OVAL_CHICK
ID OVAL_CHICK Reviewed; 386 AA.
AC P01012; Q804A4; Q90741;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ovalbumin;
DE AltName: Full=Allergen Gal d II;
DE AltName: Full=Egg albumin;
DE AltName: Full=Plakalbumin;
DE AltName: Allergen=Gal d 2;
GN Name=SERPINB14;
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=661981; DOI=10.1038/273723a0;
RA McReynolds L., O'Malley B.W., Nisbet A.D., Fothergill J.E., Givol D.,
RA Fields S., Robertson M., Brownlee G.G.;
RT "Sequence of chicken ovalbumin mRNA.";
RL Nature 273:723-728(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=692731; DOI=10.1038/275510a0;
RA Catterall J.F., O'Malley B.W., Robertson M.A., Staden R., Tanaka Y.,
RA Brownlee G.G.;
RT "Nucleotide sequence homology at 12 intron-exon junctions in the chick
RT ovalbumin gene.";
RL Nature 275:510-513(1978).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272839; DOI=10.1021/bi00525a024;
RA Woo S.L.C., Beattie W.G., Catterall J.F., Dugaiczyk A., Staden R.,
RA Brownlee G.G., O'Malley B.W.;
RT "Complete nucleotide sequence of the chicken chromosomal ovalbumin gene and
RT its biological significance.";
RL Biochemistry 20:6437-6446(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-283.
RC STRAIN=Mangyondak;
RA Kim R., Rim D., Li Y.;
RT "Ovalbumin from the chicken called Mangyondak in North Korea.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
RX PubMed=423993; DOI=10.1038/278370a0;
RA Robertson M.A., Staden R., Tanaka Y., Catterall J.F., O'Malley B.W.,
RA Brownlee G.G.;
RT "Sequence of three introns in the chick ovalbumin gene.";
RL Nature 278:370-372(1979).
RN [6]
RP PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT GLY-2.
RX PubMed=751625; DOI=10.1071/bi9780443;
RA Thompson E.O.P., Fisher W.K.;
RT "A correction and extension of the acetylated amino terminal sequence of
RT ovalbumin.";
RL Aust. J. Biol. Sci. 31:443-446(1978).
RN [7]
RP PROTEIN SEQUENCE OF 2-36, AND ACETYLATION AT GLY-2.
RX PubMed=272676; DOI=10.1073/pnas.75.1.94;
RA Palmiter R.D., Gagnon J., Walsh K.A.;
RT "Ovalbumin: a secreted protein without a transient hydrophobic leader
RT sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:94-98(1978).
RN [8]
RP PROTEIN SEQUENCE OF 6-17; 30-36; 61-79; 116-124; 367-374 AND 380-386.
RX PubMed=751624; DOI=10.1071/bi9780433;
RA Thompson E.O.P., Fisher W.K.;
RT "Amino acid sequences containing half-cystine residues in ovalbumin.";
RL Aust. J. Biol. Sci. 31:433-442(1978).
RN [9]
RP PROTEIN SEQUENCE OF 60-85 AND 338-360, AND PHOSPHORYLATION AT SER-69 AND
RP SER-345.
RX PubMed=6783411; DOI=10.1111/j.1432-1033.1981.tb05165.x;
RA Henderson J.Y., Moir A.J.G., Fothergill L.A., Fothergill J.E.;
RT "Sequences of sixteen phosphoserine peptides from ovalbumins of eight
RT species.";
RL Eur. J. Biochem. 114:439-450(1981).
RN [10]
RP PROTEIN SEQUENCE OF 85-106; 105-124; 111-124; 127-144; 143-160; 187-201;
RP 200-220; 264-279; 323-341; 360-371 AND 370-383, TISSUE SPECIFICITY,
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Egg white {ECO:0000303|PubMed:25436390};
RX PubMed=25436390; DOI=10.1021/jf504469t;
RA Kim J., Choi Y.H.;
RT "Differential abundance of egg white proteins in laying hens treated with
RT corticosterone.";
RL J. Agric. Food Chem. 62:12346-12359(2014).
RN [11]
RP PROTEIN SEQUENCE OF 354-359, PROTEOLYTIC CLEAVAGE AT ALA-353 AND PHE-359,
RP AND MUTAGENESIS OF ARG-340.
