IOVO_CHICK
ID IOVO_CHICK Reviewed; 210 AA.
AC P01005;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ovomucoid;
DE AltName: Full=Allergen Gal d I;
DE AltName: Allergen=Gal d 1;
DE Flags: Precursor;
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=7430252; DOI=10.1083/jcb.87.2.480;
RA Catterall J.F., Stein J.P., Kristo P., Means A.R., O'Malley B.W.;
RT "Primary sequence of ovomucoid messenger RNA as determined from cloned
RT complementary DNA.";
RL J. Cell Biol. 87:480-487(1980).
RN [2]
RP PROTEIN SEQUENCE OF 25-210.
RX PubMed=3548816; DOI=10.1021/bi00375a027;
RA Kato I., Schrode J., Kohr W.J., Laskowski M. Jr.;
RT "Chicken ovomucoid: determination of its amino acid sequence, determination
RT of the trypsin reactive site, and preparation of all three of its
RT domains.";
RL Biochemistry 26:193-201(1987).
RN [3]
RP PROTEIN SEQUENCE OF 1-44 (PRECURSOR PROTEIN).
RX PubMed=721826; DOI=10.1016/s0021-9258(17)34279-5;
RA Thibodeau S.N., Palmiter R.D., Walsh K.A.;
RT "Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal
RT extension.";
RL J. Biol. Chem. 253:9018-9023(1978).
RN [4]
RP GLYCOSYLATION AT ASN-77 AND ASN-199, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15253437; DOI=10.1021/pr034112b;
RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT "A new strategy for identification of N-glycosylated proteins and
RT unambiguous assignment of their glycosylation sites using HILIC enrichment
RT and partial deglycosylation.";
RL J. Proteome Res. 3:556-566(2004).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23075397; DOI=10.1111/febs.12033;
RA Derache C., Epinette C., Roussel A., Gabant G., Cadene M., Korkmaz B.,
RA Gauthier F., Kellenberger C.;
RT "Crystal structure of greglin, a novel non-classical Kazal inhibitor, in
RT complex with subtilisin.";
RL FEBS J. 279:4466-4478(2012).
CC -!- FUNCTION: Serine protease inhibitor. Inhibits trypsin.
CC {ECO:0000269|PubMed:23075397}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC No decrease in activity observed after incubating at pH 2.5 and pH
CC 7.4 for 1 hour. Retains 20% activity after incubation at pH 12 for 1
CC hour. {ECO:0000269|PubMed:23075397};
CC Temperature dependence:
CC No decrease in activity observed after heating for 1 hour at up to 80
CC degrees Celsius. Retains 20% activity after incubation at 95 degrees
CC Celsius for 1 hour. {ECO:0000269|PubMed:23075397};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: Avian ovomucoid consists of three homologous, tandem Kazal
CC family inhibitory domains.
CC -!- ALLERGEN: Causes an allergic reaction in human.
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DR EMBL; J00902; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A92754; TICHM.
DR RefSeq; NP_001295423.1; NM_001308494.1.
DR RefSeq; XP_015149249.1; XM_015293763.1.
DR AlphaFoldDB; P01005; -.
DR SMR; P01005; -.
DR Allergome; 3291; Gal d 1.0101.
DR Allergome; 359; Gal d 1.
DR MEROPS; I01.001; -.
DR MEROPS; I01.002; -.
DR MEROPS; I01.003; -.
DR GlyConnect; 479; 44 N-Linked glycans.
DR iPTMnet; P01005; -.
DR PaxDb; P01005; -.
DR Ensembl; ENSGALT00000005554; ENSGALP00000005544; ENSGALG00000003512.
DR GeneID; 416236; -.
DR KEGG; gga:416236; -.
DR CTD; 84651; -.
DR VEuPathDB; HostDB:geneid_416236; -.
DR GeneTree; ENSGT00520000060726; -.
DR HOGENOM; CLU_087965_0_0_1; -.
DR InParanoid; P01005; -.
DR OMA; CSDYPKP; -.
DR OrthoDB; 1283825at2759; -.
DR PhylomeDB; P01005; -.
DR TreeFam; TF352550; -.
DR PRO; PR:P01005; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000003512; Expressed in lung and 2 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; TAS:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0030246; F:carbohydrate binding; IDA:AgBase.
DR GO; GO:0019863; F:IgE binding; IDA:AgBase.
DR GO; GO:0019864; F:IgG binding; IMP:AgBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
DR GO; GO:0048545; P:response to steroid hormone; TAS:AgBase.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF00050; Kazal_1; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR PROSITE; PS00282; KAZAL_1; 3.
DR PROSITE; PS51465; KAZAL_2; 3.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3548816"
FT CHAIN 25..210
FT /note="Ovomucoid"
FT /id="PRO_0000016579"
FT DOMAIN 25..88
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 89..153
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 156..210
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 48..49
FT /note="Reactive bond 1 for endoproteinase Lys-C"
FT SITE 113..114
FT /note="Reactive bond 2 for trypsin"
FT SITE 172..173
FT /note="Reactive bond 3"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15253437"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:15253437"
FT DISULFID 29..68
FT DISULFID 46..65
FT DISULFID 54..86
FT DISULFID 94..133
FT DISULFID 111..130
FT DISULFID 119..151
FT DISULFID 162..192
FT DISULFID 170..189
FT DISULFID 178..210
FT VARIANT 158..159
FT /note="Missing (due to an ambiguous intron excision)"
FT CONFLICT 62
FT /note="T -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="M -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="G -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 22591 MW; 8BE9516B6D38ACF9 CRC64;
MAMAGVFVLF SFVLCGFLPD AAFGAEVDCS RFPNATDKEG KDVLVCNKDL RPICGTDGVT
YTNDCLLCAY SIEFGTNISK EHDGECKETV PMNCSSYANT TSEDGKVMVL CNRAFNPVCG
TDGVTYDNEC LLCAHKVEQG ASVDKRHDGG CRKELAAVSV DCSEYPKPDC TAEDRPLCGS
DNKTYGNKCN FCNAVVESNG TLTLSHFGKC
