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P02244 (HEMT_PHAGO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemerythrin
OrganismPhascolopsis gouldii (Peanut worm) (Golfingia gouldii)
Taxonomic identifier6442 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaSipunculaSipunculideaGolfingiidaSipunculidaePhascolopsis

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.

Subunit structure

Homooctamer.

Miscellaneous

The sequence from one of the four major component variants is shown.

Sequence similarities

Belongs to the hemerythrin family.

Ontologies

Keywords
   Biological processOxygen transport
Transport
   LigandIron
Metal-binding
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

oxygen transporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 114113Hemerythrin
PRO_0000191837

Sites

Metal binding261Iron 1
Metal binding551Iron 1
Metal binding591Iron 1
Metal binding591Iron 2
Metal binding741Iron 2
Metal binding781Iron 2
Metal binding1021Iron 2
Metal binding1071Iron 1
Metal binding1071Iron 2

Natural variations

Natural variant641Q → E in minor component.
Natural variant791E → D in minor component.
Natural variant801T → G.
Natural variant831H → N in minor component.
Natural variant971S → A in minor and major variants.

Experimental info

Mutagenesis991L → X: Increased auto-oxidation rate (when X different from Tyr). Ref.1
Mutagenesis991L → Y: Decreased auto-oxidation rate. Ref.1

Secondary structure

.............. 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02244 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BF730C540D0769FC

FASTA11413,605
        10         20         30         40         50         60 
MGFPIPDPYV WDPSFRTFYS IIDDEHKTLF NGIFHLAIDD NADNLGELRR CTGKHFLNEQ 

        70         80         90        100        110 
VLMQASQYQF YDEHKKEHET FIHALDNWKG DVKWAKSWLV NHIKTIDFKY KGKI 

« Hide

References

[1]"A leucine residue 'Gates' solvent but not O2 access to the binding pocket of Phascolopsis gouldii hemerythrin."
Farmer C.S., Kurtz D.M. Jr., Phillips R.S., Ai J., Sanders-Loehr J.
J. Biol. Chem. 275:17043-17050(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LEU-99.
[2]"The primary structure of Golfingia gouldii hemerythrin. Oder of peptides in fragments produced by tryptic digestion of succinylated hemerythrin. Complete amino acid sequence."
Klippenstein G.L., Holleman J.W., Klotz I.M.
Biochemistry 7:3868-3878(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-114.
[3]"The amino-terminal sequence of Dendrostomum pyroides hemerythrin."
Ferrell R.E., Kitto G.B.
FEBS Lett. 12:322-324(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 11-12.
[4]"New evidence for glutamic acid as an iron ligand in hemerythrin."
Gormley P.M., Loehr J.S., Brimhall B., Hermodson M.A.
Biochem. Biophys. Res. Commun. 85:1360-1366(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 59-60.
[5]"Molecular variants of Golfingia gouldii hemerythrin. The primary structure of the variants arising from five amino acid interchanges."
Klippenstein G.L.
Biochemistry 11:372-379(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS.
[6]"Atomic models for the polypeptide backbones of myohemerythrin and hemerythrin."
Hendrickson W.A., Ward K.B.
Biochem. Biophys. Res. Commun. 66:1349-1356(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS).
[7]"The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket."
Farmer C.S., Kurtz D.M. Jr., Liu Z.-J., Wang B.C., Rose J., Ai J., Sanders-Loehr J.
J. Biol. Inorg. Chem. 6:418-429(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF220529 mRNA. Translation: AAF25482.1.
PIRHRGG. A90553.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HRBX-ray5.50A/B2-114[»]
1I4YX-ray1.80A/B/C/D/E/F/G/H1-114[»]
1I4ZX-ray2.10A/B/C/D/E/F/G/H1-114[»]
ProteinModelPortalP02244.
SMRP02244. Positions 2-114.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.120.50. 1 hit.
InterProIPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view]
PIRSFPIRSF002033. Hemerythrin. 1 hit.
PRINTSPR00186. HEMERYTHRIN.
SUPFAMSSF47188. SSF47188. 1 hit.
TIGRFAMsTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02244.

Entry information

Entry nameHEMT_PHAGO
AccessionPrimary (citable) accession number: P02244
Secondary accession number(s): Q9U3V2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references