PARK7_CHLAE
ID PARK7_CHLAE Reviewed; 189 AA.
AC Q95LI9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
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 AltName: 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 Flags: Precursor;
GN Name=PARK7 {ECO:0000250|UniProtKB:Q99497};
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
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: Multifunctional protein with controversial molecular function
CC which plays an important role in cell protection against oxidative
CC stress and cell death acting as oxidative stress sensor and redox-
CC sensitive chaperone and protease. It is involved in neuroprotective
CC mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male
CC fertility as a positive regulator of androgen signaling pathway as well
CC as cell growth and transformation through, for instance, the modulation
CC of NF-kappa-B signaling pathway. Has been described as a protein and
CC nucleotide deglycase that catalyzes the deglycation of the Maillard
CC adducts formed between amino groups of proteins or nucleotides and
CC reactive carbonyl groups of glyoxals. But this function is rebuted by
CC other works. As a protein deglycase, 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. Protects histones from adduction by methylglyoxal,
CC controls the levels of methylglyoxal-derived argininine modifications
CC on chromatin. Able to remove the glycations and restore histone 3,
CC histone glycation disrupts both local and global chromatin architecture
CC by altering histone-DNA interactions as well as histone acetylation and
CC ubiquitination levels. Displays a very low glyoxalase activity that may
CC reflect its deglycase activity. Eliminates hydrogen peroxide and
CC protects cells against hydrogen peroxide-induced cell death. Required
CC for correct mitochondrial morphology and function as well as for
CC autophagy of dysfunctional mitochondria. Plays a role in regulating
CC expression or stability of the mitochondrial uncoupling proteins
CC SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra
CC pars compacta and attenuates the oxidative stress induced by calcium
CC entry into the neurons via L-type channels during pacemaking. Regulates
CC astrocyte inflammatory responses, may modulate lipid rafts-dependent
CC endocytosis in astrocytes and neuronal cells. In pancreatic islets,
CC involved in the maintenance of mitochondrial reactive oxygen species
CC (ROS) levels and glucose homeostasis in an age- and diet dependent
CC manner. Protects pancreatic beta cells from cell death induced by
CC inflammatory and cytotoxic setting. Binds to a number of mRNAs
CC containing multiple copies of GG or CC motifs and partially inhibits
CC their translation but dissociates following oxidative stress. Metal-
CC binding protein able to bind copper as well as toxic mercury ions,
CC enhances the cell protection mechanism against induced metal toxicity.
CC In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct
CC NADPH oxidase-dependent ROS production, and protects against sepsis.
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. Binds EFCAB6/DJBP and PIAS2. Part of a ternary
CC complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-
CC terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF.
CC Forms a complex with PINK1 and PRKN (By similarity). Interacts (via C-
CC terminus) with NCF1; the interaction is enhanced by LPS and modulates
CC NCF1 phosphorylation and membrane translocation (By similarity).
CC Interacts with NENF (By similarity). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000250|UniProtKB:Q99LX0}.
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}. Note=Under normal conditions, located
CC predominantly in the cytoplasm and, to a lesser extent, in the nucleus
CC and mitochondrion. Translocates to the mitochondrion and subsequently
CC to the nucleus in response to oxidative stress and exerts an increased
CC cytoprotective effect against oxidative damage. Membrane raft
CC localization in astrocytes and neuronal cells requires palmitoylation.
CC {ECO:0000250|UniProtKB:Q99497}.
CC -!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for
CC cell-growth 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: Glyoxalase activity has been reported. It may however reflect
CC its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
CC -!- CAUTION: The protein deglycation activity is controversial. It has been
CC ascribed to a TRIS buffer artifact by a publication and as a result of
CC the removal of methylglyoxal by glyoxalase activity that leads to a
CC subsequent decomposition of hemithioacetals and hemianimals due to the
CC shift in equilibrium position by another one. However, biochemical
CC experiments showing that PARK7 is a bona fide deglycase have been
CC performed. {ECO:0000250|UniProtKB:Q99497}.
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DR EMBL; AB073863; BAB71781.1; -; mRNA.
DR AlphaFoldDB; Q95LI9; -.
DR BMRB; Q95LI9; -.
DR SMR; Q95LI9; -.
DR MEROPS; C56.971; -.
DR PRIDE; Q95LI9; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1990422; F:glyoxalase (glycolic acid-forming) activity; ISS:UniProtKB.
DR GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR GO; GO:0140041; P:cellular detoxification of methylglyoxal; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
DR GO; GO:0050787; P:detoxification of mercury ion; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
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:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR GO; GO:0061727; P:methylglyoxal catabolic process to lactate; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036527; P:peptidyl-arginine deglycation; 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:0036530; P:protein deglycation, methylglyoxal removal; ISS:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0035065; P:regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0033182; P:regulation of histone ubiquitination; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
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 Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01383; not_thiJ; 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; RNA-binding; Stress response;
KW Tumor suppressor; Ubl conjugation; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT CHAIN 2..?
FT /note="Parkinson disease protein 7 homolog"
FT /id="PRO_0000250480"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405557"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT ACT_SITE 126
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT SITE 149..150
FT /note="Cleavage; by CASP6"
FT /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT MOD_RES 2
FT /note="N-acetylalanine"
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; 19905 MW; 589950C2F0175367 CRC64;
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTIAGLAG KDPVQCSRDV VICPDASLED
AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG LIAAICAGPT ALLAHEIGFG
SKVTTHPLAK DKMMNGGHYT YSENRVEKDG LILTSRGPGT SFEFALAIVE ALNGKEVAAQ
VKAPLVLKD
