Q920H8 · HEPH_RAT
- ProteinHephaestin
- GeneHeph
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1157 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plasma membrane ferroxidase that mediates the extracellular conversion of ferrous/Fe2+ iron into its ferric/Fe3+ form. Couples ferroportin which specifically exports ferrous/Fe2+ iron from cells to transferrin that only binds and shuttles extracellular ferric/Fe3+ iron throughout the body. By helping iron transfer from cells to blood mainly contributes to dietary iron absorption by the intestinal epithelium and more generally regulates iron levels in the body.
Catalytic activity
- 4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2OThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 6 Cu cations per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 70 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 73 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 126 | Cu2+ 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 126 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | Cu2+ 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 134 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 152 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 153 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 186 | Cu2+ 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 186 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 188 | Cu2+ 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 265 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 304 | Cu2+ 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 347 | Cu2+ 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 352 | Cu2+ 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 416 | Na+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 425 | Na+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 428 | Na+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 616 | Na+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 655 | Cu2+ 5 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 698 | Cu2+ 5 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 703 | Cu2+ 5 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 708 | Cu2+ 5 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 768 | Na+ 3 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 777 | Na+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 999 | Cu2+ 6 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 1002 | Cu2+ 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 1002 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1004 | Cu2+ 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 1004 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1044 | Cu2+ 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 1045 | Cu2+ 6 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 1046 | Cu2+ 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 1046 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1050 | Cu2+ 6 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 1055 | Cu2+ 6 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basolateral plasma membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | copper ion binding | |
Molecular Function | ferrous iron binding | |
Molecular Function | ferroxidase activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | erythrocyte differentiation | |
Biological Process | intestinal iron absorption | |
Biological Process | iron ion transport | |
Biological Process | multicellular organismal-level iron ion homeostasis | |
Biological Process | positive regulation of iron export across plasma membrane |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHephaestin
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ920H8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Basolateral cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-1109 | Extracellular | ||||
Sequence: AIRNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGTLDGNSPPQRKDVDHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKVDSCSMDPPVEQLTGKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEETHLGILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPACLTWMYFSAADPTRDTNSGLVGPLLVCKAGALGEDGKQKGVDKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDVHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQCSSHQDSPRQHYQASRVYYIMAEEIEWDYCPDRSWELEWYNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDMYSGLVGPLVICRNGILEPNGGRNDMDREFALLFLIFDENQSWYLKENIATYGPQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDIHTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHEEHFSTMTTITKEIGKAVILQNIGEGNVKMLGMNIPVKNVEILSS | ||||||
Transmembrane | 1110-1130 | Helical | ||||
Sequence: ALIAICVVLLLIALALGGVVW | ||||||
Topological domain | 1131-1157 | Cytoplasmic | ||||
Sequence: YQHRQRKLRRNRRSILDDSFKLLSLKQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MKAGHLLWALLLMHSLCSLPTDG | ||||||
Chain | PRO_0000002917 | 24-1157 | Hephaestin | |||
Sequence: AIRNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGTLDGNSPPQRKDVDHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKVDSCSMDPPVEQLTGKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEETHLGILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPACLTWMYFSAADPTRDTNSGLVGPLLVCKAGALGEDGKQKGVDKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDVHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQCSSHQDSPRQHYQASRVYYIMAEEIEWDYCPDRSWELEWYNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDMYSGLVGPLVICRNGILEPNGGRNDMDREFALLFLIFDENQSWYLKENIATYGPQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDIHTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHEEHFSTMTTITKEIGKAVILQNIGEGNVKMLGMNIPVKNVEILSSALIAICVVLLLIALALGGVVWYQHRQRKLRRNRRSILDDSFKLLSLKQ | ||||||
Glycosylation | 49 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 54 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 180↔206 | |||||
Sequence: CLTWIYHSHVDAPRDIATGLIGPLITC | ||||||
Glycosylation | 236 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 285↔366 | |||||
Sequence: CAQKHVAWHLFGMGNEIDVHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKVDSC | ||||||
Disulfide bond | 533↔559 | |||||
Sequence: CLTWMYFSAADPTRDTNSGLVGPLLVC | ||||||
Glycosylation | 587 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 636↔717 | |||||
Sequence: CKGDTVAWHLLGLGTENDVHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC | ||||||
Glycosylation | 713 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 757 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 876↔902 | |||||
Sequence: CVSWIYYSAVDPIKDMYSGLVGPLVIC | ||||||
Glycosylation | 930 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 1144 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1149 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1154 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of a complex composed of SLC40A1/ferroportin, TF/transferrin and HEPH/hephaestin that transfers iron from cells to transferrin.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-206 | Plastocyanin-like 1 | ||||
Sequence: AIRNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIYHSHVDAPRDIATGLIGPLITC | ||||||
Domain | 218-366 | Plastocyanin-like 2 | ||||
Sequence: QRKDVDHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKVDSC | ||||||
Domain | 370-559 | Plastocyanin-like 3 | ||||
Sequence: PPVEQLTGKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEETHLGILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPACLTWMYFSAADPTRDTNSGLVGPLLVC | ||||||
Domain | 569-717 | Plastocyanin-like 4 | ||||
Sequence: KQKGVDKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDVHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC | ||||||
Domain | 730-902 | Plastocyanin-like 5 | ||||
Sequence: ASRVYYIMAEEIEWDYCPDRSWELEWYNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDMYSGLVGPLVIC | ||||||
Domain | 910-1066 | Plastocyanin-like 6 | ||||
Sequence: NGGRNDMDREFALLFLIFDENQSWYLKENIATYGPQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDIHTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHEE |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,157
- Mass (Da)129,593
- Last updated2001-12-01 v1
- Checksum0C626FA3E2F51DE2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2R2A9 | A0A8L2R2A9_RAT | Heph | 1157 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF246120 EMBL· GenBank· DDBJ | AAL08217.1 EMBL· GenBank· DDBJ | mRNA |