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VKT_BUNFA
ID   VKT_BUNFA               Reviewed;          83 AA.
AC   B2KTG1;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Kunitz-type serine protease inhibitor bungaruskunin;
DE   Flags: Precursor;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-53, MASS SPECTROMETRY,
RP   AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18164783; DOI=10.1016/j.peptides.2007.11.013;
RA   Lu J., Yang H., Yu H., Gao W., Lai R., Liu J., Liang X.;
RT   "A novel serine protease inhibitor from Bungarus fasciatus venom.";
RL   Peptides 29:369-374(2008).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin, chymotrypsin
CC       and elastase, but does not inhibit thrombin.
CC       {ECO:0000269|PubMed:18164783}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=6752.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18164783};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; EU220207; ABY71036.1; -; mRNA.
DR   AlphaFoldDB; B2KTG1; -.
DR   SMR; B2KTG1; -.
DR   MEROPS; I02.022; -.
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; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:18164783"
FT   CHAIN           25..83
FT                   /note="Kunitz-type serine protease inhibitor bungaruskunin"
FT                   /id="PRO_0000377462"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            41..42
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..81
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   83 AA;  9316 MW;  A8762C1B78484679 CRC64;
     MSSGGLLLLL GLLTLWTELT PVSSLGGPAY CKLPPEPGPC HEYKHAFYYN PDARECEEFI
     YGGCKGNKNN FKTRHECHRV CVR
 
 
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