ASP2_ANISI
ID ASP2_ANISI Reviewed; 77 AA.
AC O77417;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Serine protease inhibitor 2;
DE AltName: Full=ASPI-2;
DE Flags: Precursor;
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9635450; DOI=10.1006/expr.1998.4284;
RA Lu C.C., Nguyen T., Morris S., Hill D., Sakanari J.A.;
RT "Anisakis simplex: mutational bursts in the reactive site centers of serine
RT protease inhibitors from an ascarid nematode.";
RL Exp. Parasitol. 89:257-261(1998).
CC -!- FUNCTION: Defends the organism against the host's proteinases.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; U94497; AAC61298.1; -; mRNA.
DR AlphaFoldDB; O77417; -.
DR SMR; O77417; -.
DR MEROPS; I08.005; -.
DR Proteomes; UP000036680; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR SUPFAM; SSF57567; SSF57567; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..77
FT /note="Serine protease inhibitor 2"
FT /id="PRO_0000034307"
FT DOMAIN 21..74
FT /note="TIL"
FT SITE 46..47
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT DISULFID 21..53
FT /evidence="ECO:0000250"
FT DISULFID 30..48
FT /evidence="ECO:0000250"
FT DISULFID 33..44
FT /evidence="ECO:0000250"
FT DISULFID 37..74
FT /evidence="ECO:0000250"
FT DISULFID 55..68
FT /evidence="ECO:0000250"
SQ SEQUENCE 77 AA; 8699 MW; 965F588F01F0511F CRC64;
MMFTPLIVLT LLVLATAEHQ CGPNEQWSDC PKCELQCGES DKPCATICGE PKCYCSPDKY
RRIPDGRCIR KIQCPQH