Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02244

- HEMT_PHAGO

UniProt

P02244 - HEMT_PHAGO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hemerythrin

Gene
N/A
Organism
Phascolopsis gouldii (Peanut worm) (Golfingia gouldii)
Status
Reviewed - 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 1
Metal bindingi55 – 551Iron 1
Metal bindingi59 – 591Iron 1
Metal bindingi59 – 591Iron 2
Metal bindingi74 – 741Iron 2
Metal bindingi78 – 781Iron 2
Metal bindingi102 – 1021Iron 2
Metal bindingi107 – 1071Iron 1
Metal bindingi107 – 1071Iron 2

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. oxygen transporter activity Source: UniProtKB-KW
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 methioninei1 – 11Removed1 Publication
Chaini2 – 114113HemerythrinPRO_0000191837Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
IPR012827. Haemerythrin-like_metal-bd.
IPR016131. Haemerythrin_Fe_BS.
[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:
EMBL
GenBank
DDBJ
Links Updated
AF220529 mRNA. Translation: AAF25482.1.
PIRiA90553. HRGG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF220529 mRNA. Translation: AAF25482.1 .
PIRi A90553. HRGG.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HRB X-ray 5.50 A/B 2-114 [» ]
1I4Y X-ray 1.80 A/B/C/D/E/F/G/H 1-114 [» ]
1I4Z X-ray 2.10 A/B/C/D/E/F/G/H 1-114 [» ]
ProteinModelPortali P02244.
SMRi P02244. Positions 2-114.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02244.

Family and domain databases

Gene3Di 1.20.120.50. 1 hit.
InterProi IPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view ]
PIRSFi PIRSF002033. Hemerythrin. 1 hit.
PRINTSi PR00186. HEMERYTHRIN.
SUPFAMi SSF47188. SSF47188. 1 hit.
TIGRFAMsi TIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEi PS00550. HEMERYTHRINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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: October 1, 2014
This is version 89 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

External Data

Dasty 3