SPI3_LONON
ID SPI3_LONON Reviewed; 383 AA.
AC Q5MGH0; Q5MGG9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Serine protease inhibitor 3/4;
DE Short=Serpin-3/4;
DE Flags: Precursor; Fragment;
OS Lonomia obliqua (Moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Hemileucinae; Lonomia.
OX NCBI_TaxID=304329;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAV91430.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Tegument {ECO:0000312|EMBL:AAV91430.1};
RX PubMed=16023793; DOI=10.1016/j.gene.2005.05.002;
RA Veiga A.B.G., Ribeiro J.M.C., Guimaraes J.A., Francischetti I.M.B.;
RT "A catalog for the transcripts from the venomous structures of the
RT caterpillar Lonomia obliqua: identification of the proteins potentially
RT involved in the coagulation disorder and hemorrhagic syndrome.";
RL Gene 355:11-27(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 329-341.
RC TISSUE=Larval bristle {ECO:0000269|PubMed:18342903};
RX PubMed=18342903; DOI=10.1016/j.toxicon.2008.01.013;
RA Ricci-Silva M.E., Valente R.H., Leon I.R., Tambourgi D.V., Ramos O.H.P.,
RA Perales J., Chudzinski-Tavassi A.M.;
RT "Immunochemical and proteomic technologies as tools for unravelling toxins
RT involved in envenoming by accidental contact with Lonomia obliqua
RT caterpillars.";
RL Toxicon 51:1017-1028(2008).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16023793};
CC IsoId=Q5MGH0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16023793};
CC IsoId=Q5MGH0-2; Sequence=VSP_052493, VSP_052494;
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000255}.
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DR EMBL; AY829816; AAV91430.1; -; mRNA.
DR EMBL; AY829817; AAV91431.1; -; mRNA.
DR AlphaFoldDB; Q5MGH0; -.
DR SMR; Q5MGH0; -.
DR MEROPS; I04.031; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Protease inhibitor;
KW Serine protease inhibitor; Signal.
FT SIGNAL <1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..383
FT /note="Serine protease inhibitor 3/4"
FT /id="PRO_0000296379"
FT SITE 363..364
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:P80034"
FT VAR_SEQ 7..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16023793"
FT /id="VSP_052493"
FT VAR_SEQ 358..383
FT /note="EFAANFSSFTRDRNYLIVKQTVRVFP -> AFGISYLSAVITQPRSFVADHP
FT FIFMLKEGRKILFFGTMMS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16023793"
FT /id="VSP_052494"
FT CONFLICT 279
FT /note="V -> A (in Ref. 1; AAV91431)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAV91430.1"
SQ SEQUENCE 383 AA; 43194 MW; F3AD6E92424371C8 CRC64;
RPLRPGKILI CIFALAALTT ATETDLQRIL RDGNDQFTAK MLPEIVKENP NKNIVFSAFS
VMSPLAQLAI ASAGESRDEL FSAIGFPNEN VTKAVFTDLN RELKSVKGVT LKIANKIYIA
NGFELNDQFA VVSKDVFNSE VQKLDFAQNK VAAKTINTWV EDHTNNRIKD LVDPNSLDDY
TRAVLVNALY FKGSWKNKFD KESTIDRPFH VDNTKTIQVP TMHRSGQYSY GESRELNAKI
IEMPYEGDET SLVIVLPNTV DGIHNLLEKL KDPKVLSRVE KDMHEIDVDV YVPKFKIETT
TDLKKVLQNM NIKKLFNGSE ARLDYLLKKS DALYVSEAVQ KAFIEVNEEG AEAAAANEFA
ANFSSFTRDR NYLIVKQTVR VFP