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Protein

Yolk ferritin

Gene
N/A
Organism
Lymnaea stagnalis (Great pond snail) (Helix stagnalis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron 1PROSITE-ProRule annotation
Metal bindingi79 – 791Iron 1PROSITE-ProRule annotation
Metal bindingi79 – 791Iron 2PROSITE-ProRule annotation
Metal bindingi165 – 1651Iron 2PROSITE-ProRule annotation
Metal bindingi199 – 1991Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Yolk ferritin (EC:1.16.3.1)
OrganismiLymnaea stagnalis (Great pond snail) (Helix stagnalis)
Taxonomic identifieri6523 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaLymnaeoideaLymnaeidaeLymnaea

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 239221Yolk ferritinPRO_0000008852Add
BLAST

Expressioni

Tissue specificityi

Midgut gland and bloodstream.

Developmental stagei

First detected during pregastrulation stage, levels increase up to the hatching stage, and is still present at the late veliger stage.

Interactioni

Subunit structurei

Oligomer of 12 or 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric ferric iron core is deposited (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP42578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 217191Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 14642Insertion; not present in other ferritinsAdd
BLAST

Domaini

Contains an 'insertion' sequence of 42 residues which is not present in other ferritins.

Sequence similaritiesi

Belongs to the ferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.20.1260.10. 2 hits.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 2 hits.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSVLFLTLA VCSSLAYGKE FVATVRQNYK ENINQLLEQQ IQKELAASYI
60 70 80 90 100
YQAYASYFQR ADVSLPGIKK FFSDASSEER DDAQSLIDYI NQRGGHVQYD
110 120 130 140 150
KIDLKDACET VMKFVTSDTS GLEEFRDRRM CICGFVATKT INDNCGERSD
160 170 180 190 200
WKEGLIAFED TLAIERYVNA QLLDIHKKAD DEKDAHLTHI LEHEFLEEQV
210 220 230
SSINKIAHAI TRLRSFEQGS GNNYKLGRVY LRPTPQISH
Length:239
Mass (Da):27,338
Last modified:November 1, 1995 - v1
Checksum:iE1C5873012DEEFFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56779 mRNA. Translation: CAA40097.1.
PIRiS45604.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56779 mRNA. Translation: CAA40097.1.
PIRiS45604.

3D structure databases

ProteinModelPortaliP42578.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.20.1260.10. 2 hits.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 2 hits.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and deduced amino acid sequence of two ferritins: soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis L."
    von Darl M., Harrison M., Bottke W.
    Eur. J. Biochem. 222:353-366(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38.
    Tissue: Midgut.

Entry informationi

Entry nameiFRIY_LYMST
AccessioniPrimary (citable) accession number: P42578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.