ID   IATR_CAPHI              Reviewed;         123 AA.
AC   P62756; P13371;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-SEP-2026, entry version 74.
DE   RecName: Full=Inter-alpha-trypsin inhibitor;
DE            Short=ITI;
DE   AltName: Full=GIK-14;
DE   AltName: Full=Inhibitory fragment of ITI;
DE   Flags: Fragment;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2481505; DOI=10.1016/0167-4838(89)90017-4;
RA   Rasp G., Hochstrasser K., Gerl C., Wachter E.;
RT   "Primary structure of a proteinase inhibitor released from goat serum
RT   inter-alpha-trypsin inhibitor.";
RL   Biochim. Biophys. Acta 999:335-337(1989).
CC   -!- FUNCTION: This inhibitory fragment, released from native ITI after
CC       limited proteolysis with trypsin, contains two homologous domains.
CC       Whereas the second domain is a strong inhibitor of trypsin, the first
CC       domain interacts weakly with PMN-granulocytic elastase and not at all
CC       with pancreatic elastase.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: The amino acid at position p2' (17) appears to determine
CC       the specificity of the inhibition of domain I. Inhibitors with
CC       methionine in this position interact weakly with chymotrypsin and
CC       elastase; those with leucine interact strongly.
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DR   AlphaFoldDB; P62756; -.
DR   SMR; P62756; -.
DR   STRING; 9925.ENSCHIP00000033442; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd22597; Kunitz_bikunin_2-like; 1.
DR   FunFam; 4.10.410.10:FF:000005; Pancreatic trypsin inhibitor; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR   InterPro; IPR029856; AMBP.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   PANTHER; PTHR46676; PROTEIN AMBP; 1.
DR   PANTHER; PTHR46676:SF1; PROTEIN AMBP; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; BPTI-like; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Repeat; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           <1..>123
FT                   /note="Inter-alpha-trypsin inhibitor"
FT                   /id="PRO_0000155404"
FT   DOMAIN          5..55
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          61..111
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            15..16
FT                   /note="Reactive bond for chymotrypsin and elastase"
FT   SITE            71..72
FT                   /note="Reactive bond for trypsin"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        5..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        14..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        30..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        61..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        70..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        86..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   NON_TER         1
FT   NON_TER         123
SQ   SEQUENCE   123 AA;  13687 MW;  295038173F22D2D1 CRC64;
     KEDSCQLGYS QGPCLGMFKR YFYNGTSMAC ETFYYGGCMG NGNNFPSEKE CLQTCRTVQA
     CNLPIVRGPC RAGIELWAFD AVKGKCVRFI YGGCNGNGNQ FYSQKECKEY CGIPGEADEE
     LLR
//