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Protein

Annexin D1

Gene

ANN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

Calcium, 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

TAIRiAT1G35720.

Subcellular locationi

  • Cytoplasmcytosol
  • Membrane

  • Note: translocate from cytosol to membrane upon salt treatment; this translocation is calcium dependent.

GO - Cellular componenti

  • apoplast Source: TAIR
  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • thylakoid Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

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

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Acetylation

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

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. 2 interactors.
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

Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158802.
InParanoidiQ9SYT0.
OMAiAQTYGED.
OrthoDBiEOG09360FWC.
PhylomeDBiQ9SYT0.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR009118. Annexin_pln.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01814. ANNEXINPLANT.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi25708. 24 interactors.
DIPiDIP-61421N.
IntActiQ9SYT0. 2 interactors.
STRINGi3702.AT1G35720.1.

PTM databases

iPTMnetiQ9SYT0.

Proteomic databases

PaxDbiQ9SYT0.
PRIDEiQ9SYT0.

Protocols and materials databases

DNASUi840476.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT1G35720.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158802.
InParanoidiQ9SYT0.
OMAiAQTYGED.
OrthoDBiEOG09360FWC.
PhylomeDBiQ9SYT0.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9SYT0.
PROiQ9SYT0.

Gene expression databases

GenevisibleiQ9SYT0. AT.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR009118. Annexin_pln.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01814. ANNEXINPLANT.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANXD1_ARATH
AccessioniPrimary (citable) accession number: Q9SYT0
Secondary accession number(s): Q39001
, Q42023, Q56Y94, Q96527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds lipids at millimolar calcium concentration.

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.