IPSG_FELCA
ID IPSG_FELCA Reviewed; 111 AA.
AC P08480;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Submandibular gland;
RX PubMed=3304339; DOI=10.1515/bchm3.1987.368.1.717;
RA Reisinger P.W.M., Hochstrasser K., Gottlicher I., Eulitz M., Wachter E.;
RT "The amino-acid sequences of the double-headed proteinase inhibitors from
RT cat, lion and dog submandibular glands.";
RL Biol. Chem. Hoppe-Seyler 368:717-726(1987).
CC -!- FUNCTION: This inhibitor is composed of two homologous actively
CC inhibiting halves: one which inhibits trypsin, the other which inhibits
CC elastase.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR PIR; A29654; A29654.
DR AlphaFoldDB; P08480; -.
DR SMR; P08480; -.
DR MEROPS; I01.016; -.
DR MEROPS; I01.017; -.
DR Ensembl; ENSFCAT00000023759; ENSFCAP00000019986; ENSFCAG00000030926.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00520000060726; -.
DR HOGENOM; CLU_087965_2_1_1; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000030926; Expressed in zone of skin and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001239; Prot_inh_Kazal-m.
DR Pfam; PF00050; Kazal_1; 2.
DR PRINTS; PR00290; KAZALINHBTR.
DR SMART; SM00280; KAZAL; 2.
DR SUPFAM; SSF100895; SSF100895; 2.
DR PROSITE; PS00282; KAZAL_1; 2.
DR PROSITE; PS51465; KAZAL_2; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor.
FT CHAIN 1..111
FT /note="Double-headed protease inhibitor, submandibular
FT gland"
FT /id="PRO_0000073036"
FT DOMAIN 2..62
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 63..111
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 22..23
FT /note="Reactive bond 1 for trypsin"
FT SITE 73..74
FT /note="Reactive bond 2 for elastase"
FT DISULFID 8..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 20..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 28..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 64..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 71..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 79..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 111 AA; 12788 MW; FB2548A726A0C1EC CRC64;
ASPPEVNCSQ YNRKGSGITC SKEWKPICGI DHKTYSNECM FCQLNQNKRF QLRKLHDNKC
QIECTNYSAI CTMEYFPLCG SDGQEYSNKC LFCNEVVKRR GTLFLAKYGQ C