ID U3FVH1_MICFL Unreviewed; 83 AA.
AC U3FVH1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Kunitz inhibitor 3 {ECO:0000313|EMBL:JAB52836.1};
DE SubName: Full=Kunitz-type protease inhibitor 5 {ECO:0000313|EMBL:JAI09063.1};
OS Micrurus fulvius (Eastern coral snake) (Coluber fulvius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=8637 {ECO:0000313|EMBL:JAB52836.1};
RN [1] {ECO:0000313|EMBL:JAB52836.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAB52836.1};
RX PubMed=23915248; DOI=10.1186/1471-2164-14-531;
RA Margres M.J., Aronow K., Loyacano J., Rokyta D.R.;
RT "The venom-gland transcriptome of the eastern coral snake (Micrurus
RT fulvius) reveals high venom complexity in the intragenomic evolution of
RT venoms.";
RL BMC Genomics 14:531-531(2013).
RN [2] {ECO:0000313|EMBL:JAI09063.1}
RP NUCLEOTIDE SEQUENCE.
RA Margres M.J., Wray K.P., McGivern J.J., Seavy M., Sanader D., Facente J.,
RA Rokyta D.R.;
RT "The extremes of toxin expression variation revealed in two sympatric snake
RT species.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:JAS05052.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26358130; DOI=10.1534/g3.115.020578;
RA Rokyta D.R., Margres M.J., Calvin K.;
RT "Post-transcriptional mechanisms contribute little to phenotypic variation
RT in snake venoms.";
RL G3 (Bethesda) 5:2375-2382(2015).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; GAEP01001985; JAB52836.1; -; mRNA.
DR EMBL; GBEW01001302; JAI09063.1; -; mRNA.
DR EMBL; GDBF01000034; JAS05052.1; -; Transcribed_RNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22594; Kunitz_textilinin-like; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083:SF377; BPTI_KUNITZ INHIBITOR DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:JAI09063.1};
KW Protease {ECO:0000313|EMBL:JAI09063.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..83
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010687033"
FT DOMAIN 31..81
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 83 AA; 9079 MW; 2F67F5B06CDF6066 CRC64;
MSSGGLLLLL GLLTLWAELT PVSSFQRPKL CSLPSETGKC NARKISFYYN PDSNKCQKFV
YGGCGGNANN FKTIHECQRT CIG
//
