ID   SPZ1A_WHEAT             Reviewed;         398 AA.
AC   Q41593;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Serpin-Z1A;
DE   AltName: Full=TriaeZ1a;
DE   AltName: Full=WSZ1a;
DE            Short=WSZ1;
DE   AltName: Full=WSZCI;
GN   Name=WZCI;
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], AND FUNCTION.
RC   STRAIN=cv. Chinese Spring; TISSUE=Grain;
RX   PubMed=8605317; DOI=10.1007/bf00049343;
RA   Rasmussen S.K., Dahl S.W., Noergaard A., Hejgaard J.;
RT   "A recombinant wheat serpin with inhibitory activity.";
RL   Plant Mol. Biol. 30:673-677(1996).
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   PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
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).
RN   [4]
RP   FUNCTION.
RX   PubMed=8163022; DOI=10.1016/0014-5793(94)80610-1;
RA   Rosenkrands I., Hejgaard J., Rasmussen S.K., Bjoern S.E.;
RT   "Serpins from wheat grain.";
RL   FEBS Lett. 343:75-80(1994).
CC   -!- FUNCTION: Inhibits chymotrypsin and cathepsin G in vitro.
CC       {ECO:0000269|PubMed:10874043, ECO:0000269|PubMed:8163022,
CC       ECO:0000269|PubMed:8605317, ECO:0000269|PubMed:8810262}.
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; Z49890; CAA90071.1; -; mRNA.
DR   PIR; S65782; S65782.
DR   AlphaFoldDB; Q41593; -.
DR   SMR; Q41593; -.
DR   Allergome; 5724; Tri a 33.
DR   MEROPS; I04.032; -.
DR   PRIDE; Q41593; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q41593; 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-Z1A"
FT                   /id="PRO_0000334568"
FT   REGION          343..367
FT                   /note="RCL"
FT   SITE            357..358
FT                   /note="Reactive bond"
SQ   SEQUENCE   398 AA;  43118 MW;  0D9456B3B6C455DF CRC64;
     MATTLATDVR LSIAHQTRFA LRLASTISSN PKSAASNAAF SPVSLYSALS LLAAGAGSAT
     RDQLVATLGT GKVEGLHALA EQVVQFVLAD ASSTGGSACR FANGVFVDAS LLLKPSFQEI
     AVCKYKAETQ SVDFQTKAAE VTTQVNSWVE KVTSGRIKDI LPPGSIDNTT KLVLANALYF
     KGAWTEQFDS YGTKNDYFYL LDGSSVQTPF MSSMDDQYLL SSDGLKVLKL PYKQGGDNRQ
     FFMYILLPEA PGGLSSLAEK LSAEPDFLER HIPRQRVALR QFKLPKFKIS FGIEASDLLK
     CLGLQLPFGD EADFSEMVDS LMPQGLRVSS VFHQAFVEVN EQGTEAAAST AIKMVLQQAR
     PPSVMDFIAD HPFLFLVRED ISGVVLFMGH VVNPLLSS