ID   SPZ2_ARATH              Reviewed;         407 AA.
AC   Q9ZQR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Serpin-Z2;
DE   AltName: Full=ArathZ2;
GN   OrderedLocusNames=At2g14540; ORFNames=T13P21.8;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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}.
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DR   EMBL; AC006067; AAD15462.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06310.1; -; Genomic_DNA.
DR   EMBL; AY072119; AAL59941.1; -; mRNA.
DR   EMBL; AY122942; AAM67475.1; -; mRNA.
DR   PIR; D84518; D84518.
DR   RefSeq; NP_179060.1; NM_127017.2.
DR   AlphaFoldDB; Q9ZQR6; -.
DR   SMR; Q9ZQR6; -.
DR   STRING; 3702.AT2G14540.1; -.
DR   PaxDb; Q9ZQR6; -.
DR   PRIDE; Q9ZQR6; -.
DR   EnsemblPlants; AT2G14540.1; AT2G14540.1; AT2G14540.
DR   GeneID; 815941; -.
DR   Gramene; AT2G14540.1; AT2G14540.1; AT2G14540.
DR   KEGG; ath:AT2G14540; -.
DR   Araport; AT2G14540; -.
DR   TAIR; locus:2055185; AT2G14540.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_4_0_1; -.
DR   InParanoid; Q9ZQR6; -.
DR   OMA; AMQFKIE; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; Q9ZQR6; -.
DR   PRO; PR:Q9ZQR6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZQR6; baseline and differential.
DR   Genevisible; Q9ZQR6; AT.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:TAIR.
DR   GO; GO:0006281; P:DNA repair; IMP:TAIR.
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; 2.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..407
FT                   /note="Serpin-Z2"
FT                   /id="PRO_0000334547"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..368
FT                   /note="RCL"
FT   SITE            358..359
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   407 AA;  45887 MW;  3E4A6CE57895A62C CRC64;
     MDSKRKNQEL STSETADPSL SKTNKKQKID MQEAMKNQNE VSLLLVGKVI SAVAKNSNCV
     FSPASINAVL TVTAANTDNK TLRSFILSFL KSSSTEETNA IFHELASVVF KDGSETGGPK
     IAAVNGVWME QSLSCNPDWE DLFLNFFKAS FAKVDFRHKA EEVRLDVNTW ASRHTNDLIK
     EILPRGSVTS LTNWIYGNAL YFKGAWEKAF DKSMTRDKPF HLLNGKSVSV PFMRSYEKQF
     IEAYDGFKVL RLPYRQGRDD TNREFSMYLY LPDKKGELDN LLERITSNPG FLDSHIPEYR
     VDVGDFRIPK FKIEFGFEAS SVFNDFELNV SLHQKALIEI DEEGTEAAAA TTVVVVTGSC
     LWEPKKKIDF VADHPFLFLI REDKTGTLLF AGQIFDPSEL SSALDRA