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-MAY-2013, entry version 83.
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).
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.
CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
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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 OrthoDB; EOG47PX78; -.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA: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; 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; Ferritin/RR_like; 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 METAL 9 9 Iron 1 (By similarity).
FT METAL 44 44 Iron 1 (By similarity).
FT METAL 44 44 Iron 2 (By similarity).
FT METAL 47 47 Iron 1 (By similarity).
FT METAL 89 89 Iron 2 (By similarity).
FT METAL 123 123 Iron 2 (By similarity).
FT MOD_RES 156 156 Phosphothreonine (By similarity).
FT MOD_RES 160 160 Phosphoserine (By similarity).
FT MOD_RES 164 164 Phosphoserine (By similarity).
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
//
