FRI_AEDAE
ID FRI_AEDAE Reviewed; 209 AA.
AC P41822; Q172H1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ferritin subunit;
DE EC=1.16.3.1;
DE AltName: Full=AeFer(H);
DE AltName: Full=Ferritin heavy chain-like protein;
DE Flags: Precursor;
GN Name=FERH; ORFNames=AAEL007385;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-68.
RC STRAIN=Rockefeller;
RX PubMed=7655055; DOI=10.1002/arch.940290307;
RA Dunkov B.C., Zhang D., Choumarov K., Winzerling J.J., Law J.H.;
RT "Isolation and characterization of mosquito ferritin and cloning of a cDNA
RT that encodes one subunit.";
RL Arch. Insect Biochem. Physiol. 29:293-307(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Red eye; TISSUE=Midgut;
RA Morlais I., Severson D.W.;
RT "Aedes aegypti ferritin heavy chain-like protein.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Red eye; TISSUE=Midgut;
RA Morlais I., Severson D.W.;
RT "Single nucleotide polymorphism and codon usage bias in Aedes aegypti.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [5]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12950250; DOI=10.1046/j.1432-1033.2003.03709.x;
RA Geiser D.L., Chavez C.A., Flores-Munguia R., Winzerling J.J., Pham D.Q.-D.;
RT "Aedes aegypti ferritin.";
RL Eur. J. Biochem. 270:3667-3674(2003).
CC -!- FUNCTION: Protection against toxic levels of iron. Stores iron in a
CC soluble, non-toxic, readily available form. Important for iron
CC homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous
CC form and deposited as ferric hydroxides after oxidation.
CC {ECO:0000269|PubMed:12950250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- SUBUNIT: Oligomer of 24 subunits. The functional molecule forms a
CC roughly spherical shell with a diameter of 12 nm and contains a central
CC cavity into which the insoluble ferric iron core is deposited (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Larvae, pupae, and adult females. Detected in
CC midgut. {ECO:0000269|PubMed:12950250}.
CC -!- INDUCTION: By blood meal, iron and hydrogen peroxide.
CC {ECO:0000269|PubMed:12950250}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; L37082; AAA99996.1; -; mRNA.
DR EMBL; AF326342; AAK15639.1; -; mRNA.
DR EMBL; AY064106; AAL85607.1; -; mRNA.
DR EMBL; CH477437; EAT40925.1; -; Genomic_DNA.
DR EMBL; CH477437; EAT40926.1; -; Genomic_DNA.
DR RefSeq; XP_001652731.1; XM_001652681.1.
DR RefSeq; XP_001652732.1; XM_001652682.1.
DR AlphaFoldDB; P41822; -.
DR SMR; P41822; -.
DR STRING; 7159.AAEL007385-PB; -.
DR PRIDE; P41822; -.
DR GeneID; 5569124; -.
DR KEGG; aag:5569124; -.
DR VEuPathDB; VectorBase:AAEL007385; -.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_2_0_1; -.
DR InParanoid; P41822; -.
DR OrthoDB; 1249457at2759; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR11431; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:7655055"
FT CHAIN 28..209
FT /note="Ferritin subunit"
FT /id="PRO_0000008853"
FT DOMAIN 40..193
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT CONFLICT 31
FT /note="Missing (in Ref. 4; EAT40925/EAT40926)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="S -> A (in Ref. 1; AAA99996, 2; AAK15639 and 3;
FT AAL85607)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> R (in Ref. 1; AAA99996, 2; AAK15639 and 3;
FT AAL85607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23747 MW; 202953E800B17B9C CRC64;
MMKSVFFGVV AITVAILSIY QETAQAQEQT VGATDNYQWD SVDDQCLAAL HRQINKEFDA
SIIYLKYAAY FAQEKINLPG FEKFFFHSAA EEREHGIKLI EYALMRGKAP VDKHFKLNYD
HEVPTVTTGE SALETALQKE VEVTKSIRGV IKACEDGSND FHLADYLTGE YLDEQHKGQR
ELAEKIATLK KMKKSAPKLG EFLFDKNHM
