GUAM_HIRNI
ID GUAM_HIRNI Reviewed; 57 AA.
AC P46443;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Guamerin;
OS Hirudo nipponia (Korean blood-sucking leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX NCBI_TaxID=42736;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7775446; DOI=10.1074/jbc.270.23.13879;
RA Jung H.I., Kim S.I., Ha K.-S., Joe C.O., Kang K.W.;
RT "Isolation and characterization of guamerin, a new human leukocyte elastase
RT inhibitor from Hirudo nipponia.";
RL J. Biol. Chem. 270:13879-13884(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHYMOTRYPSIN,
RP FUNCTION, MUTAGENESIS OF MET-36, AND DISULFIDE BONDS.
RX PubMed=18155725; DOI=10.1016/j.jmb.2007.11.089;
RA Kim H., Chu T.T.T., Kim D.Y., Kim D.R., Nguyen C.M.T., Choi J., Lee J.-R.,
RA Hahn M.-J., Kim K.K.;
RT "The crystal structure of guamerin in complex with chymotrypsin and the
RT development of an elastase-specific inhibitor.";
RL J. Mol. Biol. 376:184-192(2008).
CC -!- FUNCTION: Inhibits mammalian elastases. {ECO:0000269|PubMed:18155725}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Not found in the saliva, but in the body tissues.
CC -!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.
CC {ECO:0000305}.
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DR PIR; A57537; A57537.
DR PDB; 3BG4; X-ray; 2.50 A; D=1-57.
DR PDBsum; 3BG4; -.
DR AlphaFoldDB; P46443; -.
DR SMR; P46443; -.
DR MEROPS; I15.005; -.
DR EvolutionaryTrace; P46443; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR011061; Hirudin/antistatin.
DR InterPro; IPR008086; Prot_inh_I15_antistasin_leech.
DR Pfam; PF02822; Antistasin; 1.
DR PRINTS; PR01706; ANTISTASIN.
DR SUPFAM; SSF57262; SSF57262; 1.
DR PROSITE; PS51252; ANTISTASIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Secreted; Serine protease inhibitor.
FT CHAIN 1..57
FT /note="Guamerin"
FT /id="PRO_0000155196"
FT DOMAIN 30..56
FT /note="Antistasin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT SITE 36..37
FT /note="Reactive bond"
FT DISULFID 12..23
FT /evidence="ECO:0000269|PubMed:18155725"
FT DISULFID 17..28
FT /evidence="ECO:0000269|PubMed:18155725"
FT DISULFID 30..50
FT /evidence="ECO:0000269|PubMed:18155725"
FT DISULFID 35..54
FT /evidence="ECO:0000269|PubMed:18155725"
FT DISULFID 39..56
FT /evidence="ECO:0000269|PubMed:18155725"
FT MUTAGEN 36
FT /note="M->A: Increases inhibition of elastase and decreases
FT inhibition of chymotrypsin."
FT /evidence="ECO:0000269|PubMed:18155725"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3BG4"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3BG4"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3BG4"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3BG4"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3BG4"
SQ SEQUENCE 57 AA; 6123 MW; C5116BE6E5481D7B CRC64;
VDENAEDTHG LCGEKTCSPA QVCLNNECAC TAIRCMIFCP NGFKVDENGC EYPCTCA
