Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serpin-ZX

Gene

At1g47710

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits metacaspase-9 (MC9) cysteine protease. Functions through cleavage of its reactive center loop and covalent binding to MC9. Involved in the control of elicitor-stimulated programmed cell death (PCD). During infection by the necrotrophic fungal pathogen Botrytis cinerea, functions to protect cells by limiting the PCD-promoting protease RD21A activity that is released from the ER body or vacuole to the cytoplasm (PubMed:23398119). Involved in the control of water stress-induced cell death by limiting the pro-death protease RD21A activity that is released from the vacuole to the cytoplasm (PubMed:26884487).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei351 – 3522Reactive bond

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor, Thiol protease inhibitor

Enzyme and pathway databases

ReactomeiR-ATH-114608. Platelet degranulation.

Protein family/group databases

MEROPSiI04.087.

Names & Taxonomyi

Protein namesi
Recommended name:
Serpin-ZX
Alternative name(s):
ArathZx
AtSerpin1
Serpin-1
Gene namesi
Ordered Locus Names:At1g47710
ORF Names:F16N3.3, T2E6.22
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G47710.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi348 – 3503IKL → VRP: Slightly less efficient in metacaspase-9 inhibition. 1 Publication
Mutagenesisi351 – 3511R → A: Much less efficient in metacaspase-9 inhibition. 1 Publication
Mutagenesisi351 – 3511R → K: Slightly more efficient in metacaspase-9 inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Serpin-ZXPRO_0000334552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi375 – 3751N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9S7T8.
PRIDEiQ9S7T8.

PTM databases

iPTMnetiQ9S7T8.

Expressioni

Tissue specificityi

Expressed in root tips. Expressed in siliques (at protein level).2 Publications

Gene expression databases

GenevisibleiQ9S7T8. AT.

Interactioni

Subunit structurei

Interacts with RD21A.2 Publications

Protein-protein interaction databases

BioGridi26407. 1 interaction.
STRINGi3702.AT1G47710.1.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2321Combined sources
Beta strandi31 – 333Combined sources
Helixi35 – 4713Combined sources
Helixi52 – 6110Combined sources
Helixi66 – 7510Combined sources
Helixi77 – 815Combined sources
Helixi85 – 873Combined sources
Beta strandi91 – 10111Combined sources
Helixi108 – 11710Combined sources
Beta strandi121 – 1255Combined sources
Helixi127 – 14519Combined sources
Turni146 – 1483Combined sources
Beta strandi165 – 17410Combined sources
Beta strandi177 – 1793Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi198 – 2058Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi218 – 2258Combined sources
Beta strandi234 – 24310Combined sources
Helixi247 – 25610Combined sources
Turni258 – 2603Combined sources
Helixi261 – 2633Combined sources
Beta strandi268 – 27811Combined sources
Beta strandi280 – 2878Combined sources
Helixi289 – 2946Combined sources
Helixi299 – 3013Combined sources
Turni303 – 3053Combined sources
Turni308 – 3103Combined sources
Helixi314 – 3174Combined sources
Beta strandi324 – 33310Combined sources
Helixi347 – 3515Combined sources
Turni352 – 3543Combined sources
Beta strandi359 – 3635Combined sources
Beta strandi368 – 3747Combined sources
Turni375 – 3773Combined sources
Beta strandi380 – 3878Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LE2X-ray2.20A1-391[»]
ProteinModelPortaliQ9S7T8.
SMRiQ9S7T8. Positions 1-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9S7T8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni337 – 36125RCLAdd
BLAST

