SPZX_ARATH
ID SPZX_ARATH Reviewed; 391 AA.
AC Q9S7T8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Serpin-ZX;
DE AltName: Full=ArathZx;
DE AltName: Full=AtSerpin1;
DE AltName: Full=Serpin-1;
GN OrderedLocusNames=At1g47710; ORFNames=F16N3.3, T2E6.22;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 TISSUE SPECIFICITY.
RX PubMed=15815986; DOI=10.1002/pmic.200401062;
RA Giavalisco P., Nordhoff E., Kreitler T., Kloeppel K.-D., Lehrach H.,
RA Klose J., Gobom J.;
RT "Proteome analysis of Arabidopsis thaliana by two-dimensional gel
RT electrophoresis and matrix-assisted laser desorption/ionisation-time of
RT flight mass spectrometry.";
RL Proteomics 5:1902-1913(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-351 AND 348-ILE--LEU-350.
RX PubMed=17028019; DOI=10.1016/j.jmb.2006.09.010;
RA Vercammen D., Belenghi B., van de Cotte B., Beunens T., Gavigan J.-A.,
RA De Rycke R., Brackenier A., Inze D., Harris J.L., van Breusegem F.;
RT "Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase
RT 9.";
RL J. Mol. Biol. 364:625-636(2006).
RN [6]
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RD21A.
RX PubMed=23398119; DOI=10.1111/tpj.12141;
RA Lampl N., Alkan N., Davydov O., Fluhr R.;
RT "Set-point control of RD21 protease activity by AtSerpin1 controls cell
RT death in Arabidopsis.";
RL Plant J. 74:498-510(2013).
RN [8]
RP FUNCTION.
RX PubMed=26884487; DOI=10.1104/pp.15.02026;
RA Koh E., Carmieli R., Mor A., Fluhr R.;
RT "Singlet oxygen induced membrane disruption and serpin-protease balance in
RT vacuolar driven cell death in Arabidopsis thaliana.";
RL Plant Physiol. 171:1616-1625(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND INTERACTION WITH RD21A.
RX PubMed=20181955; DOI=10.1074/jbc.m109.095075;
RA Lampl N., Budai-Hadrian O., Davydov O., Joss T.V., Harrop S.J., Curmi P.M.,
RA Roberts T.H., Fluhr R.;
RT "Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its
RT target protease RESPONSIVE TO DESICCATION-21 (RD21).";
RL J. Biol. Chem. 285:13550-13560(2010).
CC -!- FUNCTION: Inhibits metacaspase-9 (MC9) cysteine protease. Functions
CC through cleavage of its reactive center loop and covalent binding to
CC MC9. Involved in the control of elicitor-stimulated programmed cell
CC death (PCD). During infection by the necrotrophic fungal pathogen
CC Botrytis cinerea, functions to protect cells by limiting the PCD-
CC promoting protease RD21A activity that is released from the ER body or
CC vacuole to the cytoplasm (PubMed:23398119). Involved in the control of
CC water stress-induced cell death by limiting the pro-death protease
CC RD21A activity that is released from the vacuole to the cytoplasm
CC (PubMed:26884487). {ECO:0000269|PubMed:17028019,
CC ECO:0000269|PubMed:23398119, ECO:0000269|PubMed:26884487}.
CC -!- SUBUNIT: Interacts with RD21A. {ECO:0000269|PubMed:20181955,
CC ECO:0000269|PubMed:23398119}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:17028019}. Cytoplasm {ECO:0000269|PubMed:23398119}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips. Expressed in siliques (at
CC protein level). {ECO:0000269|PubMed:15815986,
CC ECO:0000269|PubMed:17028019}.
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; AC007519; AAD46018.1; -; Genomic_DNA.
DR EMBL; AC012463; AAF99797.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32203.1; -; Genomic_DNA.
DR EMBL; BT002483; AAO00843.1; -; mRNA.
DR EMBL; BT008481; AAP37840.1; -; mRNA.
DR PIR; H96517; H96517.
DR RefSeq; NP_175202.1; NM_103664.4.
DR PDB; 3LE2; X-ray; 2.20 A; A=1-391.
DR PDBsum; 3LE2; -.
DR AlphaFoldDB; Q9S7T8; -.
DR SMR; Q9S7T8; -.
DR BioGRID; 26407; 1.
DR STRING; 3702.AT1G47710.1; -.
DR MEROPS; I04.087; -.
DR iPTMnet; Q9S7T8; -.
DR PaxDb; Q9S7T8; -.
DR PRIDE; Q9S7T8; -.
DR ProteomicsDB; 226761; -.
DR EnsemblPlants; AT1G47710.1; AT1G47710.1; AT1G47710.
DR GeneID; 841182; -.
DR Gramene; AT1G47710.1; AT1G47710.1; AT1G47710.
DR KEGG; ath:AT1G47710; -.
DR Araport; AT1G47710; -.
DR TAIR; locus:2015443; AT1G47710.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_4_0_1; -.
DR InParanoid; Q9S7T8; -.
DR PhylomeDB; Q9S7T8; -.
DR EvolutionaryTrace; Q9S7T8; -.
DR PRO; PR:Q9S7T8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7T8; baseline and differential.
DR Genevisible; Q9S7T8; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:TAIR.
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 3D-structure; Apoplast; Cytoplasm; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor;
KW Thiol protease inhibitor.
FT CHAIN 1..391
FT /note="Serpin-ZX"
FT /id="PRO_0000334552"
FT REGION 337..361
FT /note="RCL"
FT SITE 351..352
FT /note="Reactive bond"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 348..350
FT /note="IKL->VRP: Slightly less efficient in metacaspase-9
FT inhibition."
FT /evidence="ECO:0000269|PubMed:17028019"
FT MUTAGEN 351
FT /note="R->A: Much less efficient in metacaspase-9
FT inhibition."
FT /evidence="ECO:0000269|PubMed:17028019"
FT MUTAGEN 351
FT /note="R->K: Slightly more efficient in metacaspase-9
FT inhibition."
FT /evidence="ECO:0000269|PubMed:17028019"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 268..278
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:3LE2"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:3LE2"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3LE2"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:3LE2"
SQ SEQUENCE 391 AA; 42639 MW; 4AECE2C77C9EF74C CRC64;
MDVRESISLQ NQVSMNLAKH VITTVSQNSN VIFSPASINV VLSIIAAGSA GATKDQILSF
LKFSSTDQLN SFSSEIVSAV LADGSANGGP KLSVANGAWI DKSLSFKPSF KQLLEDSYKA
ASNQADFQSK AVEVIAEVNS WAEKETNGLI TEVLPEGSAD SMTKLIFANA LYFKGTWNEK
FDESLTQEGE FHLLDGNKVT APFMTSKKKQ YVSAYDGFKV LGLPYLQGQD KRQFSMYFYL
PDANNGLSDL LDKIVSTPGF LDNHIPRRQV KVREFKIPKF KFSFGFDASN VLKGLGLTSP
FSGEEGLTEM VESPEMGKNL CVSNIFHKAC IEVNEEGTEA AAASAGVIKL RGLLMEEDEI
DFVADHPFLL VVTENITGVV LFIGQVVDPL H
