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Protein

Annexin D1

Gene

ANN1

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

Functioni

Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.2 Publications

Miscellaneous

Binds lipids at millimolar calcium concentration.

pH dependencei

Active at pH 7.0 and 9.0, but not at pH 5.5.1 Publication

GO - Molecular functioni

  • ATP binding Source: TAIR
  • calcium-dependent phospholipid binding Source: UniProtKB-KW
  • calcium ion binding Source: TAIR
  • copper ion binding Source: TAIR
  • peroxidase activity Source: TAIR
  • protein homodimerization activity Source: TAIR
  • zinc ion binding Source: TAIR

GO - Biological processi

  • calcium ion transmembrane transport Source: TAIR
  • potassium ion export Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cold Source: TAIR
  • response to heat Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to water deprivation Source: TAIR

Keywordsi

Biological processStress response
LigandCalcium, Calcium/phospholipid-binding

Enzyme and pathway databases

BioCyciARA:AT1G35720-MONOMER
ReactomeiR-ATH-114608 Platelet degranulation
R-ATH-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin D1
Alternative name(s):
AnnAt1
Annexin A1
Gene namesi
Name:ANN1
Synonyms:ANNAT1, ANX23-ATH, ATOXY5, OXY5
Ordered Locus Names:At1g35720
ORF Names:F14D7.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G35720
TAIRilocus:2011344 AT1G35720

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

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Plants are hypersensitive to osmotic stress and abscisic acid (ABA) during germination and early seedling growth.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40H → A: Loss of peroxidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002788152 – 317Annexin D1Add BLAST316

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei100PhosphothreonineBy similarity1
Modified residuei102Phosphoserine1 Publication1
Modified residuei112Phosphothreonine1 Publication1
Modified residuei129PhosphotyrosineBy similarity1
Modified residuei155Phosphoserine1 Publication1
Modified residuei156Phosphotyrosine1 Publication1
Modified residuei284Phosphotyrosine1 Publication1
Modified residuei289Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9SYT0
PRIDEiQ9SYT0

PTM databases

iPTMnetiQ9SYT0

Expressioni

Tissue specificityi

Ubiquitous. Most abundant in stems.2 Publications

Developmental stagei

Expressed in the elongation zone of the root and in the root cap in germinating seedlings. Expressed later in the internal cells of the root and in the epidermal cells and the vascular tissue of the hypocotyl. By day 7, expressed in the initiating trichomes on leaf primordia and in the vasculature of hypocotyl and cotyledon. At the transition to reproductive growth (day 14), expressed in the vasculature, epidermis, basal mesophyll cells and pith meristem of leaves.2 Publications

Inductioni

Up-regulated by cold, dehydration, salt, osmotic and oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic acid (SA).3 Publications

Gene expression databases

ExpressionAtlasiQ9SYT0 baseline and differential
GenevisibleiQ9SYT0 AT

Interactioni

Subunit structurei

Monomer and homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi25708, 24 interactors
DIPiDIP-61421N
IntActiQ9SYT0, 3 interactors
MINTiQ9SYT0
STRINGi3702.AT1G35720.1

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 24Combined sources12
Helixi32 – 38Combined sources7
Helixi43 – 57Combined sources15
Turni61 – 65Combined sources5
Helixi72 – 81Combined sources10
Helixi84 – 89Combined sources6
Helixi91 – 97Combined sources7
Helixi105 – 111Combined sources7
Helixi115 – 122Combined sources8
Turni123 – 129Combined sources7
Helixi133 – 140Combined sources8
Helixi143 – 153Combined sources11
Helixi165 – 181Combined sources17
Helixi187 – 195Combined sources9
Helixi198 – 210Combined sources13
Beta strandi211 – 214Combined sources4
Helixi216 – 219Combined sources4
Turni220 – 222Combined sources3
Helixi228 – 238Combined sources11
Turni239 – 241Combined sources3
Helixi244 – 256Combined sources13
Helixi264 – 273Combined sources10
Turni274 – 276Combined sources3
Helixi277 – 288Combined sources12
Helixi292 – 296Combined sources5
Beta strandi297 – 299Combined sources3
Helixi303 – 310Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YCNX-ray2.51A/B2-317[»]
2Q4CX-ray2.51A/B2-317[»]
ProteinModelPortaliQ9SYT0
SMRiQ9SYT0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SYT0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati15 – 80Annexin 1Add BLAST66
Repeati87 – 152Annexin 2Add BLAST66
Repeati170 – 236Annexin 3Add BLAST67
Repeati246 – 311Annexin 4Add BLAST66

