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Protein

Presenilin-like protein At2g29900

Gene

At2g29900

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei198By similarity1
Active sitei318By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processNotch signaling pathway

Enzyme and pathway databases

ReactomeiR-ATH-6798695 Neutrophil degranulation

Protein family/group databases

MEROPSiA22.A02

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin-like protein At2g29900
Gene namesi
Ordered Locus Names:At2g29900
ORF Names:F6K5.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

AraportiAT2G29900
TAIRilocus:2052080 AT2G29900

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 17CytoplasmicSequence analysisAdd BLAST17
Transmembranei18 – 38HelicalSequence analysisAdd BLAST21
Topological domaini39 – 76LumenalSequence analysisAdd BLAST38
Transmembranei77 – 97HelicalSequence analysisAdd BLAST21
Topological domaini98 – 106CytoplasmicSequence analysis9
Transmembranei107 – 127HelicalSequence analysisAdd BLAST21
Topological domaini128 – 135LumenalSequence analysis8
Transmembranei136 – 156HelicalSequence analysisAdd BLAST21
Topological domaini157 – 158CytoplasmicSequence analysis2
Transmembranei159 – 179HelicalSequence analysisAdd BLAST21
Topological domaini180 – 188LumenalSequence analysis9
Transmembranei189 – 209HelicalSequence analysisAdd BLAST21
Topological domaini210 – 305CytoplasmicSequence analysisAdd BLAST96
Transmembranei306 – 326HelicalSequence analysisAdd BLAST21
Topological domaini327 – 336LumenalSequence analysis10
Transmembranei337 – 357HelicalSequence analysisAdd BLAST21
Topological domaini358 – 366CytoplasmicSequence analysis9
Intramembranei367 – 387HelicalSequence analysisAdd BLAST21
Topological domaini388 – 397CytoplasmicSequence analysis10

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000739061 – 397Presenilin-like protein At2g29900Add BLAST397

Proteomic databases

PaxDbiQ9SIK7
PRIDEiQ9SIK7

PTM databases

iPTMnetiQ9SIK7

Expressioni

Gene expression databases

ExpressionAtlasiQ9SIK7 baseline and differential
GenevisibleiQ9SIK7 AT

Interactioni

Subunit structurei

Homodimer. Probable component of the gamma-secretase complex, a complex composed of a presenilin homodimer, nicastrin, APH1 and PEN2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi2890, 2 interactors
STRINGi3702.AT2G29900.1

Structurei

3D structure databases

ProteinModelPortaliQ9SIK7
SMRiQ9SIK7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi363 – 365PAL3

Domaini

The PAL motif is required for normal active site conformation.By similarity

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2736 Eukaryota
ENOG410XPZD LUCA
HOGENOMiHOG000240228
InParanoidiQ9SIK7
KOiK04505
OMAiIAIHWKG
OrthoDBiEOG09360DOM
PhylomeDBiQ9SIK7

Family and domain databases

InterProiView protein in InterPro
IPR001108 Peptidase_A22A
IPR006639 Preselin/SPP
PANTHERiPTHR10202 PTHR10202, 2 hits
PfamiView protein in Pfam
PF01080 Presenilin, 1 hit
PRINTSiPR01072 PRESENILIN
SMARTiView protein in SMART
SM00730 PSN, 1 hit

Sequencei

Sequence statusi: Complete.

Q9SIK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRNQRPRSI LDSLGEELIA ILTPVSICMF TVVLLVCILN SDPSSSSASF
60 70 80 90 100
SSIATAAYSE SDSDSSWDKF VGALLNSVVF VAAITVATFV LVLLFYLRCV
110 120 130 140 150
KFLKFYMGFS AFIVLGNLGG EILVLLIDRF RFPIDSITFL ILLFNFSVVG
160 170 180 190 200
VFAVFMSKFS ILITQGYLVW IGVLVAYFFT LLPEWTTWVL LVALALYDIA
210 220 230 240 250
AVLLPVGPLR LLVEMAISRD EDIPALVYEA RPVIRNDSRS VQRRVWREQR
260 270 280 290 300
SSQNNANRNE VRVVESAEVE EEHVGSSERA EISVPLIDRR PEQAENSETF
310 320 330 340 350
LEGIGLGSSG AIKLGLGDFI FYSVLVGRAA MYDLMTVYAC YLAIIAGLGI
360 370 380 390
TLMLLSVYQK ALPALPVSIM LGVVFYFLAR LLLEVFVVQC SSNLVMF
Length:397
Mass (Da):44,012
Last modified:May 1, 2000 - v1
Checksum:iDE6804D6CA186783
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007113 Genomic DNA Translation: AAD23630.1
CP002685 Genomic DNA Translation: AEC08318.1
BT028914 mRNA Translation: ABI49461.1
PIRiA84702
RefSeqiNP_180551.1, NM_128544.4
UniGeneiAt.66277

Genome annotation databases

EnsemblPlantsiAT2G29900.1; AT2G29900.1; AT2G29900
GeneIDi817540
GrameneiAT2G29900.1; AT2G29900.1; AT2G29900
KEGGiath:AT2G29900

Similar proteinsi

Entry informationi

Entry nameiPSNB_ARATH
AccessioniPrimary (citable) accession number: Q9SIK7
Secondary accession number(s): Q0IGK6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 113 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health