ID   TGM2_PAGMA              Reviewed;         695 AA.
AC   P52181;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase 2 {ECO:0000305};
DE            EC=2.3.2.13 {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Fish-derived transglutaminase {ECO:0000303|PubMed:11080504};
DE            Short=FTG {ECO:0000303|PubMed:11080504};
DE   AltName: Full=Isopeptidase TGM2 {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Protein-glutamine deamidase TGM2 {ECO:0000305};
DE            EC=3.5.1.44 {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Protein-glutamine dopaminyltransferase TGM2 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Protein-glutamine histaminyltransferase TGM2 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Protein-glutamine noradrenalinyltransferase TGM2 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P08587};
DE   AltName: Full=Protein-glutamine serotonyltransferase TGM2 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P21980};
DE   AltName: Full=Tissue transglutaminase {ECO:0000303|PubMed:7556189};
DE   AltName: Full=Tissue-type transglutaminase {ECO:0000303|PubMed:7556189};
DE   AltName: Full=Transglutaminase-2 {ECO:0000250|UniProtKB:P21980};
DE            Short=TGase-2 {ECO:0000250|UniProtKB:P21980};
GN   Name=tgm2 {ECO:0000250|UniProtKB:P21980};
OS   Pagrus major (Red sea bream) (Chrysophrys major).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Pagrus.
OX   NCBI_TaxID=143350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=7556189; DOI=10.1111/j.1432-1033.1995.tb20826.x;
RA   Yasueda H., Nakanishi K., Kumazawa Y., Nagase K., Motoki M., Matsui H.;
RT   "Tissue-type transglutaminase from red sea bream (Pagrus major). Sequence
RT   analysis of the cDNA and functional expression in Escherichia coli.";
RL   Eur. J. Biochem. 232:411-419(1995).
RN   [2] {ECO:0007744|PDB:1G0D}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=11080504; DOI=10.1074/jbc.m009862200;
RA   Noguchi K., Ishikawa K., Yokoyama K., Ohtsuka T., Nio N., Suzuki E.;
RT   "Crystal structure of red sea bream transglutaminase.";
RL   J. Biol. Chem. 276:12055-12059(2001).
CC   -!- FUNCTION: Calcium-dependent acyltransferase that catalyzes the
CC       formation of covalent bonds between peptide-bound glutamine and various
CC       primary amines, such as gamma-amino group of peptide-bound lysine, or
CC       mono- and polyamines, thereby producing cross-linked or aminated
CC       proteins, respectively. Involved in many biological processes, such as
CC       bone development, angiogenesis, wound healing, cellular
CC       differentiation, chromatin modification and apoptosis. Acts as a
CC       protein-glutamine gamma-glutamyltransferase by mediating the cross-
CC       linking of proteins: under physiological conditions, the protein cross-
CC       linking activity is inhibited by GTP; inhibition is relieved by Ca(2+)
CC       in response to various stresses. When secreted, catalyzes cross-linking
CC       of proteins of the extracellular matrix, resulting in the formation of
CC       scaffolds. Plays a key role during apoptosis, both by (1) promoting the
CC       cross-linking of cytoskeletal proteins resulting in condensation of the
CC       cytoplasm, and by (2) mediating cross-linking proteins of the
CC       extracellular matrix, resulting in the irreversible formation of
CC       scaffolds that stabilize the integrity of the dying cells before their
CC       clearance by phagocytosis, thereby preventing the leakage of harmful
CC       intracellular components. In addition to protein cross-linking, can use
CC       different monoamine substrates to catalyze a vast array of protein
CC       post-translational modifications: mediates aminylation of serotonin,
CC       dopamine, noradrenaline or histamine into glutamine residues of target
CC       proteins to generate protein serotonylation, dopaminylation,
CC       noradrenalinylation or histaminylation, respectively (By similarity).
