GenomeNet

Database: UniProt
Entry: A0A340WFZ6_LIPVE
LinkDB: A0A340WFZ6_LIPVE
Original site: A0A340WFZ6_LIPVE 
ID   A0A340WFZ6_LIPVE        Unreviewed;       256 AA.
AC   A0A340WFZ6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
GN   Name=LOC103075683 {ECO:0000313|RefSeq:XP_007448523.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007448523.1};
RN   [1] {ECO:0000313|RefSeq:XP_007448523.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form
CC       (By similarity). Important for iron homeostasis (By similarity). Has
CC       ferroxidase activity (By similarity). Iron is taken up in the ferrous
CC       form and deposited as ferric hydroxides after oxidation (By
CC       similarity). Also plays a role in delivery of iron to cells (By
CC       similarity). Mediates iron uptake in capsule cells of the developing
CC       kidney. {ECO:0000256|ARBA:ARBA00037207}.
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC       Important for iron homeostasis. Iron is taken up in the ferrous form
CC       and deposited as ferric hydroxides after oxidation.
CC       {ECO:0000256|RuleBase:RU361145}.
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         Evidence={ECO:0000256|ARBA:ARBA00001830};
CC   -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC       (light) chain and H (heavy) chain. The major chain can be light or
CC       heavy, depending on the species and tissue type. The functional
CC       molecule forms a roughly spherical shell with a diameter of 12 nm and
CC       contains a central cavity into which the insoluble mineral iron core is
CC       deposited. {ECO:0000256|ARBA:ARBA00026060}.
CC   -!- SIMILARITY: Belongs to the ferritin family.
CC       {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_007448523.1; XM_007448461.1.
DR   AlphaFoldDB; A0A340WFZ6; -.
DR   STRING; 118797.A0A340WFZ6; -.
DR   GeneID; 103075683; -.
DR   KEGG; lve:103075683; -.
DR   InParanoid; A0A340WFZ6; -.
DR   OrthoDB; 4611704at2759; -.
DR   Proteomes; UP000265300; Unplaced.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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; IPR014034; Ferritin_CS.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF37; FERRITIN HEAVY CHAIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW   Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW   ECO:0000256|RuleBase:RU361145};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361145};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT   DOMAIN          84..233
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
FT   REGION          22..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  29050 MW;  27003FB572BAD886 CRC64;
     MRLNIKSRVL AESRRGFLLQ QCLDGTRRSS PAPAGRSEPA LATTSRRPPT APRSPPPLQR
     RAATATVSPQ PPAMTTASPS QVRQNYHQDS EAAINSQINL ELHASYVYLS MSYYLDRDDV
     ALKNFAKYFL HQSCEEREHA EELRKLQNQR GGRIFLQEIR KPDRDDWENG LNAMECALHL
     EKSVTQSLLE LHKLATEKND PYLCDFIETH YLNEQVKSIK ELGDHVTNLR TMGAPESGMA
     QYLFDKHTLG NSDNES
//
DBGET integrated database retrieval system