RX PubMed=11931671; DOI=10.1042/0264-6021:3630403;
RA Arii Y., Hirose M.;
RT "Probing the serpin structural-transition mechanism in ovalbumin mutant
RT R339T by proteolytic-cleavage kinetics of the reactive-centre loop.";
RL Biochem. J. 363:403-409(2002).
RN [12]
RP FUNCTION OF UNCLEAVED SIGNAL PEPTIDE, AND SUBCELLULAR LOCATION.
RX PubMed=6749856; DOI=10.1016/s0021-9258(18)33707-4;
RA Meek R.L., Walsh K.A., Palmiter R.D.;
RT "The signal sequence of ovalbumin is located near the NH2 terminus.";
RL J. Biol. Chem. 257:12245-12251(1982).
RN [13]
RP FUNCTION OF UNCLEAVED SIGNAL PEPTIDE.
RX PubMed=3732511; DOI=10.1016/0014-5793(86)80751-7;
RA Robinson A., Meredith C., Austen B.M.;
RT "Isolation and properties of the signal region from ovalbumin.";
RL FEBS Lett. 203:243-246(1986).
RN [14]
RP GLYCOSYLATION AT ASN-293.
RX PubMed=19358553; DOI=10.1021/ac900231w;
RA Thaysen-Andersen M., Mysling S., Hojrup P.;
RT "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS:
RT strong correlation between signal strength and glycoform quantities.";
RL Anal. Chem. 81:3933-3943(2009).
RN [15]
RP THERMOSTABILITY OF N- AND S-CONFORMERS.
RX PubMed=20512973; DOI=10.1002/pro.398;
RA Ishimaru T., Ito K., Tanaka M., Matsudomi N.;
RT "Thermostabilization of ovalbumin by alkaline treatment: Examination of the
RT possible roles of D-serine residues.";
RL Protein Sci. 19:1205-1212(2010).
RN [16]
RP DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP CYS-74 AND CYS-121.
RX PubMed=21389617; DOI=10.1271/bbb.100772;
RA Ishimaru T., Ito K., Tanaka M., Tanaka S., Matsudomi N.;
RT "The role of the disulfide bridge in the stability and structural integrity
RT of ovalbumin evaluated by site-directed mutagenesis.";
RL Biosci. Biotechnol. Biochem. 75:544-549(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=2352279; DOI=10.1016/s0022-2836(05)80212-8;
RA Wright H.T., Qian H.X., Huber R.;
RT "Crystal structure of plakalbumin, a proteolytically nicked form of
RT ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase
RT inhibitor.";
RL J. Mol. Biol. 213:513-528(1990).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=2395463; DOI=10.1038/347099a0;
RA Stein P.E., Leslie A.G.W., Finch J.T., Turnell W.G., McLaughlin P.J.,
RA Carrell R.W.;
RT "Crystal structure of ovalbumin as a model for the reactive centre of
RT serpins.";
RL Nature 347:99-102(1990).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), METAL-BINDING, SUBUNIT, DISULFIDE
RP BOND, AND GLYCOSYLATION AT ASN-293.
RX PubMed=1942038; DOI=10.1016/0022-2836(91)80185-w;
RA Stein P.E., Leslie A.G.W., Finch J.T., Carrell R.W.;
RT "Crystal structure of uncleaved ovalbumin at 1.95-A resolution.";
RL J. Mol. Biol. 221:941-959(1991).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-385 OF MUTANT THR-340, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=11779232; DOI=10.1006/jmbi.2001.5056;
RA Yamasaki M., Arii Y., Mikami B., Hirose M.;
RT "Loop-inserted and thermostabilized structure of P1-P1' cleaved ovalbumin
RT mutant R339T.";
RL J. Mol. Biol. 315:113-120(2002).
CC -!- FUNCTION: Non-inhibitory serpin. Storage protein of egg white.
CC {ECO:0000269|PubMed:3732511, ECO:0000269|PubMed:6749856}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1942038}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6749856}.
CC -!- TISSUE SPECIFICITY: Major protein of egg white. Expressed in the magnum
CC of the oviduct (at protein level) (PubMed:25436390).
CC {ECO:0000269|PubMed:25436390}.
CC -!- INDUCTION: Down-regulated by dietary stress. Decreased expression at
CC day 14 in the magnum of the oviduct in the corticosterone-fed laying
CC hens. {ECO:0000269|PubMed:25436390}.
