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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)DescriptionActionsGraphical viewLength
Sitei351 – 352Reactive bond2

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)DescriptionActionsGraphical viewLength
Mutagenesisi348 – 350IKL → VRP: Slightly less efficient in metacaspase-9 inhibition. 1 Publication3
Mutagenesisi351R → A: Much less efficient in metacaspase-9 inhibition. 1 Publication1
Mutagenesisi351R → K: Slightly more efficient in metacaspase-9 inhibition. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003345521 – 391Serpin-ZXAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi375N-linked (GlcNAc...)PROSITE-ProRule annotation1

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 interactor.
STRINGi3702.AT1G47710.1.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 23Combined sources21
Beta strandi31 – 33Combined sources3
Helixi35 – 47Combined sources13
Helixi52 – 61Combined sources10
Helixi66 – 75Combined sources10
Helixi77 – 81Combined sources5
Helixi85 – 87Combined sources3
Beta strandi91 – 101Combined sources11
Helixi108 – 117Combined sources10
Beta strandi121 – 125Combined sources5
Helixi127 – 145Combined sources19
Turni146 – 148Combined sources3
Beta strandi165 – 174Combined sources10
Beta strandi177 – 179Combined sources3
Helixi183 – 185Combined sources3
Beta strandi187 – 192Combined sources6
Beta strandi198 – 205Combined sources8
Beta strandi210 – 215Combined sources6
Beta strandi218 – 225Combined sources8
Beta strandi234 – 243Combined sources10
Helixi247 – 256Combined sources10
Turni258 – 260Combined sources3
Helixi261 – 263Combined sources3
Beta strandi268 – 278Combined sources11
Beta strandi280 – 287Combined sources8
Helixi289 – 294Combined sources6
Helixi299 – 301Combined sources3
Turni303 – 305Combined sources3
Turni308 – 310Combined sources3
Helixi314 – 317Combined sources4
Beta strandi324 – 333Combined sources10
Helixi347 – 351Combined sources5
Turni352 – 354Combined sources3
Beta strandi359 – 363Combined sources5
Beta strandi368 – 374Combined sources7
Turni375 – 377Combined sources3
Beta strandi380 – 387Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9S7T8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni337 – 361RCLAdd BLAST25

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.
OrthoDBiEOG09360C4A.
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_103664.4.
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_103664.4.
UniGeneiAt.24855.

3D structure databases

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

Protein-protein interaction databases

BioGridi26407. 1 interactor.
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.
OrthoDBiEOG09360C4A.
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...

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: November 30, 2016
This is version 109 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.