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VKT3_VIPAA
ID   VKT3_VIPAA              Reviewed;          93 AA.
AC   P00992; Q6XPY7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Kunitz-type serine protease inhibitor 3;
DE   AltName: Full=Venom basic protease inhibitor 3;
DE   AltName: Full=Venom chymotrypsin inhibitor;
DE            Short=cVamChi;
DE   Flags: Precursor;
OS   Vipera ammodytes ammodytes (Western sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=8705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12860400; DOI=10.1016/s0014-5793(03)00693-8;
RA   Zupunski V., Kordis D., Gubensek F.;
RT   "Adaptive evolution in the snake venom Kunitz/BPTI protein family.";
RL   FEBS Lett. 547:131-136(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-89, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RA   Ritonja A., Meloun B., Gubensek F.;
RT   "The primary structure of Vipera ammodytes venom chymotrypsin inhibitor.";
RL   Biochim. Biophys. Acta 746:138-145(1983).
RN   [3]
RP   AMINO-ACID COMPOSITION, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=6602050; DOI=10.1111/j.1432-1033.1983.tb07481.x;
RA   Ritonja A., Turk V., Gubensek F.;
RT   "Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and
RT   kinetic studies.";
RL   Eur. J. Biochem. 133:427-432(1983).
CC   -!- FUNCTION: Serine protease inhibitor that principally inhibits alpha-
CC       chymotrypsin (Ki=4.3 nM). Shows weak inhibition on trypsin (Ki=5100
CC       nM), and plasma kallikrein. {ECO:0000269|PubMed:6602050,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.2}.
CC   -!- MISCELLANEOUS: Does not inhibit plasmin, and pancreatic kallikrein.
CC       {ECO:0000305|PubMed:6602050}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AY217782; AAP04485.1; -; mRNA.
DR   PIR; A01223; TIVIVC.
DR   AlphaFoldDB; P00992; -.
DR   SMR; P00992; -.
DR   MEROPS; I02.062; -.
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|Ref.2"
FT   CHAIN           25..89
FT                   /note="Kunitz-type serine protease inhibitor 3"
FT                   /id="PRO_0000155445"
FT   PROPEP          90..93
FT                   /id="PRO_0000377479"
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                   ECO:0000269|Ref.2"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|Ref.2"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|Ref.2"
FT   CONFLICT        46
FT                   /note="S -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..51
FT                   /note="DS -> NP (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="K -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   93 AA;  10330 MW;  9E839122108BD209 CRC64;
     MSSGGLLLLL GLLTLWAELT PVSTRDRPKF CYLPADPGRC LAYMPSFYYD SASNKCKKFI
     YGGCRGNANN FKTWDECRHT CVASGIQPRI ASN
 
 
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