ID   SPZ1B_WHEAT             Reviewed;         399 AA.
AC   P93693;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serpin-Z1B;
DE   AltName: Full=TriaeZ1b;
DE   AltName: Full=WSZ1b;
DE   AltName: Full=WZS2;
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 and cathepsin G 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; Y11485; CAA72273.1; -; mRNA.
DR   PIR; T06488; T06488.
DR   AlphaFoldDB; P93693; -.
DR   SMR; P93693; -.
DR   STRING; 4565.Traes_5DL_D4B0422E9.1; -.
DR   Allergome; 5724; Tri a 33.
DR   MEROPS; I04.032; -.
DR   PRIDE; P93693; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P93693; 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..399
FT                   /note="Serpin-Z1B"
FT                   /id="PRO_0000334569"
FT   REGION          344..368
FT                   /note="RCL"
FT   SITE            358..359
FT                   /note="Reactive bond"
SQ   SEQUENCE   399 AA;  43033 MW;  4A22615566B9A590 CRC64;
     MATTLATDVR LSIAHQTRFA LRLASTISSN PKSAASNAAF SPVSLHSALS LLAAGAGSAT
     RDQLVATLGT GEVEGGHALA EQVVQFVLAD ASSAGGPRVA FANGVFVDAS LLLKPSFQEL
     AVCKYKAETQ SVDFQTKAAE VTTQVNSWVE KVTSGRIKNI LPSGSVDNTT KLVLANALYF
     KGAWTDQFDS YGTKNDYFYL LDGSSVQTPF MSSMDDDQYI SSSDGLKVLK LPYKQGGDNR
     QFSMYILLPE APGGLSSLAE KLSAEPDFLE RHIPRQRVAI RQFKLPKFKI SFGMEASDLL
     KCLGLQLPFS DEADFSEMVD SPMPQGLRVS SVFHQAFVEV NEQGTEAAAS TAIKMVPQQA
     RPPSVMDFIA DHPFLFLLRE DISGVVLFMG HVVNPLLSS