ANTA_HAEGH
ID ANTA_HAEGH Reviewed; 119 AA.
AC P16242;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ghilanten;
OS Haementeria ghilianii (Amazon leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Haementeria.
OX NCBI_TaxID=6409;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Saliva;
RX PubMed=2306252; DOI=10.1016/0006-291x(90)91020-s;
RA Blankenship D.T., Brankamp R.G., Manley G.D., Cardin A.D.;
RT "Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle
RT of the South American leech, Haementeria ghilianii.";
RL Biochem. Biophys. Res. Commun. 166:1384-1389(1990).
CC -!- FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of
CC factor Xa. May have therapeutic utility as an anticoagulant. Also
CC exhibits a strong metastatic activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Binds to heparin-agarose, binds to sulfated
CC glycoconjugates.
CC -!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A34816; A34816.
DR AlphaFoldDB; P16242; -.
DR SMR; P16242; -.
DR MEROPS; I15.009; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS51252; ANTISTASIN; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Heparin-binding;
KW Protease inhibitor; Pyrrolidone carboxylic acid; Repeat; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..119
FT /note="Ghilanten"
FT /id="PRO_0000155193"
FT DOMAIN 28..53
FT /note="Antistasin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 83..108
FT /note="Antistasin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT BINDING 97..100
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT BINDING 111..118
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT SITE 34..35
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 89..90
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2306252"
FT DISULFID 8..19
FT /evidence="ECO:0000250"
FT DISULFID 13..26
FT /evidence="ECO:0000250"
FT DISULFID 28..48
FT /evidence="ECO:0000250"
FT DISULFID 33..51
FT /evidence="ECO:0000250"
FT DISULFID 37..53
FT /evidence="ECO:0000250"
FT DISULFID 62..73
FT /evidence="ECO:0000250"
FT DISULFID 67..80
FT /evidence="ECO:0000250"
FT DISULFID 82..103
FT /evidence="ECO:0000250"
FT DISULFID 88..106
FT /evidence="ECO:0000250"
FT DISULFID 92..108
FT /evidence="ECO:0000250"
SQ SEQUENCE 119 AA; 13318 MW; 5A94805DBBB850EF CRC64;
QGPFGPGCEE AGCPEGSACN IITDRCTCPE VRCRVYCSHG FQRSRYGCEV CRCRTEPMKA
TCDISECPEG MMCSRLTNKC DCKIDINCRK TCPNGLKRDK LGCEYCECKP KRKLVPRLS
