ANTA_HYDVU
ID ANTA_HYDVU Reviewed; 220 AA.
AC P38977;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Antistasin;
DE Short=ATS;
DE AltName: Full=Blood coagulation factor Xa/proclotting enzyme inhibitor;
DE Flags: Precursor;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SF1;
RX PubMed=1516699; DOI=10.1016/0014-5793(92)80791-e;
RA Holstein T.W., Mala C., Kurz E., Bauer K., Greber M., David C.N.;
RT "The primitive metazoan Hydra expresses antistasin, a serine protease
RT inhibitor of vertebrate blood coagulation: cDNA cloning, cellular
RT localisation and developmental regulation.";
RL FEBS Lett. 309:288-292(1992).
CC -!- FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of
CC factor Xa. Facilitates digestion of tissues and may also protect the
CC gastric tissues from its own digestive enzymes. May have therapeutic
CC utility as an anticoagulant. Also exhibits a strong metastatic
CC activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Gland cells. It is more strongly expressed in the
CC head than in the gastric tissue.
CC -!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.
CC {ECO:0000305}.
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DR EMBL; X67590; CAA47864.1; -; mRNA.
DR PIR; S29195; S29195.
DR AlphaFoldDB; P38977; -.
DR SMR; P38977; -.
DR MEROPS; I15.003; -.
DR Proteomes; UP000694840; Unplaced.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR011061; Hirudin/antistatin.
DR Pfam; PF02822; Antistasin; 6.
DR SUPFAM; SSF57262; SSF57262; 6.
DR PROSITE; PS51252; ANTISTASIN; 6.
PE 2: Evidence at transcript level;
KW Blood coagulation; Hemostasis; Heparin-binding; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..220
FT /note="Antistasin"
FT /id="PRO_0000001699"
FT DOMAIN 21..46
FT /note="Antistasin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 54..79
FT /note="Antistasin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 91..117
FT /note="Antistasin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 120..145
FT /note="Antistasin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 154..180
FT /note="Antistasin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 183..208
FT /note="Antistasin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT SITE 27..28
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 60..61
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 98..99
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 161..162
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 25016 MW; E7987F01900D0278 CRC64;
MNYLFVFLAL SAAVTFANAE CNKIQCRMFC KFGFQQDENG CDICKCAERP EKKCSNRYCK
MLCPEGFQVD ANGCQICRCK RSALEAPEKK CDGLKQCKMH CENGFVRDEN GCPKCECSKC
KQFQCLIFCP HGNEVDENGC KTCKCKAAPE KKKCDDLKQC RMFCENGFVR DENGCKKCEC
NKCKNFICQI FCEYGNVVDE NGCKTCKCNS KPLKLSLHCR