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: -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

Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor, Thiol protease inhibitor

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

AraportiAT1G47710
TAIRilocus:2015443 AT1G47710

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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...) asparaginePROSITE-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

ExpressionAtlasiQ9S7T8 baseline and differential
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
OMAiVQNGFHV
OrthoDBiEOG09360C4A
PhylomeDBiQ9S7T8

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

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
AT1G47710.2; AT1G47710.2; AT1G47710
GeneIDi841182
GrameneiAT1G47710.1; AT1G47710.1; AT1G47710
AT1G47710.2; AT1G47710.2; AT1G47710
KEGGiath:AT1G47710

Similar proteinsi

Entry informationi

Entry nameiSPZX_ARATH
AccessioniPrimary (citable) accession number: Q9S7T8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health