CC       Mediates protein serotonylation of small GTPases during activation and
CC       aggregation of platelets, leading to constitutive activation of these
CC       GTPases (By similarity). Plays a key role in chromatin organization by
CC       mediating serotonylation and dopaminylation of histone H3. Catalyzes
CC       serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic
CC       neuron differentiation, thereby facilitating transcription. Acts as a
CC       mediator of neurotransmission-independent role of nuclear dopamine in
CC       ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-
CC       5' of histone H3 (H3Q5dop), thereby regulating relapse-related
CC       transcriptional plasticity in the reward system. Also acts as a protein
CC       deamidase by mediating the side chain deamidation of specific glutamine
CC       residues of proteins to glutamate. May also act as an isopeptidase
CC       cleaving the previously formed cross-links. Also able to participate in
CC       signaling pathways independently of its acyltransferase activity: acts
CC       as a signal transducer in alpha-1 adrenergic receptor-mediated
CC       stimulation of phospholipase C-delta (PLCD) activity and is required
CC       for coupling alpha-1 adrenergic agonists to the stimulation of
CC       phosphoinositide lipid metabolism (By similarity).
CC       {ECO:0000250|UniProtKB:P08587, ECO:0000250|UniProtKB:P21980}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13;
CC         Evidence={ECO:0000250|UniProtKB:P21980, ECO:0000255|PROSITE-
CC         ProRule:PRU10024};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + serotonin = 5-serotonyl-L-glutamyl-
CC         [protein] + NH4(+); Xref=Rhea:RHEA:66552, Rhea:RHEA-COMP:10207,
CC         Rhea:RHEA-COMP:17052, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:167174, ChEBI:CHEBI:350546;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine + L-glutaminyl-[protein] = 5-dopaminyl-L-glutamyl-
CC         [protein] + NH4(+); Xref=Rhea:RHEA:66556, Rhea:RHEA-COMP:10207,
CC         Rhea:RHEA-COMP:17053, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:59905, ChEBI:CHEBI:167175;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=histamine + L-glutaminyl-[protein] = 5-histaminyl-L-glutamyl-
CC         [protein] + NH4(+); Xref=Rhea:RHEA:66564, Rhea:RHEA-COMP:10207,
CC         Rhea:RHEA-COMP:17056, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:58432, ChEBI:CHEBI:167179;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-noradrenaline + L-glutaminyl-[protein] = 5-(R)-
CC         noradrenalinyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66560,
CC         Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17054, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:72587, ChEBI:CHEBI:167178;
CC         Evidence={ECO:0000250|UniProtKB:P08587};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561;
CC         Evidence={ECO:0000250|UniProtKB:P08587};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC         Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:30011; EC=3.5.1.44;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P21980};
CC   -!- ACTIVITY REGULATION: Acyltransferase activity is regulated by the
CC       binding of GTP and Ca(2+): inactivated by GTP, which stabilizes its
CC       closed structure, thereby obstructing the accessibility of substrates
CC       to the active sites. In contrast, Ca(2+) acts as a cofactor by inducing
CC       conformational change to the active open form. In absence of Ca(2+),
CC       Mg(2+) may bind Ca(2+)-binding sites, promoting GTP-binding and
CC       subsequent inhibition of the acyltransferase activity.
CC       {ECO:0000250|UniProtKB:P21980}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P21980}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P21980}. Nucleus {ECO:0000250|UniProtKB:P21980}.
CC       Chromosome {ECO:0000250|UniProtKB:P21980}. Secreted, extracellular
CC       space, extracellular matrix {ECO:0000250|UniProtKB:P21980}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P21980}. Note=Mainly localizes to the cytosol.
CC       Present at much lower level in the nucleus and chromatin. Also secreted
CC       via a non-classical secretion pathway to the extracellular matrix.
CC       {ECO:0000250|UniProtKB:P21980}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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DR   EMBL; S79761; AAB35370.1; -; mRNA.
DR   PIR; S66662; S66662.
DR   PDB; 1G0D; X-ray; 2.50 A; A=1-695.
DR   PDBsum; 1G0D; -.
DR   AlphaFoldDB; P52181; -.
DR   SMR; P52181; -.
DR   EvolutionaryTrace; P52181; -.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0120297; F:histone dopaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0120295; F:histone serotonyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0120299; F:peptide histaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0120298; F:peptide noradrenalinyltransferase activity; IEA:RHEA.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; ISS:UniProtKB.
