VKT2_HEMHA
ID VKT2_HEMHA Reviewed; 57 AA.
AC P00985;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Kunitz-type serine protease inhibitor 2;
DE AltName: Full=Venom basic protease inhibitor 2;
OS Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Hemachatus.
OX NCBI_TaxID=8626;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=950337; DOI=10.1093/oxfordjournals.jbchem.a131100;
RA Hokama Y., Iwanaga S., Tatsuki T., Suzuki T.;
RT "Snake venom proteinase inhibitors. III. Isolation of five polypeptide
RT inhibitors from the venoms of Hemachatus haemachatus (Ringhal's corbra) and
RT Naja nivea (Cape cobra) and the complete amino acid sequences of two of
RT them.";
RL J. Biochem. 79:559-578(1976).
CC -!- FUNCTION: Serine protease inhibitor. {ECO:0000269|PubMed:950337}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR PIR; A01216; TIRIV2.
DR AlphaFoldDB; P00985; -.
DR SMR; P00985; -.
DR MEROPS; I02.055; -.
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; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..57
FT /note="Kunitz-type serine protease inhibitor 2"
FT /id="PRO_0000155438"
FT DOMAIN 5..55
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 15..16
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 57 AA; 6407 MW; 37CF03D3A03D7F2A CRC64;
RPDFCELPAE TGLCKAYIRS FHYNLAAQQC LQFIYGGCGG NANRFKTIDE CRRTCVG