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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2Q4C

Ensemble refinement of the protein crystal structure of annexin from Arabidopsis thaliana gene At1g35720

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0001786molecular_functionphosphatidylserine binding
A0004601molecular_functionperoxidase activity
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0005524molecular_functionATP binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006970biological_processresponse to osmotic stress
A0008270molecular_functionzinc ion binding
A0009408biological_processresponse to heat
A0009409biological_processresponse to cold
A0009414biological_processresponse to water deprivation
A0009505cellular_componentplant-type cell wall
A0009506cellular_componentplasmodesma
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0009579cellular_componentthylakoid
A0009651biological_processresponse to salt stress
A0009737biological_processresponse to abscisic acid
A0016020cellular_componentmembrane
A0035619cellular_componentroot hair tip
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0048046cellular_componentapoplast
A0070588biological_processcalcium ion transmembrane transport
A0080022biological_processprimary root development
A0097623biological_processpotassium ion export across plasma membrane
A0098869biological_processcellular oxidant detoxification
A0110128biological_processphloem sucrose unloading
B0000325cellular_componentplant-type vacuole
B0001786molecular_functionphosphatidylserine binding
B0004601molecular_functionperoxidase activity
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005524molecular_functionATP binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006970biological_processresponse to osmotic stress
B0008270molecular_functionzinc ion binding
B0009408biological_processresponse to heat
B0009409biological_processresponse to cold
B0009414biological_processresponse to water deprivation
B0009505cellular_componentplant-type cell wall
B0009506cellular_componentplasmodesma
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0009579cellular_componentthylakoid
B0009651biological_processresponse to salt stress
B0009737biological_processresponse to abscisic acid
B0016020cellular_componentmembrane
B0035619cellular_componentroot hair tip
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0048046cellular_componentapoplast
B0070588biological_processcalcium ion transmembrane transport
B0080022biological_processprimary root development
B0097623biological_processpotassium ion export across plasma membrane
B0098869biological_processcellular oxidant detoxification
B0110128biological_processphloem sucrose unloading
Functional Information from PROSITE/UniProt
site_idPS00223
Number of Residues53
DetailsANNEXIN_1 Annexin repeat signature. GTdegaltriVttRaeiDlkVigeeYqrrnsipLekaItkdtrGdyekmLvaL
ChainResidueDetails
AGLY259-LEU311
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues142
DetailsRepeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues144
DetailsRepeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues142
DetailsRepeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P93157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9XEE2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"26452715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"26452715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9XEE2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"26452715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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