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VMPA1_TITSE
ID   VMPA1_TITSE             Reviewed;         394 AA.
AC   P86392; A0A076L876; V9Z8X8;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 4.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Venom metalloproteinase antarease TserMP_A;
DE            Short=VMPA;
DE            EC=3.4.24.-;
DE   AltName: Full=Metalloserrulase 1 {ECO:0000303|PubMed:25091350};
DE            Short=TsMS 1 {ECO:0000303|PubMed:25091350};
DE   Flags: Precursor;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1] {ECO:0000312|EMBL:AIJ02109.2}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=25091350; DOI=10.1016/j.toxicon.2014.07.014;
RA   Carmo A.O., Oliveira-Mendes B.B., Horta C.C., Magalhaes B.F., Dantas A.E.,
RA   Chaves L.M., Chavez-Olortegui C., Kalapothakis E.;
RT   "Molecular and functional characterization of metalloserrulases, new
RT   metalloproteases from the Tityus serrulatus venom gland.";
RL   Toxicon 90:45-55(2014).
RN   [2] {ECO:0000312|EMBL:AHE40588.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 159-393.
RC   TISSUE=Venom gland;
RX   PubMed=24361608; DOI=10.1016/j.bbagen.2013.12.012;
RA   Ortiz E., Rendon-Anaya M., Rego S.C., Schwartz E.F., Possani L.D.;
RT   "Antarease-like Zn-metalloproteases are ubiquitous in the venom of
RT   different scorpion genera.";
RL   Biochim. Biophys. Acta 1840:1738-1746(2014).
RN   [3]
RP   PROTEIN SEQUENCE OF 158-194 AND 203-393, FUNCTION, ACTIVITY REGULATION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=20026600; DOI=10.1074/jbc.m109.028365;
RA   Fletcher P.L. Jr., Fletcher M.D., Weninger K., Anderson T.E., Martin B.M.;
RT   "Vesicle-associated membrane protein (VAMP) cleavage by a new
RT   metalloprotease from the Brazilian scorpion Tityus serrulatus.";
RL   J. Biol. Chem. 285:7405-7416(2010).
CC   -!- FUNCTION: Acts as a metalloprotease. Penetrates intact tissue and
CC       specifically cleaves the vesicle-associated membrane protein 2 (VAMP2)
CC       (part of the SNARE complex) involved in pancreatic secretion, thus
CC       disrupting the normal vesicular traffic. {ECO:0000269|PubMed:20026600}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q3ZD74};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q3ZD74};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:20026600}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20026600}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20026600}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000305|PubMed:25091350}.
CC   -!- MASS SPECTROMETRY: Mass=25500; Mass_error=100; Method=SELDI;
CC       Evidence={ECO:0000269|PubMed:20026600};
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   EMBL; KM115016; AIJ02109.2; -; mRNA.
DR   EMBL; KC693035; AHE40588.1; -; mRNA.
DR   AlphaFoldDB; P86392; -.
DR   SMR; P86392; -.
DR   MEROPS; M12.191; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..157
FT                   /evidence="ECO:0000305|PubMed:20026600,
FT                   ECO:0000305|PubMed:25091350"
FT                   /id="PRO_0000455749"
FT   CHAIN           158..394
FT                   /note="Venom metalloproteinase antarease TserMP_A"
FT                   /id="PRO_0000391698"
FT   DOMAIN          162..391
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        295..386
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CONFLICT        340
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362
FT                   /note="K -> KV (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="T -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  42975 MW;  6E428AA50F6CD603 CRC64;
     MISYLASIFL LATVSAVPSG RVEVVFPSVE TSRSGVKTVK FTALDQDVEL KLRSAGEILG
     KRFAIQDVDV ESLRRKIYRD SVNGAALLID EDGPLTIEGI VNSKLRIQPF ESGRITKDGI
     IAHQIVEVID DKKSYDRVAV IPENVKRNAE NVSRMARDDD CIVVEYYIVT DSAFTKRFKS
     NSALTNYVTV MFTGVQNLMD TLELGIGVRL LGVTTFTEKT EPSFIKDNLI PGPPAAFDPD
     VLISAMSKYY CNHQTGLAKD TDLIFLITAR GMGDPREDGT VDINTAGIAN SAGVCKPCFK
     SGIATDDSDY NERVDTLAHE SVHLLGSPHD GEGPNLVSLE GSPGAANCPA KAGYIMGNRN
     DKNKYKFSPC TKKCVEYLLS KPTASCIFQQ CTDF
 
 
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