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Protein

Hemerythrin

Gene
N/A
Organism
Phascolopsis gouldii (Peanut worm) (Golfingia gouldii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Iron 1Combined sources1 Publication
Metal bindingi55 – 551Iron 1Combined sources1 Publication
Metal bindingi59 – 591Iron 1Combined sources1 Publication
Metal bindingi59 – 591Iron 2Combined sources1 Publication
Metal bindingi74 – 741Iron 2Combined sources1 Publication
Metal bindingi78 – 781Iron 2Combined sources1 Publication
Metal bindingi102 – 1021Iron 2Combined sources1 Publication
Metal bindingi107 – 1071Iron 1Combined sources1 Publication
Metal bindingi107 – 1071Iron 2Combined sources1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemerythrin
OrganismiPhascolopsis gouldii (Peanut worm) (Golfingia gouldii)
Taxonomic identifieri6442 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaSipunculaSipunculideaGolfingiidaSipunculidaePhascolopsis

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991L → X: Increased auto-oxidation rate (when X different from Tyr). 1 Publication
Mutagenesisi99 – 991L → Y: Decreased auto-oxidation rate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 114113HemerythrinPRO_0000191837Add
BLAST

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 153Combined sources
Helixi20 – 3819Combined sources
Helixi42 – 6524Combined sources
Helixi71 – 8616Combined sources
Helixi92 – 10514Combined sources
Helixi107 – 1104Combined sources
Turni111 – 1133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02244.
SMRiP02244. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02244.

Family & Domainsi

Sequence similaritiesi

Belongs to the hemerythrin family.Curated

Family and domain databases

Gene3Di1.20.120.50. 1 hit.
InterProiIPR002063. Haemerythrin.
IPR016131. Haemerythrin_Fe_BS.
IPR012827. Haemerythrin_metal-bd.
[Graphical view]
PIRSFiPIRSF002033. Hemerythrin. 1 hit.
PRINTSiPR00186. HEMERYTHRIN.
SUPFAMiSSF47188. SSF47188. 1 hit.
TIGRFAMsiTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEiPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFPIPDPYV WDPSFRTFYS IIDDEHKTLF NGIFHLAIDD NADNLGELRR
60 70 80 90 100
CTGKHFLNEQ VLMQASQYQF YDEHKKEHET FIHALDNWKG DVKWAKSWLV
110
NHIKTIDFKY KGKI
Length:114
Mass (Da):13,605
Last modified:January 23, 2007 - v3
Checksum:iBF730C540D0769FC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641Q → E in minor component.
Natural varianti79 – 791E → D in minor component.
Natural varianti80 – 801T → G.
Natural varianti83 – 831H → N in minor component.
Natural varianti97 – 971S → A in minor and major variants.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220529 mRNA. Translation: AAF25482.1.
PIRiA90553. HRGG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220529 mRNA. Translation: AAF25482.1.
PIRiA90553. HRGG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02244.
SMRiP02244. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02244.

Family and domain databases

Gene3Di1.20.120.50. 1 hit.
InterProiIPR002063. Haemerythrin.
IPR016131. Haemerythrin_Fe_BS.
IPR012827. Haemerythrin_metal-bd.
[Graphical view]
PIRSFiPIRSF002033. Hemerythrin. 1 hit.
PRINTSiPR00186. HEMERYTHRIN.
SUPFAMiSSF47188. SSF47188. 1 hit.
TIGRFAMsiTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEiPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEMT_PHAGO
AccessioniPrimary (citable) accession number: P02244
Secondary accession number(s): Q9U3V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.