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 02-SEP-2026, entry version 210. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_990483.2; NM_205152.3. 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 AlphaFoldDB; P01012; -. DR PCDDB; P01012; -. DR SASBDB; P01012; -. DR SMR; P01012; -. DR BioGRID; 676326; 4. DR FunCoup; P01012; 62. DR STRING; 9031.ENSGALP00000036403; -. DR ChEMBL; CHEMBL1075085; -. DR Allergome; 3292; Gal d 2.0101. DR Allergome; 360; Gal d 2. DR MEROPS; I04.958; -. DR GlyConnect; P01012; 57 N-Linked glycans (1 site). DR GlyCosmos; P01012; 1 site, 73 glycans. DR GlyGen; P01012; 3 sites, 70 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; P01012; -. DR PaxDb; 9031-ENSGALP00000036403; -. DR ABCD; P01012; 2 sequenced antibodies. DR Ensembl; ENSGALT00010027940.1; ENSGALP00010016033.1; ENSGALG00010011679.1. DR GeneID; 396058; -. DR KEGG; gga:396058; -. DR CTD; 396058; -. DR VEuPathDB; HostDB:geneid_396058; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000154520; -. DR HOGENOM; CLU_023330_0_2_1; -. DR InParanoid; P01012; -. DR OMA; QMMYQIG; -. DR OrthoDB; 671595at2759; -. DR PhylomeDB; P01012; -. DR Reactome; R-GGA-6798695; Neutrophil degranulation. DR Reactome; R-GGA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes. DR CD-CODE; 783B6188; Synthetic Condensate 000211. DR CD-CODE; DFAB25C5; Synthetic Condensate 000216. DR EvolutionaryTrace; P01012; -. DR PRO; PR:P01012; -. DR Proteomes; UP000000539; Chromosome 2. DR Bgee; ENSGALG00000012869; Expressed in ovary and 2 other cell types or tissues. 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: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:0009792; P:embryo development ending in birth or egg hatching; TAS:AgBase. DR GO; GO:0080144; P:intracellular amino acid homeostasis; TAS:AgBase. DR GO; GO:0050801; P:monoatomic ion homeostasis; TAS:AgBase. DR GO; GO:0006811; P:monoatomic ion transport; TAS:AgBase. 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 CDD; cd02059; serpinB14_OVA; 1. DR FunFam; 2.30.39.10:FF:000001; Serpin family B member 2; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR PANTHER; PTHR11461:SF186; SERPIN B4; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. 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; -. 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 113..115 FT /evidence="ECO:0007829|PDB:1OVA" 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 188..190 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 //