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi224 – 227Poly-Asp4

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similaritiesi

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819 Eukaryota
ENOG410XPUN LUCA
HOGENOMiHOG000158802
InParanoidiQ9SYT0
KOiK17098
OMAiFAETLYY
OrthoDBiEOG09360FWC
PhylomeDBiQ9SYT0

Family and domain databases

Gene3Di1.10.220.10, 4 hits
InterProiView protein in InterPro
IPR001464 Annexin
IPR018502 Annexin_repeat
IPR018252 Annexin_repeat_CS
IPR037104 Annexin_sf
IPR009118 AnnexinD_plant
PfamiView protein in Pfam
PF00191 Annexin, 4 hits
PRINTSiPR00196 ANNEXIN
PR01814 ANNEXINPLANT
SMARTiView protein in SMART
SM00335 ANX, 4 hits
PROSITEiView protein in PROSITE
PS00223 ANNEXIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SYT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKVSDSV PAPSDDAEQL RTAFEGWGTN EDLIISILAH RSAEQRKVIR
60 70 80 90 100
QAYHETYGED LLKTLDKELS NDFERAILLW TLEPGERDAL LANEATKRWT
110 120 130 140 150
SSNQVLMEVA CTRTSTQLLH ARQAYHARYK KSLEEDVAHH TTGDFRKLLV
160 170 180 190 200
SLVTSYRYEG DEVNMTLAKQ EAKLVHEKIK DKHYNDEDVI RILSTRSKAQ
210 220 230 240 250
INATFNRYQD DHGEEILKSL EEGDDDDKFL ALLRSTIQCL TRPELYFVDV
260 270 280 290 300
LRSAINKTGT DEGALTRIVT TRAEIDLKVI GEEYQRRNSI PLEKAITKDT
310
RGDYEKMLVA LLGEDDA
Length:317
Mass (Da):36,204
Last modified:May 1, 2000 - v1
Checksum:i92516D630325005F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59E → K in AAC49472 (PubMed:8855345).Curated1
Sequence conflicti196R → I in CAA67608 (Ref. 7) Curated1
Sequence conflicti229 – 232FLAL → LPCT in AAC49472 (PubMed:8855345).Curated4
Sequence conflicti293 – 294EK → R in CAA67608 (Ref. 7) Curated2
Sequence conflicti300 – 301TR → NC in CAA67608 (Ref. 7) Curated2
Sequence conflicti305E → G in CAA67608 (Ref. 7) Curated1
Sequence conflicti311 – 312LL → IF in CAA67608 (Ref. 7) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28415 mRNA Translation: AAC49472.1
AF083913 mRNA Translation: AAD34236.1
AC021198 Genomic DNA Translation: AAF79882.1
CP002684 Genomic DNA Translation: AEE31825.1
BT003359 mRNA Translation: AAO29977.1
AF332435 mRNA Translation: AAG48798.1
AY086570 mRNA Translation: AAM63633.1
AY072347 mRNA Translation: AAL61954.1
X99224 mRNA Translation: CAA67608.1
Z18518 mRNA Translation: CAA79214.1
AK221429 mRNA Translation: BAD94442.1
PIRiC86479
RefSeqiNP_174810.1, NM_103274.4
UniGeneiAt.25241
At.50678

Genome annotation databases

EnsemblPlantsiAT1G35720.1; AT1G35720.1; AT1G35720
GeneIDi840476
GrameneiAT1G35720.1; AT1G35720.1; AT1G35720
KEGGiath:AT1G35720

Similar proteinsi

Entry informationi

Entry nameiANXD1_ARATH
AccessioniPrimary (citable) accession number: Q9SYT0
Secondary accession number(s): Q39001
, Q42023, Q56Y94, Q96527
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 132 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

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

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