ID V8NSI6_OPHHA Unreviewed; 292 AA.
AC V8NSI6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine protease 27 {ECO:0000313|EMBL:ETE64653.1};
DE Flags: Fragment;
GN Name=PRSS27 {ECO:0000313|EMBL:ETE64653.1};
GN ORFNames=L345_09581 {ECO:0000313|EMBL:ETE64653.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE64653.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE64653.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE64653.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000256|ARBA:ARBA00009228}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE64653.1}.
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DR EMBL; AZIM01002161; ETE64653.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NSI6; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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; 1.
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; PTHR24253:SF144; BRAIN-SPECIFIC SERINE PROTEASE 4; 1.
DR PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ETE64653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 21..272
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE64653.1"
SQ SEQUENCE 292 AA; 32081 MW; D80345416C9EFC53 CRC64;
MRKTLCSIKI CGRPKVHSPR IVGGKRAEEG EWPWQVSIRE NRLHVCGGSL ISSQWVVTAA
HCFDGPLVAS KYRVHLGEYE LPKPASTMVS SAVSLIVVHP YYAGVGLSAD IALVKLEEPV
HFSRTILPIC LSTVADPEPF PVGMMCWVTG WGDLYPDASF VTRTLQKLEM PILDIDKCDE
MYHNDSSSSD IDTEVLPKDY KLIYDDMICA GYPEGKKDSC QGDSGGPLAC KLNGTWFLAG
IVSFGVGCSE PNRPGVYTRV TSYMDWIQHT IEKNSVSNDG VPHAKSLLPS TQ
//
