TGM2_PAGMA
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 03-AUG-2022, entry version 107.
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; -; 3.
DR Gene3D; 3.90.260.10; -; 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 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; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
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
