IATR_CAPHI
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 25-MAY-2022, entry version 64.
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:UniProtKB-KW.
DR CDD; cd00109; KU; 2.
DR Gene3D; 4.10.410.10; -; 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; PTHR46676; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; SSF57362; 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
