IOV7_CHICK
ID IOV7_CHICK Reviewed; 517 AA.
AC P10184; A0A3Q2UJ85; F1NMN2; Q6XLT0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ovoinhibitor {ECO:0000303|PubMed:13944692, ECO:0000303|PubMed:23122126, ECO:0000303|PubMed:25436390, ECO:0000303|PubMed:8973172, ECO:0000312|EMBL:AAP50264.1};
DE Short=OI {ECO:0000303|PubMed:8973172};
DE Short=OvoI {ECO:0000303|PubMed:23122126};
DE AltName: Full=Serine protease inhibitor Kazal-type 5 {ECO:0000305};
DE AltName: Allergen=Gal d OIH {ECO:0000305};
GN Name=SPINK5 {ECO:0000305, ECO:0000312|Ensembl:ENSGALP00000005535,
GN ECO:0000312|Ensembl:ENSGALP00000071498}; Synonyms=OIH;
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] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-517, PROTEIN SEQUENCE OF 69-517
RP (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Oviduct {ECO:0000303|PubMed:3571241};
RX PubMed=3571241; DOI=10.1016/s0021-9258(18)45659-1;
RA Scott M.J., Huckaby C.S., Kato I., Kohr W.J., Laskowski M. Jr., Tsai M.-J.,
RA O'Malley B.W.;
RT "Ovoinhibitor introns specify functional domains as in the related and
RT linked ovomucoid gene.";
RL J. Biol. Chem. 262:5899-5907(1987).
RN [3]
RP PROTEIN SEQUENCE OF 82-93; 92-117; 116-125; 133-148; 147-158; 189-197;
RP 216-224; 223-251; 262-278; 321-329; 391-404; 457-465; 472-496 AND 495-508,
RP TISSUE SPECIFICITY, 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 [4]
RP PROTEIN SEQUENCE OF 83-92 AND 149-157, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Bursa of Fabricius {ECO:0000303|PubMed:15252730};
RX PubMed=15252730; DOI=10.1007/s00441-004-0910-x;
RA Moore R.W., Hargis B.M., Porter T.E., Caldwell D.Y., Oubre C.M.,
RA Vandesande F., Berghman L.R.;
RT "Ovoinhibitor in the chicken bursa of Fabricius: identification, isolation,
RT and localization.";
RL Cell Tissue Res. 317:247-251(2004).
RN [5]
RP PROTEIN SEQUENCE OF 93-116; 134-147; 190-213; 197-216; 224-250; 261-277;
RP 263-277; 473-495 AND 508-517, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Egg yolk {ECO:0000303|PubMed:22010862};
RX PubMed=22010862; DOI=10.1021/jf203339t;
RA Bourin M., Gautron J., Berges M., Attucci S., Le Blay G., Labas V., Nys Y.,
RA Rehault-Godbert S.;
RT "Antimicrobial potential of egg yolk ovoinhibitor, a multidomain Kazal-like
RT inhibitor of chicken egg.";
RL J. Agric. Food Chem. 59:12368-12374(2011).
RN [6] {ECO:0000312|EMBL:AAP50264.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-512.
RX PubMed=15265086; DOI=10.1111/j.1365-2052.2004.01159.x;
RA Kinoshita K., Shimogiri T., Okamoto S., Yoshizawa K., Mannen H.,
RA Ibrahim H.R., Cheng H.H., Maeda Y.;
RT "Linkage mapping of chicken ovoinhibitor and ovomucoid genes to chromosome
RT 13.";
RL Anim. Genet. 35:356-358(2004).
RN [7]
RP FUNCTION.
RX PubMed=13944692;
RA Feeney R.E., Stevens F.C., Osuga D.T.;
RT "The specificities of chicken ovomucoid and ovoinhibitor.";
RL J. Biol. Chem. 238:1415-1418(1963).
RN [8]
RP FUNCTION, AND DOMAIN.
RX PubMed=6904299; DOI=10.1111/j.1432-1033.1980.tb04900.x;
RA Gertler A., Ben-Valid I.;
RT "Stoichiometry of interaction of chicken ovoinhibitor with pancreatic
RT trypsin, chymotrypsin and elastase I.";
RL Eur. J. Biochem. 110:571-577(1980).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=6838526; DOI=10.1016/0006-291x(83)91262-7;
RA Matsuda T., Watanabe K., Nakamura R.;
RT "Ovomucoid and ovoinhibitor isolated from chicken egg white are
RT immunologically cross-reactive.";
RL Biochem. Biophys. Res. Commun. 110:75-81(1983).
