VKT5_OXYMI
ID VKT5_OXYMI Reviewed; 79 AA.
AC B5L5Q6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Kunitz-type serine protease inhibitor microlepidin-5;
DE Flags: Precursor;
OS Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=111177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Venom gland;
RX PubMed=18979207; DOI=10.1007/s00018-008-8573-5;
RA St Pierre L., Earl S.T., Filippovich I., Sorokina N., Masci P.P.,
RA De Jersey J., Lavin M.F.;
RT "Common evolution of waprin and Kunitz-like toxin families in Australian
RT venomous snakes.";
RL Cell. Mol. Life Sci. 65:4039-4054(2008).
CC -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU401844; ACC77793.1; -; Genomic_DNA.
DR AlphaFoldDB; B5L5Q6; -.
DR SMR; B5L5Q6; -.
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 3: Inferred from homology;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..79
FT /note="Kunitz-type serine protease inhibitor microlepidin-
FT 5"
FT /id="PRO_5000395644"
FT DOMAIN 31..79
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 40..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 56..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 79 AA; 8788 MW; 28B71EF2FEEE32B9 CRC64;
MSSGGLLLLL GLLTLWEVLT PVSSKDRPKF YELPADIGPC EDFTGAFHYS PREHECIEFI
YGGCEGNANN FNTLEECET