CC -!- DOMAIN: The uncleaved signal peptide becomes available for membrane
CC translocation of ovalbumin when the nascent chain is 50 to 60 residues
CC long. The hydrophobic sequence, which lies between residues 27 and 43,
CC folds back on the preceding residues to form an amphipathic hairpin
CC structure which is the signal element recognized by the membrane.
CC -!- DOMAIN: Unlike other serpins, after protease cleavage at the P-P' site,
CC ovalbumin does not have the ability to undergo the conformational
CC transition into the loop-inserted reactive-center-containing
CC thermostabilized form. The bulky arginine residue (Arg-340) at the
CC hinge region appears to be responsible for this lack of loop-inserted
CC conformational change, but not for the absence of serpin inhibitory
CC activity.
CC -!- DOMAIN: During storage of fertilized and non-fertilized eggs or under
CC alkaline conditions, the native ovalbumin conformer (N-ovalbumin) is
CC transformed into a thermostabilized conformer, S-ovalbumin. Ser-165,
CC Ser-237 and Ser-321 take on a D-configuration in this conformer and may
CC be responsible for the thermostability.
CC -!- PTM: Undergoes proteolytic cleavage first at the canonical P1-P1' site,
CC and then at the P8-P7 site by subtilisin. {ECO:0000269|PubMed:11779232,
CC ECO:0000269|PubMed:11931671}.
CC -!- ALLERGEN: Can cause an allergic reaction in humans.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/OA/";
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DR EMBL; V00383; CAA23682.1; -; mRNA.
DR EMBL; M34352; AAA48998.1; -; Genomic_DNA.
DR EMBL; M34346; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; M34347; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; M34348; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; M34349; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; M34350; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; M34351; AAA48998.1; JOINED; Genomic_DNA.
DR EMBL; V00438; CAA23716.1; -; Genomic_DNA.
DR EMBL; J00895; AAB59956.1; -; Genomic_DNA.
DR EMBL; AY223553; AAO43266.1; -; mRNA.
DR EMBL; V00382; CAA23681.1; -; Genomic_DNA.
DR PIR; A90455; OACH.
DR RefSeq; NP_990483.1; NM_205152.2.
DR PDB; 1JTI; X-ray; 2.30 A; A/B=2-386.
DR PDB; 1OVA; X-ray; 1.95 A; A/B/C/D=2-386.
DR PDB; 1P1Z; X-ray; 3.26 A; P=258-265.
DR PDB; 1P4L; X-ray; 2.90 A; P=258-265.
DR PDB; 1UHG; X-ray; 1.90 A; A/B/C/D=2-386.
DR PDB; 1VAC; X-ray; 2.50 A; P=258-265.
DR PDB; 3C8K; X-ray; 2.90 A; P=258-265.
DR PDB; 3CVH; X-ray; 2.90 A; C/O=258-265.
DR PDB; 3P9L; X-ray; 2.00 A; C/F=258-265.
DR PDB; 3P9M; X-ray; 2.00 A; C/F=258-265.
DR PDB; 3PAB; X-ray; 2.20 A; C/F=258-265.
DR PDB; 4HKJ; X-ray; 3.00 A; C/G/K/O=258-265.
DR PDBsum; 1JTI; -.
DR PDBsum; 1OVA; -.
DR PDBsum; 1P1Z; -.
DR PDBsum; 1P4L; -.
DR PDBsum; 1UHG; -.
DR PDBsum; 1VAC; -.
DR PDBsum; 3C8K; -.
DR PDBsum; 3CVH; -.
DR PDBsum; 3P9L; -.
DR PDBsum; 3P9M; -.
DR PDBsum; 3PAB; -.
DR PDBsum; 4HKJ; -.
DR AlphaFoldDB; P01012; -.
DR PCDDB; P01012; -.
DR SASBDB; P01012; -.
DR SMR; P01012; -.
DR STRING; 9031.ENSGALP00000020965; -.
DR ChEMBL; CHEMBL1075085; -.
DR Allergome; 3292; Gal d 2.0101.
DR Allergome; 360; Gal d 2.
DR MEROPS; I04.958; -.
DR GlyConnect; 475; 45 N-Linked glycans.
DR iPTMnet; P01012; -.
DR PaxDb; P01012; -.
DR PRIDE; P01012; -.
DR ABCD; P01012; 2 sequenced antibodies.
