P02244 (HEMT_PHAGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hemerythrin
Organism	Phascolopsis gouldii (Peanut worm) (Golfingia gouldii)
Taxonomic identifier	6442 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Annelida › Polychaeta › Sipuncula › Sipunculidea › Golfingiida › Sipunculidae › Phascolopsis

Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Oxygen transport Transport
Ligand	Iron Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	iron 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 114

113

Hemerythrin

PRO_0000191837

Sites

Metal binding

26

1

Iron 1

Metal binding

55

1

Iron 1

Metal binding

59

1

Iron 1

Metal binding

59

1

Iron 2

Metal binding

74

1

Iron 2

Metal binding

78

1

Iron 2

Metal binding

102

1

Iron 2

Metal binding

107

1

Iron 1

Metal binding

107

1

Iron 2

Natural variations

Natural variant

64

1

Q → E in minor component.

Natural variant

79

1

E → D in minor component.

Natural variant

80

1

T → G.

Natural variant

83

1

H → N in minor component.

Natural variant

97

1

S → A in minor and major variants.

Experimental info

Mutagenesis

99

1

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

Mutagenesis

99

1

L → Y: Decreased auto-oxidation rate. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

114

Helix Strand Turn

Details...

Helix

13 – 15

3

Helix

20 – 38

19

Helix

42 – 65

24

Helix

71 – 86

16

Helix

92 – 105

14

Helix

107 – 110

4

Turn

111 – 113

3

Sequences

	Sequence		Length	Mass (Da)
	P02244 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BF730C540D0769FC	FASTA	114	13,605
	10 20 30 40 50 60 MGFPIPDPYV WDPSFRTFYS IIDDEHKTLF NGIFHLAIDD NADNLGELRR CTGKHFLNEQ 70 80 90 100 110 VLMQASQYQF YDEHKKEHET FIHALDNWKG DVKWAKSWLV NHIKTIDFKY KGKI

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.

PIR

HRGG. A90553.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P02244.

SMR

P02244. Positions 2-114.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.20.120.50. 1 hit.

InterPro

IPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view]

PIRSF

PIRSF002033. Hemerythrin. 1 hit.

PRINTS

PR00186. HEMERYTHRIN.

SUPFAM

SSF47188. Hemryth_metal_bd. 1 hit.

TIGRFAMs

TIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.

PROSITE

PS00550. HEMERYTHRINS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02244.

Entry information

Entry name

HEMT_PHAGO

Accession

Primary (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:	April 3, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)