ID   SPZX_HORVU              Reviewed;         398 AA.
AC   Q40066;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Serpin-ZX;
DE   AltName: Full=BSZx;
DE   AltName: Full=HorvuZx;
GN   Name=PAZX;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8439552; DOI=10.1016/0167-4781(93)90282-i;
RA   Rasmussen S.K.;
RT   "A gene coding for a new plant serpin.";
RL   Biochim. Biophys. Acta 1172:151-154(1993).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=8810262; DOI=10.1074/jbc.271.41.25083;
RA   Dahl S.W., Rasmussen S.K., Hejgaard J.;
RT   "Heterologous expression of three plant serpins with distinct inhibitory
RT   specificities.";
RL   J. Biol. Chem. 271:25083-25088(1996).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=14504298; DOI=10.1093/jxb/erg248;
RA   Roberts T.H., Marttila S., Rasmussen S.K., Hejgaard J.;
RT   "Differential gene expression for suicide-substrate serine proteinase
RT   inhibitors (serpins) in vegetative and grain tissues of barley.";
RL   J. Exp. Bot. 54:2251-2263(2003).
CC   -!- FUNCTION: Inhibits chymotrypsin, cathepsin G and trypsin in vitro.
CC       {ECO:0000269|PubMed:8810262}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, coleoptiles, shoots, leaves,
CC       embryo and endosperm. {ECO:0000269|PubMed:14504298}.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; Z15116; CAA78822.1; -; Genomic_DNA.
DR   PIR; S29819; S29819.
DR   AlphaFoldDB; Q40066; -.
DR   SMR; Q40066; -.
DR   MEROPS; I04.032; -.
DR   PRIDE; Q40066; -.
DR   ExpressionAtlas; Q40066; baseline and differential.
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; IPR023795; Serpin_CS.
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.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..398
FT                   /note="Serpin-ZX"
FT                   /id="PRO_0000334567"
FT   REGION          342..366
FT                   /note="RCL"
FT   SITE            356..357
FT                   /note="Reactive bond"
SQ   SEQUENCE   398 AA;  42947 MW;  34D04C5EFF790C95 CRC64;
     MATTDIRLSI AHQTRFAVRL ASAISSPSHA KGSSGNAAFS PLSLHVALSL VAAGAAATRD
     QLAATLGAAE KGDAEGLHAL AEQVVQVVLA DASGAGGPRS FANVFVDSSL KLKPSFKDLV
     VGKYKGETQS VDFQTKAPEV AGQVNSWVEK ITTGLIKEIL PAGSVDSTTR LVLGNALYFK
     GSWTEKFDAS KTKDEKFHLL DGSSVQTPFM SSTKKQYISS YDSLKVLKLP YQQGGDKRQF
     SMYILLPEAQ DGLWNLANKL STEPEFMEKH MPMQKVPVGQ FKLPKFKISF GFEASDMLKG
     LGLQLPFSSE ADLSEMVDSP AARSLYVSSV FHKSFVEVNE EGTEAAARTA RVVTLRSLPV
     EPVKVDFVAD HPFLFLIRED LTGVVLFVGH VFNPLVSA