(data stored in ACNUC3659 zone)

HOVERGEN: VSP3_TRIMU

ID   VSP3_TRIMU              Reviewed;         257 AA.
AC   Q91509;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Mucrofibrase-3;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops
OS   mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=95110313; PubMed=7811255; DOI=10.1006/bbrc.1994.2865;
RA   Hung C.-C., Huang K.F., Chiou S.-H.;
RT   "Characterization of one novel venom protease with beta-fibrinogenase
RT   activity from the Taiwan habu (Trimeresurus mucrosquamatus):
RT   purification and cDNA sequence analysis.";
RL   Biochem. Biophys. Res. Commun. 205:1707-1715(1994).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves beta-
CC       chain of fibrinogen molecules efficiently and shows relatively
CC       lower activity on alpha-chain, with almost no activity on gamma-
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; X83223; CAA58223.1; -; mRNA.
DR   HSSP; P00760; 1EZX.
DR   SMR; Q91509; 25-256.
DR   MEROPS; S01.343; -.
DR   MEROPS; S01.344; -.
DR   HOVERGEN; Q91509; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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;
DR   PRODOM; Q91509.
DR   SWISS-2DPAGE; Q91509.
KW   Disulfide bond; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin; Zymogen.
FT   DOMAIN       10     64       PRODOM:2005.1:PD474467  1445
FT   DOMAIN       65    110       PRODOM:2005.1:PD623661  90
FT   DOMAIN      115    153       PRODOM:2005.1:PD702116  144
FT   DOMAIN      154    192       PRODOM:2005.1:PD745353  91
FT   DOMAIN      193    244       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     18       By similarity.
FT   PROPEP       19     24       By similarity.
FT                                /FTId=PRO_0000028411.
FT   CHAIN        25    257       Mucrofibrase-3.
FT                                /FTId=PRO_0000028412.
FT   DOMAIN       25    248       Peptidase S1.
FT   ACT_SITE     64     64       Charge relay system (By similarity).
FT   ACT_SITE    109    109       Charge relay system (By similarity).
FT   ACT_SITE    203    203       Charge relay system (By similarity).
FT   DISULFID     31    162       By similarity.
FT   DISULFID     49     65       By similarity.
FT   DISULFID     97    255       By similarity.
FT   DISULFID    141    209       By similarity.
FT   DISULFID    173    188       By similarity.
FT   DISULFID    199    224       By similarity.
SQ   SEQUENCE   257 AA;  28159 MW;  781E8531FB641416 CRC64;
     MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHPFLV LVYYDDYQCG GTLLNEEWVL
     TAAHCNGKDM EIYLGVHSKK VPNKDVQRRV PKEKFFCDSS KTYTKWNKDI MLIRLDRPVR
     KSAHIAPLSL PSSPPSVGSV CRVMGWGTIT SPQETYPDVP HCANINLLDY EVCRAAYAGL
     PATSRTLCAG ILEGGKDSCV GDSGGPLICN GQFQGIVSWG GDPCAQPREP GVYTNVFDHL
     DWIKGIIAGN TDVTCPL
//

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