ID   SPZ2B_WHEAT             Reviewed;         398 AA.
AC   P93692;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Serpin-Z2B;
DE   AltName: Full=TriaeZ2b;
DE   AltName: Full=WSZ2b;
DE   AltName: Full=WZS3;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC   STRAIN=cv. Chinese Spring; TISSUE=Grain;
RX   PubMed=10874043; DOI=10.1074/jbc.m004633200;
RA   Oestergaard H., Rasmussen S.K., Roberts T.H., Hejgaard J.;
RT   "Inhibitory serpins from wheat grain with reactive centers resembling
RT   glutamine-rich repeats of prolamin storage proteins. Cloning and
RT   characterization of five major molecular forms.";
RL   J. Biol. Chem. 275:33272-33279(2000).
CC   -!- FUNCTION: Inhibits chymotrypsin, cathepsin G and trypsin in vitro.
CC       {ECO:0000269|PubMed:10874043}.
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; Y11486; CAA72274.1; -; mRNA.
DR   PIR; T06597; T06597.
DR   AlphaFoldDB; P93692; -.
DR   SMR; P93692; -.
DR   STRING; 4565.Traes_5DL_8115D3D0D.1; -.
DR   Allergome; 5724; Tri a 33.
DR   MEROPS; I04.032; -.
DR   PRIDE; P93692; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P93692; baseline.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..398
FT                   /note="Serpin-Z2B"
FT                   /id="PRO_0000334572"
FT   REGION          343..367
FT                   /note="RCL"
FT   SITE            357..358
FT                   /note="Reactive bond"
SQ   SEQUENCE   398 AA;  42981 MW;  94688D2F821BA741 CRC64;
     MATTLATDVR LSIAHQTRFA FRLASAISSN PESTVNNAAF SPVSLHVALS LITAGAGGAT
     RNQLAATLGE GEVEGLHALA EQVVQFVLAD ASNIGGPRVA FANGVFVDAS LQLKPSFQEL
     AVCKYKAEAQ SVDFQTKAAE VTAQVNSWVE KVTTGLIKDI LPAGSIDNTT RLVLGNALYF
     KGAWTDQFDP RATQSDDFYL LDGSSIQTPF MYSSEEQYIS SSDGLKVLKL PYKQGGDKRQ
     FSMYILLPEA LSGLWSLAEK LSAEPEFLEQ HIPRQKVALR QFKLPKFKIS LGIEASDLLK
     GLGLLLPFGA EADLSEMVDS PMAQNLYISS IFHKAFVEVN ETGTEAAATT IAKVVLRQAP
     PPSVLDFIVD HPFLFLIRED TSGVVLFIGH VVNPLLSS