RN [10]
RP GLYCOSYLATION, AND MISCELLANEOUS.
RX PubMed=3025257; DOI=10.1172/jci112775;
RA Yolken R.H., Willoughby R., Wee S.B., Miskuff R., Vonderfecht S.;
RT "Sialic acid glycoproteins inhibit in vitro and in vivo replication of
RT rotaviruses.";
RL J. Clin. Invest. 79:148-154(1987).
RN [11]
RP FUNCTION.
RX PubMed=8973172; DOI=10.1021/bi961452k;
RA Moss G.W.J., Marshall J., Morabito M., Howe J.R., Moczydlowski E.;
RT "An evolutionarily conserved binding site for serine proteinase inhibitors
RT in large conductance calcium-activated potassium channels.";
RL Biochemistry 35:16024-16035(1996).
RN [12]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11572089; DOI=10.1007/s004410100414;
RA Zhu Y., Wang M., Lin H., Li Z., Luo J.;
RT "Identification of estrogen-responsive genes in chick liver.";
RL Cell Tissue Res. 305:357-363(2001).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND BIOTECHNOLOGY.
RX PubMed=14519973; DOI=10.1271/bbb.67.1897;
RA Begum S., Saito A., Xu X., Kato A.;
RT "Improved functional properties of the ovoinhibitor by conjugating with
RT galactomannan.";
RL Biosci. Biotechnol. Biochem. 67:1897-1902(2003).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14609095; DOI=10.1002/food.200390082;
RA Begum S., Saito A., Kato A., He J., Azakami H.;
RT "Expression and characterization of chicken ovoinhibitor in Pichia
RT pastoris.";
RL Nahrung 47:359-363(2003).
RN [15]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=23122126; DOI=10.1016/j.foodchem.2012.07.106;
RA Martos G., Lopez-Fandino R., Molina E.;
RT "Immunoreactivity of hen egg allergens: influence on in vitro
RT gastrointestinal digestion of the presence of other egg white proteins and
RT of egg yolk.";
RL Food Chem. 136:775-781(2013).
CC -!- FUNCTION: Serine protease inhibitor involved in antimicrobial egg
CC defense preventing contamination of table eggs (non-fertilized eggs)
CC and protecting the chick embryo (fertilized eggs) (Probable). Inhibits
CC trypsin, chymotrypsin, elastase, subtilisin and a proteinase of fungus
CC Aspergillus oryzae (PubMed:13944692, PubMed:6904299, PubMed:6838526,
CC PubMed:14519973, PubMed:14609095, PubMed:22010862). Inhibits calcium-
CC activated potassium channels KCNMA1 (bovine) and slo (Drosophila)
CC (PubMed:8973172). Has antibacterial activity against B.thuringiensis
CC LMSA 3.06.004, but not against S.aureus CIP 103 811, P.aeruginosa PAO1,
CC B.cereus ATCC6464 or B.subtilis ATCC 6633 (PubMed:22010862).
CC {ECO:0000269|PubMed:13944692, ECO:0000269|PubMed:14519973,
CC ECO:0000269|PubMed:14609095, ECO:0000269|PubMed:22010862,
CC ECO:0000269|PubMed:6838526, ECO:0000269|PubMed:6904299,
CC ECO:0000269|PubMed:8973172, ECO:0000305|PubMed:22010862}.
CC -!- INTERACTION:
CC P10184; P00766; Xeno; NbExp=2; IntAct=EBI-6663991, EBI-6664027;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22010862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10184-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10184-2; Sequence=VSP_060580;
CC -!- TISSUE SPECIFICITY: Expressed in oviduct (at protein level)
CC (PubMed:3571241). Expressed in egg white (at protein level)
CC (PubMed:6838526, PubMed:14519973, PubMed:23122126, PubMed:25436390).