Domaini

The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
HOGENOMiHOG000238520.
InParanoidiQ9S7T8.
KOiK13963.
OMAiACIEVNE.
PhylomeDBiQ9S7T8.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9S7T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVRESISLQ NQVSMNLAKH VITTVSQNSN VIFSPASINV VLSIIAAGSA
60 70 80 90 100
GATKDQILSF LKFSSTDQLN SFSSEIVSAV LADGSANGGP KLSVANGAWI
110 120 130 140 150
DKSLSFKPSF KQLLEDSYKA ASNQADFQSK AVEVIAEVNS WAEKETNGLI
160 170 180 190 200
TEVLPEGSAD SMTKLIFANA LYFKGTWNEK FDESLTQEGE FHLLDGNKVT
210 220 230 240 250
APFMTSKKKQ YVSAYDGFKV LGLPYLQGQD KRQFSMYFYL PDANNGLSDL
260 270 280 290 300
LDKIVSTPGF LDNHIPRRQV KVREFKIPKF KFSFGFDASN VLKGLGLTSP
310 320 330 340 350
FSGEEGLTEM VESPEMGKNL CVSNIFHKAC IEVNEEGTEA AAASAGVIKL
360 370 380 390
RGLLMEEDEI DFVADHPFLL VVTENITGVV LFIGQVVDPL H
Length:391
Mass (Da):42,639
Last modified:May 1, 2000 - v1
Checksum:i4AECE2C77C9EF74C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007519 Genomic DNA. Translation: AAD46018.1.
AC012463 Genomic DNA. Translation: AAF99797.1.
CP002684 Genomic DNA. Translation: AEE32203.1.
BT002483 mRNA. Translation: AAO00843.1.
BT008481 mRNA. Translation: AAP37840.1.
PIRiH96517.
RefSeqiNP_175202.1. NM_103664.3.
UniGeneiAt.24855.

Genome annotation databases

EnsemblPlantsiAT1G47710.1; AT1G47710.1; AT1G47710.
GeneIDi841182.
GrameneiAT1G47710.1; AT1G47710.1; AT1G47710.
KEGGiath:AT1G47710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007519 Genomic DNA. Translation: AAD46018.1.
AC012463 Genomic DNA. Translation: AAF99797.1.
CP002684 Genomic DNA. Translation: AEE32203.1.
BT002483 mRNA. Translation: AAO00843.1.
BT008481 mRNA. Translation: AAP37840.1.
PIRiH96517.
RefSeqiNP_175202.1. NM_103664.3.
UniGeneiAt.24855.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LE2X-ray2.20A1-391[»]
ProteinModelPortaliQ9S7T8.
SMRiQ9S7T8. Positions 1-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26407. 1 interaction.
STRINGi3702.AT1G47710.1.

Protein family/group databases

MEROPSiI04.087.

PTM databases

iPTMnetiQ9S7T8.

Proteomic databases

PaxDbiQ9S7T8.
PRIDEiQ9S7T8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G47710.1; AT1G47710.1; AT1G47710.
GeneIDi841182.
GrameneiAT1G47710.1; AT1G47710.1; AT1G47710.
KEGGiath:AT1G47710.

Organism-specific databases

TAIRiAT1G47710.

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
HOGENOMiHOG000238520.
InParanoidiQ9S7T8.
KOiK13963.
OMAiACIEVNE.
PhylomeDBiQ9S7T8.

Enzyme and pathway databases

ReactomeiR-ATH-114608. Platelet degranulation.

Miscellaneous databases

EvolutionaryTraceiQ9S7T8.
PROiQ9S7T8.

Gene expression databases

GenevisibleiQ9S7T8. AT.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry."
    Giavalisco P., Nordhoff E., Kreitler T., Kloeppel K.-D., Lehrach H., Klose J., Gobom J.
    Proteomics 5:1902-1913(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-351 AND 348-ILE--LEU-350.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis."
    Lampl N., Alkan N., Davydov O., Fluhr R.
    Plant J. 74:498-510(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RD21A.
  8. "Singlet oxygen induced membrane disruption and serpin-protease balance in vacuolar driven cell death in Arabidopsis thaliana."
    Koh E., Carmieli R., Mor A., Fluhr R.
    Plant Physiol. 0:0-0(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease RESPONSIVE TO DESICCATION-21 (RD21)."
    Lampl N., Budai-Hadrian O., Davydov O., Joss T.V., Harrop S.J., Curmi P.M., Roberts T.H., Fluhr R.
    J. Biol. Chem. 285:13550-13560(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), INTERACTION WITH RD21A.

Entry informationi

Entry nameiSPZX_ARATH
AccessioniPrimary (citable) accession number: Q9S7T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.