ID   SPZ3_ARATH              Reviewed;         389 AA.
AC   O48706;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Serpin-Z3;
DE   AltName: Full=ArathZ3;
GN   OrderedLocusNames=At2g26390; ORFNames=T9J22.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18060440; DOI=10.1007/s10142-007-0059-2;
RA   Roberts T.H., Hejgaard J.;
RT   "Serpins in plants and green algae.";
RL   Funct. Integr. Genomics 8:1-27(2008).
CC   -!- FUNCTION: Probable serine protease inhibitor. {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC002505; AAC14489.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07832.1; -; Genomic_DNA.
DR   PIR; T00972; T00972.
DR   RefSeq; NP_180207.1; NM_128196.2.
DR   AlphaFoldDB; O48706; -.
DR   SMR; O48706; -.
DR   STRING; 3702.AT2G26390.1; -.
DR   PaxDb; O48706; -.
DR   PRIDE; O48706; -.
DR   ProteomicsDB; 226707; -.
DR   EnsemblPlants; AT2G26390.1; AT2G26390.1; AT2G26390.
DR   GeneID; 817179; -.
DR   Gramene; AT2G26390.1; AT2G26390.1; AT2G26390.
DR   KEGG; ath:AT2G26390; -.
DR   Araport; AT2G26390; -.
DR   TAIR; locus:2066316; AT2G26390.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_4_0_1; -.
DR   InParanoid; O48706; -.
DR   OMA; ATHDFTT; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; O48706; -.
DR   PRO; PR:O48706; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48706; baseline and differential.
DR   Genevisible; O48706; AT.
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   3: Inferred from homology;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..389
FT                   /note="Serpin-Z3"
FT                   /id="PRO_0000334548"
FT   REGION          337..361
FT                   /note="RCL"
FT   SITE            351..352
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   389 AA;  43221 MW;  F4CA48D726E700C7 CRC64;
     MELGKSIENQ NNVVARLAKK VIETDVANGS NVVFSPMSIN VLLSLIAAGS NPVTKEEILS
     FLMSPSTDHL NAVLAKIADG GTERSDLCLS TAHGVWIDKS SYLKPSFKEL LENSYKASCS
     QVDFATKPVE VIDEVNIWAD VHTNGLIKQI LSRDCTDTIK EIRNSTLILA NAVYFKAAWS
     RKFDAKLTKD NDFHLLDGNT VKVPFMMSYK DQYLRGYDGF QVLRLPYVED KRHFSMYIYL
     PNDKDGLAAL LEKISTEPGF LDSHIPLHRT PVDALRIPKL NFSFEFKASE VLKDMGLTSP
     FTSKGNLTEM VDSPSNGDKL HVSSIIHKAC IEVDEEGTEA AAVSVAIMMP QCLMRNPDFV
     ADHPFLFTVR EDNSGVILFI GQVLDPSKH