ID   FRIH_AEDAE              Reviewed;         209 AA.
AC   P41822; Q172H1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Ferritin heavy chain {ECO:0000305};
DE            EC=1.16.3.1 {ECO:0000250|UniProtKB:P02794};
DE   AltName: Full=AeFer(H);
DE   AltName: Full=Ferritin heavy chain-like protein;
DE   Flags: Precursor;
GN   Name=FERH; Synonyms=HCH {ECO:0000303|PubMed:12950250};
GN   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], PROTEIN SEQUENCE OF 28-68, AND DEVELOPMENTAL
RP   STAGE.
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   INDUCTION, AND DEVELOPMENTAL STAGE.
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).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=16503479; DOI=10.1016/j.ibmb.2005.12.001;
RA   Geiser D.L., Zhang D., Winzerling J.J.;
RT   "Secreted ferritin: mosquito defense against iron overload?";
RL   Insect Biochem. Mol. Biol. 36:177-187(2006).
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC       Important for iron homeostasis. Has ferroxidase activity. Iron is taken
CC       up in the ferrous form and deposited as ferric hydroxides after
CC       oxidation. {ECO:0000250|UniProtKB:P02794}.
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. There are two types of subunits: L
CC       (light) chain and H (heavy) chain. 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 mineral iron core is deposited.
CC       {ECO:0000250|UniProtKB:P02794}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16503479}. Cytoplasm
CC       {ECO:0000269|PubMed:16503479}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in larvae, pupae and female adults (at
CC       protein Level). {ECO:0000269|PubMed:12950250,
CC       ECO:0000269|PubMed:7655055}.
CC   -!- INDUCTION: By blood meal, iron and hydrogen peroxide (at protein
CC       level). {ECO:0000269|PubMed:12950250, ECO:0000269|PubMed:16503479}.
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.P41822; -.
DR   PaxDb; 7159-AAEL007385-PB; -.
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; 5346227at2759; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   Proteomes; UP000682892; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   CDD; cd01056; Euk_Ferritin; 1.
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; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF43; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; 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 heavy chain"
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
//