MSPI2_MELSA
ID MSPI2_MELSA Reviewed; 36 AA.
AC B3A0N9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Serine protease inhibitor 2;
DE AltName: Full=Protease inhibitor MSPI-2;
OS Melanoplus sanguinipes (Migratory grasshopper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Melanoplinae; Melanoplini; Melanoplus.
OX NCBI_TaxID=65742;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph {ECO:0000269|Ref.1};
RA Taub-Montemayor T.E., Jones N.T., Linse K.D., Rankin M.A.;
RT "Pacifastin-related serine protease inhibitors of the migratory
RT grasshopper, Melanoplus sanguinipes.";
RL Submitted (OCT-2011) to UniProtKB.
CC -!- FUNCTION: Probable serine protease inhibitor.
CC {ECO:0000250|UniProtKB:O46162}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed in hemolymph. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00776}.
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DR AlphaFoldDB; B3A0N9; -.
DR SMR; B3A0N9; -.
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; IPR008037; Pacifastin_dom.
DR InterPro; IPR036201; Pacifastin_dom_sf.
DR InterPro; IPR016307; Prtase-inh_pacifastin.
DR Pfam; PF05375; Pacifastin_I; 1.
DR PIRSF; PIRSF001625; Prot_inhib_pacifastin; 1.
DR SUPFAM; SSF57283; SSF57283; 1.
DR PROSITE; PS51446; PACIFASTIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW Serine protease inhibitor.
FT PEPTIDE 1..36
FT /note="Serine protease inhibitor 2"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000414707"
FT DOMAIN 1..36
FT /note="Pacifastin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT SITE 31..32
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:O46162,
FT ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 4..19
FT /evidence="ECO:0000250|UniProtKB:O46162,
FT ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 14..34
FT /evidence="ECO:0000250|UniProtKB:O46162,
FT ECO:0000255|PROSITE-ProRule:PRU00776"
FT DISULFID 17..29
FT /evidence="ECO:0000250|UniProtKB:O46162,
FT ECO:0000255|PROSITE-ProRule:PRU00776"
SQ SEQUENCE 36 AA; 3752 MW; AECAFE1329D3D3BA CRC64;
EISCEPGTTF QDKCNTCRCG KDGKSAAGCT LKACPQ