277; -.
DR   KEGG; gga:395277; -.
DR   CTD; 11315; -.
DR   VEuPathDB; HostDB:geneid_395277; -.
DR   eggNOG; KOG2764; Eukaryota.
DR   InParanoid; Q8UW59; -.
DR   PhylomeDB; Q8UW59; -.
DR   PRO; PR:Q8UW59; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0036524; F:protein deglycase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; ISS:AgBase.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0061691; P:detoxification of hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISS:AgBase.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IBA:GO_Central.
DR   GO; GO:1903189; P:glyoxal metabolic process; IBA:GO_Central.
DR   GO; GO:0106044; P:guanine deglycation; ISS:UniProtKB.
DR   GO; GO:0106046; P:guanine deglycation, glyoxal removal; ISS:UniProtKB.
DR   GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:AgBase.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:AgBase.
DR   CDD; cd03135; GATase1_DJ-1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR006287; DJ-1.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   NCBIfam; TIGR01383; not_thiJ; 1.
DR   PANTHER; PTHR48094:SF12; PARKINSON DISEASE PROTEIN 7 HOMOLOG; 1.
DR   PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Autophagy; Cell membrane; Chaperone; Copper; Cytoplasm;
KW   Endoplasmic reticulum; Fertilization; Hydrolase; Inflammatory response;
KW   Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Nucleus; Oxidation;
KW   Palmitate; Phosphoprotein; Protease; Reference proteome; RNA-binding;
KW   Stress response; Tumor suppressor; Ubl conjugation; Zymogen.
FT   CHAIN           1..?
FT                   /note="Protein/nucleic acid deglycase DJ-1"
FT                   /id="PRO_0000252486"
FT   PROPEP          ?..189
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000405562"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   MOD_RES         67
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   MOD_RES         106
FT                   /note="Cysteine sulfinic acid (-SO2H); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT   MOD_RES         182
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT   LIPID           46
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   LIPID           53
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   LIPID           106
FT                   /note="S-palmitoyl cysteine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
FT   CROSSLNK        130
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:Q99497"
SQ   SEQUENCE   189 AA;  19943 MW;  A39FE229D97DB942 CRC64;
     MASKRALVIL AKGAEEMETV IPTDVMRRAG IKVTVAGLTG KEPVQCSRDV LICPDASLED
     ARKEGPYDVI VLPGGNLGAQ NLSESAAVKD ILKDQESRKG LIAAICAGPT ALLAHGIGFG
     SKVITHPLAK DKMMNGAHYC YSESRVEKDG NILTSRGPGT SFEFGLAIVE ALMGKEVAEQ
     VKAPLILKD
//
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