P02245 (HEMT_THEHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hemerythrin
Organism	Themiste hennahi (Peanut worm) (Themiste zostericola)
Taxonomic identifier	360549 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Annelida › Polychaeta › Sipuncula › Sipunculidea › Golfingiida › Themistidae › