KAT3_MOUSE
ID KAT3_MOUSE Reviewed; 455 AA.
AC Q71RI9; Q8BJ84;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 3 {ECO:0000305|PubMed:19029248};
DE EC=2.6.1.7 {ECO:0000269|PubMed:19029248};
DE AltName: Full=Cysteine-S-conjugate beta-lyase 2 {ECO:0000305|PubMed:19029248};
DE EC=4.4.1.13 {ECO:0000269|PubMed:19029248};
DE AltName: Full=Kynurenine aminotransferase 3;
DE AltName: Full=Kynurenine aminotransferase III;
DE Short=KATIII;
DE AltName: Full=Kynurenine--glyoxylate transaminase {ECO:0000305|PubMed:19029248};
DE EC=2.6.1.63 {ECO:0000269|PubMed:19029248};
DE AltName: Full=Kynurenine--oxoglutarate transaminase III;
GN Name=Kyat3; Synonyms=Ccbl2, Kat3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16376499; DOI=10.1016/j.gene.2005.09.034;
RA Yu P., Li Z., Zhang L., Tagle D.A., Cai T.;
RT "Characterization of kynurenine aminotransferase III, a novel member of a
RT phylogenetically conserved KAT family.";
RL Gene 365:111-118(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 42-451, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
RP COFACTOR, AND PATHWAY.
RX PubMed=19029248; DOI=10.1128/mcb.01272-08;
RA Han Q., Robinson H., Cai T., Tagle D.A., Li J.;
RT "Biochemical and structural properties of mouse kynurenine aminotransferase
RT III.";
RL Mol. Cell. Biol. 29:784-793(2009).
RN [8]
RP ERRATUM OF PUBMED:19029248.
RX PubMed=29712768; DOI=10.1128/mcb.00099-18;
RA Han Q., Robinson H., Cai T., Tagle D.A., Li J.;
RT "Correction for Han et al., 'Biochemical and structural properties of mouse
RT kynurenine aminotransferase III'.";
RL Mol. Cell. Biol. 38:0-0(2018).
RN [9] {ECO:0007744|PDB:5VEP, ECO:0007744|PDB:5VEQ, ECO:0007744|PDB:5VER}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 42-451.
RX PubMed=29113027; DOI=10.1111/febs.14320;
RA Wlodawer A., Dauter Z., Porebski P.J., Minor W., Stanfield R.,
RA Jaskolski M., Pozharski E., Weichenberger C.X., Rupp B.;
RT "Detect, correct, retract: How to manage incorrect structural models.";
RL FEBS J. 285:444-466(2018).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC the tryptophan catabolic pathway which is also a broad spectrum
CC antagonist of the three ionotropic excitatory amino acid receptors
CC among others (PubMed:19029248). May catalyze the beta-elimination of S-
CC conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the
CC cleavage of the C-S or C-Se bond (PubMed:19029248). Has transaminase
CC activity towards L-kynurenine, tryptophan, phenylalanine, serine,
CC cysteine, methionine, histidine, glutamine and asparagine with
CC glyoxylate as an amino group acceptor (in vitro). Has lower activity
CC with 2-oxoglutarate as amino group acceptor (in vitro)
CC (PubMed:19029248). {ECO:0000269|PubMed:19029248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7;
CC Evidence={ECO:0000269|PubMed:19029248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000305|PubMed:19029248};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
CC Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:19029248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000305|PubMed:19029248};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:19029248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901;
CC Evidence={ECO:0000305|PubMed:19029248};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000269|PubMed:19029248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000305|PubMed:19029248};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19029248};
CC -!- ACTIVITY REGULATION: Kynurenine transamination is competitively
CC inhibited by cysteine, glutamine, histidine, methionine, leucine, or
CC phenylalanine. {ECO:0000269|PubMed:19029248}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for glutamine {ECO:0000269|PubMed:19029248};
CC KM=0.7 mM for histidine {ECO:0000269|PubMed:19029248};
CC KM=0.7 mM for cysteine {ECO:0000269|PubMed:19029248};
CC KM=0.9 mM for methionine {ECO:0000269|PubMed:19029248};
CC KM=1.1 mM for phenylalanine {ECO:0000269|PubMed:19029248};
CC KM=1.4 mM for asparagine {ECO:0000269|PubMed:19029248};
CC KM=1.5 mM for kynurenine {ECO:0000269|PubMed:19029248};
CC KM=7.1 mM for tryptophan {ECO:0000269|PubMed:19029248};
CC KM=3.0 mM for serine {ECO:0000269|PubMed:19029248};
CC KM=0.4 mM for glyoxylate {ECO:0000269|PubMed:19029248};
CC KM=0.6 mM for phenylpyruvate {ECO:0000269|PubMed:19029248};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:19029248};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:19029248};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000269|PubMed:19029248}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19029248}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q71RI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71RI9-2; Sequence=VSP_025605;
CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression levels in
CC liver, kidney, heart and neuroendocrine tissues.
CC {ECO:0000269|PubMed:16376499}.
CC -!- DEVELOPMENTAL STAGE: Expressed from postnatal day (PND) 7 and peaks in
CC adult. {ECO:0000269|PubMed:16376499}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF363737; AAQ15190.1; -; mRNA.
DR EMBL; AK049569; BAC33817.1; -; mRNA.
DR EMBL; AK145623; BAE26546.1; -; mRNA.
DR EMBL; BC131942; AAI31943.1; -; mRNA.
DR EMBL; BC132615; AAI32616.1; -; mRNA.
DR CCDS; CCDS17881.1; -. [Q71RI9-2]
DR CCDS; CCDS80040.1; -. [Q71RI9-1]
DR RefSeq; NP_001280489.1; NM_001293560.1. [Q71RI9-1]
DR RefSeq; NP_776124.1; NM_173763.4. [Q71RI9-2]
DR RefSeq; XP_006501494.1; XM_006501431.3. [Q71RI9-2]
DR RefSeq; XP_011238416.1; XM_011240114.2. [Q71RI9-2]
DR PDB; 2ZJG; X-ray; 3.00 A; A/B=42-451.
DR PDB; 3E2F; X-ray; 2.59 A; A/B=42-451.
DR PDB; 3E2Y; X-ray; 2.26 A; A/B=42-451.
DR PDB; 3E2Z; X-ray; 2.81 A; A/B=42-451.
DR PDB; 5VEP; X-ray; 2.59 A; A/B=42-451.
DR PDB; 5VEQ; X-ray; 2.26 A; A/B=42-451.
DR PDB; 5VER; X-ray; 2.81 A; A/B=42-451.
DR PDBsum; 2ZJG; -.
DR PDBsum; 3E2F; -.
DR PDBsum; 3E2Y; -.
DR PDBsum; 3E2Z; -.
DR PDBsum; 5VEP; -.
DR PDBsum; 5VEQ; -.
DR PDBsum; 5VER; -.
DR AlphaFoldDB; Q71RI9; -.
DR SMR; Q71RI9; -.
DR BioGRID; 230916; 1.
DR STRING; 10090.ENSMUSP00000041675; -.
DR iPTMnet; Q71RI9; -.
DR PhosphoSitePlus; Q71RI9; -.
DR SwissPalm; Q71RI9; -.
DR EPD; Q71RI9; -.
DR jPOST; Q71RI9; -.
DR MaxQB; Q71RI9; -.
DR PaxDb; Q71RI9; -.
DR PeptideAtlas; Q71RI9; -.
DR PRIDE; Q71RI9; -.
DR ProteomicsDB; 268958; -. [Q71RI9-1]
DR ProteomicsDB; 268959; -. [Q71RI9-2]
DR Antibodypedia; 19822; 90 antibodies from 20 providers.
DR DNASU; 229905; -.
DR Ensembl; ENSMUST00000044392; ENSMUSP00000041675; ENSMUSG00000040213. [Q71RI9-2]
DR Ensembl; ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213. [Q71RI9-1]
DR GeneID; 229905; -.
DR KEGG; mmu:229905; -.
DR UCSC; uc008roz.2; mouse. [Q71RI9-1]
DR CTD; 56267; -.
DR MGI; MGI:2677849; Kyat3.
DR VEuPathDB; HostDB:ENSMUSG00000040213; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000155827; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q71RI9; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q71RI9; -.
DR TreeFam; TF352342; -.
DR BRENDA; 2.6.1.15; 3474.
DR BRENDA; 2.6.1.7; 3474.
DR BRENDA; 4.4.1.13; 3474.
DR UniPathway; UPA00334; UER00726.
DR BioGRID-ORCS; 229905; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Kyat3; mouse.
DR PRO; PR:Q71RI9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q71RI9; protein.
DR Bgee; ENSMUSG00000040213; Expressed in left lobe of liver and 223 other tissues.
DR ExpressionAtlas; Q71RI9; baseline and differential.
DR Genevisible; Q71RI9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034612; KAT_III.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF6; PTHR43807:SF6; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..455
FT /note="Kynurenine--oxoglutarate transaminase 3"
FT /id="PRO_0000287705"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 281
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025605"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3E2Z"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3E2F"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5VEP"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2ZJG"
FT HELIX 339..359
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:5VEP"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3E2Y"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:3E2Y"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:3E2Y"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:3E2Y"
SQ SEQUENCE 455 AA; 51126 MW; 94FA35EC67121EF2 CRC64;
MLLAQRRLIS LGCRSKPIKT IYSSSKVLGL CTSAKMALKF KNAKRIEGLD SNVWVEFTKL
AADPSVVNLG QGFPDISPPS YVKEELSKAA FIDNMNQYTR GFGHPALVKA LSCLYGKIYQ
RQIDPNEEIL VAVGAYGSLF NSIQGLVDPG DEVIIMVPFY DCYEPMVRMA GAVPVFIPLR
SKPTDGMKWT SSDWTFDPRE LESKFSSKTK AIILNTPHNP LGKVYTRQEL QVIADLCVKH
DTLCISDEVY EWLVYTGHTH VKIATLPGMW ERTITIGSAG KTFSVTGWKL GWSIGPAHLI
KHLQTVQQNS FYTCATPLQA ALAEAFWIDI KRMDDPECYF NSLPKELEVK RDRMVRLLNS
VGLKPIVPDG GYFIIADVSS LGADLSDMNS DEPYDYKFVK WMTKHKKLTA IPVSAFCDSK
SKPHFEKLVR FCFIKKDSTL DAAEEIFRAW NSQKS
