OVAL_DRONO
ID OVAL_DRONO Reviewed; 386 AA.
AC E2RVI8; P86380;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Ovalbumin {ECO:0000303|PubMed:21058653};
DE Short=OVA {ECO:0000303|PubMed:21058653};
DE AltName: Full=Egg albumin {ECO:0000250|UniProtKB:P01012};
GN Name=SERPINB14;
OS Dromaius novaehollandiae (Emu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX NCBI_TaxID=8790;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 173-192, AND BLOCKAGE OF
RP N-TERMINUS.
RC TISSUE=Egg white {ECO:0000269|PubMed:21058653}, and
RC Oviduct {ECO:0000312|EMBL:BAJ23166.1};
RX PubMed=21058653; DOI=10.1021/jf103239v;
RA Maehashi K., Matano M., Irisawa T., Uchino M., Itagaki Y., Takano K.,
RA Kashiwagi Y., Watanabe T.;
RT "Primary structure of potential allergenic proteins in emu (Dromaius
RT novaehollandiae) egg white.";
RL J. Agric. Food Chem. 58:12530-12536(2010).
CC -!- FUNCTION: Storage protein of egg white. Lacks protease inhibitory
CC activity (By similarity). {ECO:0000250|UniProtKB:P01012}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01012}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:21058653}.
CC -!- MISCELLANEOUS: Much lower abundance than corresponding protein in
CC chicken egg white. {ECO:0000269|PubMed:21058653}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000255}.
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DR EMBL; AB525084; BAJ23166.1; -; mRNA.
DR PDB; 6KGA; X-ray; 3.30 A; A/B/C=1-386.
DR PDBsum; 6KGA; -.
DR AlphaFoldDB; E2RVI8; -.
DR SMR; E2RVI8; -.
DR Ensembl; ENSDNVT00000018679; ENSDNVP00000015532; ENSDNVG00000010949.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Phosphoprotein; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT CHAIN 2..386
FT /note="Ovalbumin"
FT /id="PRO_0000411101"
FT SITE 353..354
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..121
FT /evidence="ECO:0000250|UniProtKB:P01012"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 99..112
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 173..187
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 207..223
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:6KGA"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 323..335
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 337..351
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6KGA"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:6KGA"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:6KGA"
SQ SEQUENCE 386 AA; 43081 MW; 0D35DA6CA8D59543 CRC64;
MGSIGAASTE FCFDMFKELK VHHVNENIIY SPLSIISILS MVFLGARENT KTQMEKVIHF
DKITGFGESL ESQCGTSVSV HASLKDILSE ITKPSDNYSL SLASKLYAEE TYPVLPEYLQ
CIKELYKGSL ETVSFQTAAD QARELINSWV ETQTNGVIKN FLQPGSVDPQ TEMVLVDAIY
FKGTWEKAFK DEDTQEVPFR ITEQESKPVQ MMYQAGSFKV ATVAAEKMKI LELPYASGEL
SMFVLLPDDI SGLEQLETTI SIEKLSEWTS SNMMEDRKMK VYLPHMKIEE KYNLTSVLVA
LGMTDLFSPS ANLSGISTAQ TLKMSEAIHG AYVEIYEAGS EMATSTGVLV EAASVSEEFR
VDHPFLFLIK HNPSNSILFF GRCIFP
