ID E2E4H3_9SAUR Unreviewed; 250 AA.
AC E2E4H3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Kallikrein-Vpan1 {ECO:0000313|EMBL:ADK39254.1};
DE Flags: Fragment;
OS Varanus panoptes.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX NCBI_TaxID=169847 {ECO:0000313|EMBL:ADK39254.1};
RN [1] {ECO:0000313|EMBL:ADK39254.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VPAN_CL2Ct1 {ECO:0000313|EMBL:ADK39254.1};
RC TISSUE=Mandibular venom gland {ECO:0000313|EMBL:ADK39254.1};
RX PubMed=20631207; DOI=10.1074/mcp.M110.001370;
RA Fry B.G., Winter K., Norman J.A., Roelants K., Nabuurs R.J., van Osch M.J.,
RA Teeuwisse W.M., van der Weerd L., McNaughtan J.E., Kwok H.F., Scheib H.,
RA Greisman L., Kochva E., Miller L.J., Gao F., Karas J., Scanlon D., Lin F.,
RA Kuruppu S., Shaw C., Wong L., Hodgson W.C.;
RT "Functional and structural diversification of the Anguimorpha lizard venom
RT system.";
RL Mol. Cell. Proteomics 9:2369-2390(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000256|ARBA:ARBA00009228}.
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DR EMBL; GU441490; ADK39254.1; -; mRNA.
DR AlphaFoldDB; E2E4H3; -.
DR MEROPS; S01.435; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0035821; P:modulation of process of another organism; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 17..250
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADK39254.1"
SQ SEQUENCE 250 AA; 27189 MW; B4084261F0F25815 CRC64;
GVLLMHPSLV SANPMRITAG EECNEDSHPW LVLLTTESGT MCGATLLNQD WVLTAAHCYE
REKIWLSFGV HNREQRRGDE QVREAVGTFC YPDIPSTTNS SCPSFTLDRG DDIMLIKLNA
PVTYNEHIAP LALPDHAAPL GTECNIIGWG ETELIVGSAS DVPLCASIST KENQFCQDVY
QRNITDDMIC AGVLEGGPDA CRGDSGGPLL CGGQLQGLVS FGGYPCGEPM VPGVYTKIVK
YRKWIQSHML
//