DR   GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR   GO; GO:1903351; P:cellular response to dopamine; ISS:UniProtKB.
DR   GO; GO:1904015; P:cellular response to serotonin; ISS:UniProtKB.
DR   GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR   GO; GO:0018277; P:protein deamination; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:2000425; P:regulation of apoptotic cell clearance; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF73; NOVEL TRANSGLUTAMINASE FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   Pfam; PF00927; Transglut_C; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Calcium; Cell membrane; Chromosome;
KW   Cytoplasm; Direct protein sequencing; Extracellular matrix; GTP-binding;
KW   Hydrolase; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Nucleus; Protease; Secreted; Transferase.
FT   CHAIN           1..695
FT                   /note="Protein-glutamine gamma-glutamyltransferase 2"
FT                   /id="PRO_0000213710"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024,
FT                   ECO:0000305|PubMed:11080504, ECO:0007744|PDB:1G0D"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024,
FT                   ECO:0000305|PubMed:11080504, ECO:0007744|PDB:1G0D"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024,
FT                   ECO:0000305|PubMed:11080504, ECO:0007744|PDB:1G0D"
FT   BINDING         395
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         397
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         434
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P21980"
FT   BINDING         444
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         449
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         476..482
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P21980"
FT   BINDING         578..581
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P21980"
FT   SITE            515
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000305|PubMed:11080504,
FT                   ECO:0007744|PDB:1G0D"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           15..21
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          40..48
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          55..63
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          67..76
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          90..98
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          106..115
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           148..154
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          159..166
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          169..176
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           184..193
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           196..200
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           202..208
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           212..223
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           253..261
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           272..286
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          290..298
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            301..304
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          306..312
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          327..339
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          350..355
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            363..365
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          368..372
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           373..378
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            384..386
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           387..395
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          397..403
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          413..416
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          428..431
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           437..440
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           447..456
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          473..478
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          488..496
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          502..513
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          525..532
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          536..544
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   HELIX           546..549
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            550..552
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          558..566
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          573..581
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          588..590
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          601..608
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          611..613
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          615..617
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          619..624
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   TURN            625..627
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          628..634
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          636..639
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          644..651
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          657..666
FT                   /evidence="ECO:0007829|PDB:1G0D"
FT   STRAND          673..682
FT                   /evidence="ECO:0007829|PDB:1G0D"
SQ   SEQUENCE   695 AA;  78216 MW;  A9A128345D474CF8 CRC64;
     MASYKGLIVD VNGRSHENNL AHRTREIDRE RLIVRRGQPF SITLQCSDSL PPKHHLELVL
     HLGKRDEVVI KVQKEHGARD KWWFNQQGAQ DEILLTLHSP ANAVIGHYRL AVLVMSPDGH
     IVERADKISF HMLFNPWCRD DMVYLPDESK LQEYVMNEDG VIYMGTWDYI RSIPWNYGQF
     EDYVMDICFE VLDNSPAALK NSEMDIEHRS DPVYVGRTIT AMVNSNGDRG VLTGRWEEPY
     TDGVAPYRWT GSVPILQQWS KAGVRPVKYG QCWVFAAVAC TVLRCLGIPT RPITNFASAH
     DVDGNLSVDF LLNERLESLD SRQRSDSSWN FHCWVESWMS REDLPEGNDG WQVLDPTPQE
     LSDGEFCCGP CPVAAIKEGN LGVKYDAPFV FAEVNADTIY WIVQKDGQRR KITEDHASVG
     KNISTKSVYG NHREDVTLHY KYPEGSQKER EVYKKAGRRV TEPSNEIAEQ GRLQLSIKHA
     QPVFGTDFDV IVEVKNEGGR DAHAQLTMLA MAVTYNSLRR GECQRKTISV TVPAHKAHKE
     VMRLHYDDYV RCVSEHHLIR VKALLDAPGE NGPIMTVANI PLSTPELLVQ VPGKAVVWEP
     LTAYVSFTNP LPVPLKGGVF TLEGAGLLSA TQIHVNGAVA PSGKVSVKLS FSPMRTGVRK
     LLVDFDSDRL KDVKGVTTVV VHKKYRSLIT GLHTD
//