ID   SPZ1C_WHEAT             Reviewed;         398 AA.
AC   Q9ST58;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Serpin-Z1C;
DE   AltName: Full=TriaeZ1c;
DE   AltName: Full=WSZ1c;
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; AJ245878; CAB52709.1; -; mRNA.
DR   AlphaFoldDB; Q9ST58; -.
DR   SMR; Q9ST58; -.
DR   Allergome; 5724; Tri a 33.
DR   MEROPS; I04.032; -.
DR   PRIDE; Q9ST58; -.
DR   EnsemblPlants; TraesCS5A02G359700.1; TraesCS5A02G359700.1; TraesCS5A02G359700.
DR   Gramene; TraesCS5A02G359700.1; TraesCS5A02G359700.1; TraesCS5A02G359700.
DR   OMA; FEKFTAW; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q9ST58; 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-Z1C"
FT                   /id="PRO_0000334570"
FT   REGION          343..367
FT                   /note="RCL"
FT   SITE            357..358
FT                   /note="Reactive bond"
SQ   SEQUENCE   398 AA;  42882 MW;  FB7B43E5DA3A9019 CRC64;
     MATTLATDVR LSIAHQTRFA LRLASTISSN PKSAASNAVF SPVSLHVALS LLAAGAGSAT
     RDQLVATLGT GEVEGLHALA EQVVQFVLAD ASSAGGPHVA FANGVFVDAS LPLKPSFQEL
     AVCKYKADTQ SVDFQTKAAE VATQVNSWVE KVTSGRIKDI LPSGSVDNTT KLVLANALYF
     KGAWTDQFDS SGTKNDYFYL PDGSSVQTPF MSSMDDQYLS SSDGLKVLKL PYKQGGDKRQ
     FSMYILLPEA PGGLSNLAEK LSAEPDFLER HIPRQRVALR QFKLPKFKIS FETEASDLLK
     CLGLQLPFSN EADFSEMVDS PMAHGLRVSS VFHQAFVEVN EQGTEAAAST AIKMALLQAR
     PPSVMDFIAD HPFLFLLRED ISGVVLFMGH VVNPLLSS