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Q9SRL5

- FRI2_ARATH

UniProt

Q9SRL5 - FRI2_ARATH

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Protein

Ferritin-2, chloroplastic

Gene

FER2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron 1PROSITE-ProRule annotation
Metal bindingi135 – 1351Iron 1PROSITE-ProRule annotation
Metal bindingi135 – 1351Iron 2PROSITE-ProRule annotation
Metal bindingi138 – 1381Iron 1PROSITE-ProRule annotation
Metal bindingi184 – 1841Iron 2PROSITE-ProRule annotation
Metal bindingi218 – 2181Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. iron ion transport Source: InterPro
  3. response to abscisic acid Source: TAIR
  4. response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G11050-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin-2, chloroplastic (EC:1.16.3.1)
Gene namesi
Name:FER2
Ordered Locus Names:At3g11050
ORF Names:F11B9.26, F9F8.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G11050.

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545ChloroplastSequence AnalysisAdd
BLAST
Chaini46 – 253208Ferritin-2, chloroplasticPRO_0000008855Add
BLAST

Proteomic databases

PaxDbiQ9SRL5.
PRIDEiQ9SRL5.

Expressioni

Inductioni

By abscisic acid (ABA).1 Publication

Gene expression databases

ExpressionAtlasiQ9SRL5. baseline and differential.
GenevestigatoriQ9SRL5.

Interactioni

Subunit structurei

Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited (By similarity).By similarity

Protein-protein interaction databases

BioGridi5610. 1 interaction.
STRINGi3702.AT3G11050.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SRL5.
SMRiQ9SRL5. Positions 56-251.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 236154Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 8237Extension peptide (EP)Add
BLAST

Sequence similaritiesi

Belongs to the ferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1528.
HOGENOMiHOG000223383.
InParanoidiQ9SRL5.
KOiK00522.
OMAiSASHAYM.
PhylomeDBiQ9SRL5.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9SRL5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLHKASPALS LLSSGYTGGG NLFPPSRNSS NLLFSPSGSR FSVQAAKGTN
60 70 80 90 100
TKSLTGVVFE PFEEVKKEME LVPTTPFVSL ARHKFSDDSE SAINDQINVE
110 120 130 140 150
YNVSYVYHAL YAYFDRDNVG LKGFAKFFND SSLEERGHAE MFMEYQNKRG
160 170 180 190 200
GRVKLQSILM PVSEFDHEEK GDALHAMELA LSLEKLTNEK LLKLQSVGVK
210 220 230 240 250
NNDVQLVDFV ESEFLGEQVE AIKKISEYVA QLRRIGKGHG VWHFDQMLLN

DEV
Length:253
Mass (Da):28,378
Last modified:May 1, 2000 - v1
Checksum:i92A59DCA3B8EBE3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31H → L in AAM65872. 1 PublicationCurated
Sequence conflicti16 – 161Y → S in AAM65872. 1 PublicationCurated
Sequence conflicti32 – 321L → R in AAM65872. 1 PublicationCurated
Sequence conflicti40 – 401R → K in AAM65872. 1 PublicationCurated
Sequence conflicti69 – 702ME → LD in AAM65872. 1 PublicationCurated
Sequence conflicti89 – 891S → A in AAM65872. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ312192 mRNA. Translation: CAC85498.1.
AC009991 Genomic DNA. Translation: AAF01516.1.
AC073395 Genomic DNA. Translation: AAG50984.1.
CP002686 Genomic DNA. Translation: AEE74997.1.
AK175807 mRNA. Translation: BAD43570.1.
AK175899 mRNA. Translation: BAD43662.1.
AK175901 mRNA. Translation: BAD43664.1.
AK175910 mRNA. Translation: BAD43673.1.
AY088333 mRNA. Translation: AAM65872.1.
Z34949 mRNA. Translation: CAA84408.1.
RefSeqiNP_187716.1. NM_111942.3.
UniGeneiAt.17409.

Genome annotation databases

EnsemblPlantsiAT3G11050.1; AT3G11050.1; AT3G11050.
GeneIDi820276.
KEGGiath:AT3G11050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ312192 mRNA. Translation: CAC85498.1 .
AC009991 Genomic DNA. Translation: AAF01516.1 .
AC073395 Genomic DNA. Translation: AAG50984.1 .
CP002686 Genomic DNA. Translation: AEE74997.1 .
AK175807 mRNA. Translation: BAD43570.1 .
AK175899 mRNA. Translation: BAD43662.1 .
AK175901 mRNA. Translation: BAD43664.1 .
AK175910 mRNA. Translation: BAD43673.1 .
AY088333 mRNA. Translation: AAM65872.1 .
Z34949 mRNA. Translation: CAA84408.1 .
RefSeqi NP_187716.1. NM_111942.3.
UniGenei At.17409.

3D structure databases

ProteinModelPortali Q9SRL5.
SMRi Q9SRL5. Positions 56-251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 5610. 1 interaction.
STRINGi 3702.AT3G11050.1-P.

Proteomic databases

PaxDbi Q9SRL5.
PRIDEi Q9SRL5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G11050.1 ; AT3G11050.1 ; AT3G11050 .
GeneIDi 820276.
KEGGi ath:AT3G11050.

Organism-specific databases

TAIRi AT3G11050.

Phylogenomic databases

eggNOGi COG1528.
HOGENOMi HOG000223383.
InParanoidi Q9SRL5.
KOi K00522.
OMAi SASHAYM.
PhylomeDBi Q9SRL5.

Enzyme and pathway databases

BioCyci ARA:AT3G11050-MONOMER.

Gene expression databases

ExpressionAtlasi Q9SRL5. baseline and differential.
Genevestigatori Q9SRL5.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
PANTHERi PTHR11431. PTHR11431. 1 hit.
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family."
    Petit J.-M., Briat J.-F., Lobreaux S.
    Biochem. J. 359:575-582(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-212.
    Strain: cv. Columbia.
    Tissue: Leaf.

Entry informationi

Entry nameiFRI2_ARATH
AccessioniPrimary (citable) accession number: Q9SRL5
Secondary accession number(s): Q42288, Q8L9N6, Q8WHW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3