DR Ensembl; ENSGALT00000037195; ENSGALP00000036403; ENSGALG00000012869.
DR GeneID; 396058; -.
DR KEGG; gga:396058; -.
DR CTD; 101801591; -.
DR VEuPathDB; HostDB:geneid_396058; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154520; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; P01012; -.
DR OMA; ILPEYIQ; -.
DR PhylomeDB; P01012; -.
DR TreeFam; TF352619; -.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR EvolutionaryTrace; P01012; -.
DR PRO; PR:P01012; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000012869; Expressed in ovary and 2 other tissues.
DR ExpressionAtlas; P01012; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031905; C:early endosome lumen; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
DR GO; GO:0032010; C:phagolysosome; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:AgBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
DR GO; GO:0080144; P:amino acid homeostasis; TAS:AgBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:AgBase.
DR GO; GO:0050801; P:ion homeostasis; TAS:AgBase.
DR GO; GO:0006811; P:ion transport; TAS:AgBase.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051412; P:response to corticosterone; IDA:AgBase.
DR GO; GO:0043627; P:response to estrogen; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR GO; GO:0048545; P:response to steroid hormone; IDA:AgBase.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allergen; Calcium; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:272676,
FT ECO:0000269|PubMed:751625"
FT CHAIN 2..386
FT /note="Ovalbumin"
FT /id="PRO_0000094126"
FT SIGNAL 22..48
FT /note="Not cleaved"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT SITE 353..354
FT /note="Cleavage; by elastase or subtilisin"
FT /evidence="ECO:0000269|PubMed:11931671"
FT SITE 359..360
FT /note="Cleavage; by subtilisin"
FT /evidence="ECO:0000269|PubMed:11931671"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:272676,
FT ECO:0000269|PubMed:751625"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6783411"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6783411"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19358553,
FT ECO:0000269|PubMed:1942038"
FT DISULFID 74..121
FT /evidence="ECO:0000269|PubMed:1942038,
FT ECO:0000269|PubMed:21389617"
FT VARIANT 283
FT /note="L -> F (in strain: Mangyondak)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 312
FT /note="N -> D (in a minor component)"
FT MUTAGEN 74
FT /note="C->A: Lower thermal denaturation temperature, more
FT susceptible to elastase or subtilisin cleavage and assumes
FT a native-like conformation on alkaline treatment; when
FT associated with or without A-121."
FT /evidence="ECO:0000269|PubMed:21389617"
FT MUTAGEN 121
FT /note="C->A: Lower thermal denaturation temperature, more
FT susceptible to elastase or subtilisin cleavage and assumes
FT a native-like conformation on alkaline treatment; when
FT associated with or without A-74."
FT /evidence="ECO:0000269|PubMed:21389617"
FT MUTAGEN 340
FT /note="R->T: Significantly more thermostabilized following
FT cleavage at P-P' site. Inserts reactive loop at very slow
FT rate. No inhibitory action against serine proteinases."
FT /evidence="ECO:0000269|PubMed:11931671"
FT CONFLICT 5
FT /note="G -> A (in Ref. 5; CAA23681)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> F (in Ref. 5; CAA23681)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> T (in Ref. 1; CAA23682)"
FT /evidence="ECO:0000305"
FT HELIX 4..22
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1OVA"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 173..183
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 207..223
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1OVA"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 275..284
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1JTI"
FT STRAND 324..335
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1UHG"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:1UHG"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1UHG"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:1UHG"
SQ SEQUENCE 386 AA; 42881 MW; 87179F028B20CEF2 CRC64;
MGSIGAASME FCFDVFKELK VHHANENIFY CPIAIMSALA MVYLGAKDST RTQINKVVRF
DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF SLASRLYAEE RYPILPEYLQ
CVKELYRGGL EPINFQTAAD QARELINSWV ESQTNGIIRN VLQPSSVDSQ TAMVLVNAIV
FKGLWEKAFK DEDTQAMPFR VTEQESKPVQ MMYQIGLFRV ASMASEKMKI LELPFASGTM
SMLVLLPDEV SGLEQLESII NFEKLTEWTS SNVMEERKIK VYLPRMKMEE KYNLTSVLMA
MGITDVFSSS ANLSGISSAE SLKISQAVHA AHAEINEAGR EVVGSAEAGV DAASVSEEFR
ADHPFLFCIK HIATNAVLFF GRCVSP