CC Expressed in egg yolk plasma of non-fertilized eggs (at protein level)
CC (PubMed:22010862). Expressed in the magnum of the oviduct (at protein
CC level) (PubMed:25436390). Expressed in oviduct (PubMed:3571241,
CC PubMed:14609095). Expressed in liver (PubMed:3571241, PubMed:11572089,
CC PubMed:22010862). Expressed in the cortico-medullary border region of
CC the bursa of Fabricius by the bursal secretory dendritic-like cells
CC (PubMed:15252730). Highly expressed in the magnum of the oviduct, and
CC at a lower level in uterus. Weakly expressed in white isthmus and very
CC weakly in infundibulum. Not expressed in duodenum and kidney
CC (PubMed:22010862). {ECO:0000269|PubMed:11572089,
CC ECO:0000269|PubMed:14519973, ECO:0000269|PubMed:14609095,
CC ECO:0000269|PubMed:15252730, ECO:0000269|PubMed:22010862,
CC ECO:0000269|PubMed:23122126, ECO:0000269|PubMed:25436390,
CC ECO:0000269|PubMed:3571241, ECO:0000269|PubMed:6838526}.
CC -!- DEVELOPMENTAL STAGE: Expressed in liver of pre-laying and egg-laying
CC hens throughout sexual maturation. Expression increases gradually from
CC 13 weeks of age reaching its maximum at 15 weeks of age (pre-laying
CC hens). A significant decrease in expression is observed in 41-week-old
CC hens (egg-laying), a level that is significantly lower than that
CC measured initially in 13-week-old pullets.
CC {ECO:0000269|PubMed:22010862}.
CC -!- INDUCTION: Expression is regulated by dietary stress. Significantly
CC increased expression between days 0 to 5 in egg whites of eggs laid by
CC corticosterone-fed hens (at protein level). Decreased expression at day
CC 14 in the magnum of the oviduct in the corticosterone-fed laying hens
CC (PubMed:25436390). Significantly increased expression by estrogen.
CC Rapidly up-regulated within 0.5 hour after extrogen exposure with a
CC peak at 1-4 hours and diminishing thereafter (PubMed:11572089). Up-
CC regulated during sexual maturation of pullets (PubMed:22010862).
CC {ECO:0000269|PubMed:11572089, ECO:0000269|PubMed:22010862,
CC ECO:0000269|PubMed:25436390}.
CC -!- DOMAIN: Seems to have at least five separate non-overlapping active
CC inhibitory domains; two for trypsin, two for chymotrypsin and one for
CC elastase. They can be bound to the domains simultaneously.
CC {ECO:0000269|PubMed:6904299}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:3025257}.
CC -!- ALLERGEN: Causes an allergic reaction in humans. Binds to IgE of egg-
CC allergic patients. Immunoreactivity is lost by simulated gastric and
CC gastroduodenal digestion (PubMed:23122126). Binds to rabbit anti-
CC ovomucoid IgG antibody indicating the cross-reactivity between this
CC protein and the ovomucoid protein from egg white (PubMed:6838526).
CC {ECO:0000269|PubMed:23122126, ECO:0000269|PubMed:6838526}.
CC -!- BIOTECHNOLOGY: The galactomannan conjugate of this protein prepared
CC through the Maillard reaction shows almost the same inhibitory activity
CC toward trypsin, chymotrypsin and elastase, with stronger heat and
CC emulsion stability, and better emulsifying properties than the
CC untreated protein. The conjugate can therefore be useful for industrial
CC application. {ECO:0000269|PubMed:14519973}.
CC -!- MISCELLANEOUS: Prevents symptomatic gastoroenteritis in vivo in a mouse
CC model of rotavirus infection. Significantly inhibits intestinal
CC replication of EDIM strain of murine rotavirus in infant mice up to 4
CC days after intragastrical administration of the virus.
CC {ECO:0000269|PubMed:3025257}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA48994.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AADN05000072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M16141; AAA48994.1; ALT_INIT; Genomic_DNA.
DR EMBL; M15962; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16127; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16128; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16129; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16130; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16131; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16132; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16133; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16134; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16135; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16136; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16137; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16138; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16139; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; M16140; AAA48994.1; JOINED; Genomic_DNA.
DR EMBL; AY225161; AAP50264.1; -; Genomic_DNA.
DR PIR; A26730; A26730.
DR AlphaFoldDB; P10184; -.
DR SMR; P10184; -.
DR IntAct; P10184; 1.
DR STRING; 9031.ENSGALP00000005535; -.
