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P41822 (FRI_AEDAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin subunit
EC=1.16.3.1
Alternative name(s):
AeFer(H)
Ferritin heavy chain-like protein
Gene names
Name:FERH
ORF Names:AAEL007385
OrganismAedes aegypti (Yellowfever mosquito) (Culex aegypti) [Reference proteome]
Taxonomic identifier7159 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Aedini › Aedes › Stegomyia

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protection against toxic levels of iron. 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. Ref.5

Catalytic activity

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

Subunit structure

Oligomer of 24 subunits. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble ferric iron core is deposited By similarity.

Subcellular location

Secreted.

Tissue specificity

Larvae, pupae, and adult females. Detected in midgut. Ref.5

Induction

By blood meal, iron and hydrogen peroxide. Ref.5

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 209182Ferritin subunit
PRO_0000008853

Regions

Domain40 – 193154Ferritin-like diiron

Sites

Metal binding571Iron 1 By similarity
Metal binding921Iron 1 By similarity
Metal binding921Iron 2 By similarity
Metal binding951Iron 1 By similarity
Metal binding1401Iron 2 By similarity
Metal binding1751Iron 2 By similarity

Experimental info

Sequence conflict311Missing in EAT40925. Ref.4
Sequence conflict311Missing in EAT40926. Ref.4
Sequence conflict881S → A in AAA99996. Ref.1
Sequence conflict881S → A in AAK15639. Ref.2
Sequence conflict881S → A in AAL85607. Ref.3
Sequence conflict1451K → R in AAA99996. Ref.1
Sequence conflict1451K → R in AAK15639. Ref.2
Sequence conflict1451K → R in AAL85607. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P41822 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 202953E800B17B9C

FASTA20923,747
        10         20         30         40         50         60 
MMKSVFFGVV AITVAILSIY QETAQAQEQT VGATDNYQWD SVDDQCLAAL HRQINKEFDA 

        70         80         90        100        110        120 
SIIYLKYAAY FAQEKINLPG FEKFFFHSAA EEREHGIKLI EYALMRGKAP VDKHFKLNYD 

       130        140        150        160        170        180 
HEVPTVTTGE SALETALQKE VEVTKSIRGV IKACEDGSND FHLADYLTGE YLDEQHKGQR 

       190        200 
ELAEKIATLK KMKKSAPKLG EFLFDKNHM

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit."
Dunkov B.C., Zhang D., Choumarov K., Winzerling J.J., Law J.H.
Arch. Insect Biochem. Physiol. 29:293-307(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-68.
Strain: Rockefeller.
[2]"Aedes aegypti ferritin heavy chain-like protein."
Morlais I., Severson D.W.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Red eye.
Tissue: Midgut.
[3]"Single nucleotide polymorphism and codon usage bias in Aedes aegypti."
Morlais I., Severson D.W.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Red eye.
Tissue: Midgut.
[4]"Genome sequence of Aedes aegypti, a major arbovirus vector."
Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P. expand/collapse author list , Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.
Science 316:1718-1723(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LVPib12.
[5]"Aedes aegypti ferritin."
Geiser D.L., Chavez C.A., Flores-Munguia R., Winzerling J.J., Pham D.Q.-D.
Eur. J. Biochem. 270:3667-3674(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L37082 mRNA. Translation: AAA99996.1.
AF326342 mRNA. Translation: AAK15639.1.
AY064106 mRNA. Translation: AAL85607.1.
CH477437 Genomic DNA. Translation: EAT40925.1.
CH477437 Genomic DNA. Translation: EAT40926.1.
RefSeqXP_001652731.1. XM_001652681.1.
XP_001652732.1. XM_001652682.1.
UniGeneAae.4382.

3D structure databases

ProteinModelPortalP41822.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5569124.
KEGGaag:AaeL_AAEL007385.
VectorBaseAAEL007385. Aedes aegypti.

Phylogenomic databases

eggNOGNOG278794.
HOGENOMHOG000223383.
InParanoidP41822.
KOK00522.
OrthoDBEOG4N02XD.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
PROSITEPS00540. FERRITIN_1. False negative.
PS00204. FERRITIN_2. False negative.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRI_AEDAE
AccessionPrimary (citable) accession number: P41822
Secondary accession number(s): Q172H1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 1, 2008
Last modified: May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents