SPZ2A_WHEAT
ID SPZ2A_WHEAT Reviewed; 398 AA.
AC Q9ST57;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Serpin-Z2A;
DE AltName: Full=TriaeZ2a;
DE AltName: Full=WSZ2a;
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; AJ245879; CAB52710.1; -; mRNA.
DR AlphaFoldDB; Q9ST57; -.
DR SMR; Q9ST57; -.
DR STRING; 4565.Traes_5BL_22ED571AE.1; -.
DR Allergome; 5724; Tri a 33.
DR Allergome; 9500; Tri a 33.0101.
DR MEROPS; I04.032; -.
DR PRIDE; Q9ST57; -.
DR EnsemblPlants; TraesCS5B02G419900.1; TraesCS5B02G419900.1; TraesCS5B02G419900.
DR Gramene; TraesCS5B02G419900.1; TraesCS5B02G419900.1; TraesCS5B02G419900.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_4_0_1; -.
DR OMA; KDVWRGL; -.
DR Proteomes; UP000019116; Unplaced.
DR Genevisible; Q9ST57; TA.
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-Z2A"
FT /id="PRO_0000334571"
FT REGION 343..367
FT /note="RCL"
FT SITE 357..358
FT /note="Reactive bond"
SQ SEQUENCE 398 AA; 43311 MW; AA6AE41D46AAF3B0 CRC64;
MATTLATDVR LSIAHQTRFG FRLASTISSN PESTANNVAF SPVSLHVALS LITAGAGGAT
RDQLVATLGE GEAERLHALA EQVVQFVLAD ASYADSPRVT FANGVFVDAS LPLKPSFQEL
AVCKYKAEAQ SVDFQTKAAE VTAQVNSWVE KVTTGLIKDI LPAGSISNTT RLVLGNALYF
KGAWTDQFDS RVTKSDYFYL LDGSSIQTPF MYSSEEQYIS SSDGLKVLKL PYKQGGDKRQ
FSMYILLPEA PSGIWSLAEK LSAEPELLER HIPRQKVALR QFKLPKFKIS FGIEASDLLK
HLGLQLPFSD EADLSEMVDS PMPQGLRISS VFHKTFVEVN ETGTEAAAAT IAKAVLLSAS
PPSDMDFIAD HPFLFLIRED TSGVVLFIGH VVNPLRSL