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Ghilanten

 ANTA_HAEGH              Reviewed;         119 AA.
P16242;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
25-OCT-2017, entry version 84.
RecName: Full=Ghilanten;
Haementeria ghilianii (Amazon leech).
Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea;
Rhynchobdellida; Glossiphoniidae; Haementeria.
NCBI_TaxID=6409;
[1]
PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
TISSUE=Saliva;
PubMed=2306252; DOI=10.1016/0006-291X(90)91020-S;
Blankenship D.T., Brankamp R.G., Manley G.D., Cardin A.D.;
"Amino acid sequence of ghilanten: anticoagulant-antimetastatic
principle of the South American leech, Haementeria ghilianii.";
Biochem. Biophys. Res. Commun. 166:1384-1389(1990).
-!- FUNCTION: This highly disulfide-bonded protein is a potent
inhibitor of factor Xa. May have therapeutic utility as an
anticoagulant. Also exhibits a strong metastatic activity.
-!- SUBCELLULAR LOCATION: Secreted.
-!- MISCELLANEOUS: Binds to heparin-agarose, binds to sulfated
glycoconjugates.
-!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin)
family. {ECO:0000305}.
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PIR; A34816; A34816.
ProteinModelPortal; P16242; -.
SMR; P16242; -.
MEROPS; I15.009; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
InterPro; IPR004094; Antistasin-like.
InterPro; IPR011061; Hirudin/antistatin.
InterPro; IPR008086; Prot_inh_I15_antistasin_leech.
Pfam; PF02822; Antistasin; 1.
PRINTS; PR01706; ANTISTASIN.
SUPFAM; SSF57262; SSF57262; 2.
PROSITE; PS51252; ANTISTASIN; 2.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Heparin-binding;
Protease inhibitor; Pyrrolidone carboxylic acid; Repeat; Secreted;
Serine protease inhibitor.
CHAIN 1 119 Ghilanten.
/FTId=PRO_0000155193.
DOMAIN 28 53 Antistasin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00582}.
DOMAIN 83 108 Antistasin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00582}.
REGION 97 100 Heparin-binding. {ECO:0000255}.
REGION 111 118 Heparin-binding. {ECO:0000255}.
SITE 34 35 Reactive bond. {ECO:0000250}.
SITE 89 90 Reactive bond. {ECO:0000250}.
MOD_RES 1 1 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2306252}.
DISULFID 8 19 {ECO:0000250}.
DISULFID 13 26 {ECO:0000250}.
DISULFID 28 48 {ECO:0000250}.
DISULFID 33 51 {ECO:0000250}.
DISULFID 37 53 {ECO:0000250}.
DISULFID 62 73 {ECO:0000250}.
DISULFID 67 80 {ECO:0000250}.
DISULFID 82 103 {ECO:0000250}.
DISULFID 88 106 {ECO:0000250}.
DISULFID 92 108 {ECO:0000250}.
SEQUENCE 119 AA; 13318 MW; 5A94805DBBB850EF CRC64;
QGPFGPGCEE AGCPEGSACN IITDRCTCPE VRCRVYCSHG FQRSRYGCEV CRCRTEPMKA
TCDISECPEG MMCSRLTNKC DCKIDINCRK TCPNGLKRDK LGCEYCECKP KRKLVPRLS


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