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Database: UniProt
Entry: P25915
LinkDB: P25915
Original site: P25915 
ID   FRIH_RABIT              Reviewed;         164 AA.
AC   P25915;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   01-OCT-2014, entry version 87.
DE   RecName: Full=Ferritin heavy chain;
DE            Short=Ferritin H subunit;
DE            EC=1.16.3.1;
DE   Flags: Fragment;
GN   Name=FTH1; Synonyms=FTH;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Vascular smooth muscle;
RX   PubMed=1655764;
RA   Liau G., Chan L.M., Feng P.;
RT   "Increased ferritin gene expression is both promoted by cAMP and a
RT   marker of growth arrest in rabbit vascular smooth muscle cells.";
RL   J. Biol. Chem. 266:18819-18826(1991).
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
CC       form. Important for iron homeostasis. Has ferroxidase activity.
CC       Iron is taken up in the ferrous form and deposited as ferric
CC       hydroxides after oxidation. Also plays a role in delivery of iron
CC       to cells. Mediates iron uptake in capsule cells of the developing
CC       kidney (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
CC   -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
CC       L (light) chain and H (heavy) chain. The major chain can be light
CC       or heavy, depending on the species and tissue type. The functional
CC       molecule forms a roughly spherical shell with a diameter of 12 nm
CC       and contains a central cavity into which the insoluble mineral
CC       iron core is deposited.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00085}.
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DR   EMBL; M63912; AAA31247.1; -; mRNA.
DR   PIR; I46710; I46710.
DR   UniGene; Ocu.1521; -.
DR   ProteinModelPortal; P25915; -.
DR   SMR; P25915; 1-158.
DR   STRING; 9986.ENSOCUP00000012121; -.
DR   eggNOG; COG1528; -.
DR   HOGENOM; HOG000223383; -.
DR   HOVERGEN; HBG000410; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IEA:Ensembl.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR001519; Ferritin.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012347; Ferritin-rel.
DR   InterPro; IPR014034; Ferritin_CS.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; PTHR11431; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS00540; FERRITIN_1; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Iron; Iron storage; Metal-binding; Oxidoreductase;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN        <1    164       Ferritin heavy chain.
FT                                /FTId=PRO_0000201052.
FT   DOMAIN       <1    141       Ferritin-like diiron.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00085}.
FT   METAL         9      9       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL        44     44       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL        44     44       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL        47     47       Iron 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL        89     89       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   METAL       123    123       Iron 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00085}.
FT   MOD_RES     160    160       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     164    164       Phosphoserine. {ECO:0000250}.
FT   NON_TER       1      1
SQ   SEQUENCE   164 AA;  19193 MW;  C1805C5CE8FBB389 CRC64;
     AINRQINLEL YASYVYLSMS YYFDRDDVAL KNFAKYFLHQ SHEEREHAEK LMKLQNQRGG
     RIFLQDIKKP EYDDWESGLN AMECALHLEK SVNQSLLELH KLATDKNDPH LCDFIETHYL
     NEQVKSIKEL GDHVTNLRKM GAPESGMAEY LFDKHTLGHS DNES
//
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