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VKT1_HETMG
ID   VKT1_HETMG              Reviewed;          56 AA.
AC   C0HK72;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Kunitz-type serine protease inhibitor HMRG1 {ECO:0000303|PubMed:29191747};
DE   AltName: Full=PI-stichotoxin-Hmg3a {ECO:0000305};
DE            Short=PI-SHTX-Hmg3a {ECO:0000305};
OS   Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Stichodactylidae; Heteractis.
OX   NCBI_TaxID=38281 {ECO:0000303|PubMed:29191747};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND PRESENCE OF DISULFIDE
RP   BONDS.
RX   PubMed=29191747; DOI=10.1016/j.jprot.2017.11.019;
RA   Sintsova O., Gladkikh I., Chausova V., Monastyrnaya M., Anastyuk S.,
RA   Chernikov O., Yurchenko E., Aminin D., Isaeva M., Leychenko E.,
RA   Kozlovskaya E.;
RT   "Peptide fingerprinting of the sea anemone Heteractis magnifica mucus
RT   revealed neurotoxins, Kunitz-type proteinase inhibitors and a new beta-
RT   defensin alpha-amylase inhibitor.";
RL   J. Proteomics 173:12-21(2018).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin (Ki=50 nM)
CC       and probably also chymotrypsin (Kd=1.6 nM). Has an anti-inflammatory
CC       effect in LPS-activated macrophages in vitro, specifically reducing
CC       release of TNF and IL6 but not nitric oxide and reducing expression of
CC       IL1B precursor. {ECO:0000250|UniProtKB:C0HJU7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- PTM: Contains three disulfide bonds. {ECO:0000269|PubMed:29191747}.
CC   -!- MASS SPECTROMETRY: Mass=6152.93; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29191747};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2
CC       potassium channel toxin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HK72; -.
DR   SMR; C0HK72; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; 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; Nematocyst; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..56
FT                   /note="Kunitz-type serine protease inhibitor HMRG1"
FT                   /evidence="ECO:0000269|PubMed:29191747"
FT                   /id="PRO_0000443113"
FT   DOMAIN          4..54
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            14..15
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P31713"
FT   DISULFID        4..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        13..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   56 AA;  6157 MW;  784379275B8F3369 CRC64;
     RGICLEPKVV GPCKARIRRF YYDSETGKCT PFIYGGCGGN GNNFETLHAC RGICRA
 
 
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