DR Allergome; 10163; Gal d OIH.
DR MEROPS; I01.004; -.
DR MEROPS; I01.006; -.
DR PaxDb; P10184; -.
DR Ensembl; ENSGALT00000005545; ENSGALP00000005535; ENSGALG00000031496. [P10184-1]
DR Ensembl; ENSGALT00000103221; ENSGALP00000071498; ENSGALG00000031496. [P10184-2]
DR VEuPathDB; HostDB:geneid_416235; -.
DR GeneTree; ENSGT00940000165772; -.
DR HOGENOM; CLU_579946_0_0_1; -.
DR InParanoid; P10184; -.
DR OMA; SIQKMSM; -.
DR OrthoDB; 1283825at2759; -.
DR PhylomeDB; P10184; -.
DR PRO; PR:P10184; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000031496; Expressed in liver and 9 other tissues.
DR GO; GO:0005576; C:extracellular region; TAS:AgBase.
DR GO; GO:0005615; C:extracellular space; TAS:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:AgBase.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:AgBase.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:AgBase.
DR GO; GO:0002020; F:protease binding; IDA:AgBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:AgBase.
DR GO; GO:0051412; P:response to corticosterone; IDA:AgBase.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF00050; Kazal_1; 7.
DR SMART; SM00280; KAZAL; 7.
DR SUPFAM; SSF100895; SSF100895; 7.
DR PROSITE; PS00282; KAZAL_1; 7.
DR PROSITE; PS51465; KAZAL_2; 7.
PE 1: Evidence at protein level;
KW Allergen; Alternative splicing; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Repeat; Secreted; Serine protease inhibitor.
FT CHAIN 1..517
FT /note="Ovoinhibitor"
FT /id="PRO_0000016578"
FT DOMAIN 67..132
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 133..197
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 198..263
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 264..329
FT /note="Kazal-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 330..394
FT /note="Kazal-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 395..460
FT /note="Kazal-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 461..517
FT /note="Kazal-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 92..93
FT /note="Reactive bond 1 for trypsin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 157..158
FT /note="Reactive bond 2 for trypsin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 223..224
FT /note="Reactive bond 3 for trypsin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 289..290
FT /note="Reactive bond 4 for trypsin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 354..355
FT /note="Reactive bond 5 for chymotrypsin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 420..421
FT /note="Reactive bond 6 for chymotrypsin and elastase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 479..480
FT /note="Reactive bond 7 for chymotrypsin and elastase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 90..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 98..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 139..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 155..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 163..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 204..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 221..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 229..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 270..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 287..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 295..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 336..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 352..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 360..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 401..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 418..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 426..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 467..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 477..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 485..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1..70
FT /note="MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQF
FT VQVALALCCFADIAFGIE -> MIPQ (in isoform 2)"
FT /id="VSP_060580"
FT CONFLICT 136
FT /note="T -> M (in Ref. 2; AAA48994/AA sequence and 5; AA
FT sequence)"
FT CONFLICT 378
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 57005 MW; A3E2DE5570597C1C CRC64;
MTDWVLHHKV GPLDMTTRYI FPLLPLPFLP HSESKRAVCA PRCSAMRTAR QFVQVALALC
CFADIAFGIE VNCSLYASGI GKDGTSWVAC PRNLKPVCGT DGSTYSNECG ICLYNREHGA
NVEKEYDGEC RPKHVTIDCS PYLQVVRDGN TMVACPRILK PVCGSDSFTY DNECGICAYN
AEHHTNISKL HDGECKLEIG SVDCSKYPST VSKDGRTLVA CPRILSPVCG TDGFTYDNEC
GICAHNAEQR THVSKKHDGK CRQEIPEIDC DQYPTRKTTG GKLLVRCPRI LLPVCGTDGF
TYDNECGICA HNAQHGTEVK KSHDGRCKER STPLDCTQYL SNTQNGEAIT ACPFILQEVC
GTDGVTYSND CSLCAHNIEL GTSVAKKHDG RCREEVPELD CSKYKTSTLK DGRQVVACTM
IYDPVCATNG VTYASECTLC AHNLEQRTNL GKRKNGRCEE DITKEHCREF QKVSPICTME
YVPHCGSDGV TYSNRCFFCN AYVQSNRTLN LVSMAAC
