ID   BSZ7_HORVU              Reviewed;         397 AA.
AC   Q43492;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Serpin-Z7;
DE   AltName: Full=BSZ7;
DE   AltName: Full=HorvuZ7;
GN   Name=PAZ7;
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 [MRNA], PROTEIN SEQUENCE OF 2-18; 23-46; 62-96;
RP   102-129; 107-131; 154-174; 175-184; 196-215; 206-236; 233-242; 243-259;
RP   246-268; 264-277; 286-293; 293-322; 320-335; 320-341; 326-341; 359-377 AND
RP   378-396, FUNCTION, AND ACETYLATION AT ALA-2.
RC   STRAIN=cv. Bomi; TISSUE=Endosperm;
RX   PubMed=8917613; DOI=10.1016/s0167-4838(96)00115-x;
RA   Rasmussen S.K., Klausen J., Hejgaard J., Svensson B., Svendsen I.;
RT   "Primary structure of the plant serpin BSZ7 having the capacity of
RT   chymotrypsin inhibition.";
RL   Biochim. Biophys. Acta 1297:127-130(1996).
RN   [2]
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 in vitro. {ECO:0000269|PubMed:8917613}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in endosperm, at intermediate
CC       level in embryo and at lower levels in roots.
CC       {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; X95277; CAA64599.1; -; mRNA.
DR   PIR; T06183; T06183.
DR   AlphaFoldDB; Q43492; -.
DR   SMR; Q43492; -.
DR   MEROPS; I04.032; -.
DR   iPTMnet; Q43492; -.
DR   PRIDE; Q43492; -.
DR   ExpressionAtlas; Q43492; baseline.
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   Acetylation; Direct protein sequencing; Protease inhibitor;
KW   Serine protease inhibitor.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8917613"
FT   CHAIN           2..397
FT                   /note="Serpin-Z7"
FT                   /id="PRO_5000146725"
FT   REGION          344..368
FT                   /note="RCL"
FT   SITE            358..359
FT                   /note="Reactive bond"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:8917613"
FT   CONFLICT        173
FT                   /note="T -> A (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="I -> T (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="K -> E (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="M -> L (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  42821 MW;  65956C5F7E6A86AB CRC64;
     MATTLTTDLR LSIAHQTRFG LRLASAISSD PESAATNVAF SPVSLHVALS LVAAGARGAT
     RDQLVAVLGG GGAGEAEALQ SLAEQVVQFV LADASINSGP RIAFANGVFV DASLSLKPSF
     QELAVCNYKS EVQSVDFKTK APEAASQVNS WVKNVTAGLI EEILPAGSID NTTRLVLGNA
     LYFKGLWTKK FDESKTKYDD FHLLNGSTVQ TPFMSSTNKQ YLSSSDGLKV LKLPYQHGGD
     NRQFSMYILL PEAHDGLSRL AQKLSTEPDF LENRIPTEEV EVGQFMLPKF KISFGFEANK
     LLKTLGLQLP FSLEANLSEM VNSPMGLYIS SVFHKTFVEV DEEGTKAGAA TGDVIVDRSL
     PIRMDFVANH PFLFLIREDI AGVVLFIGHV ANPAVSS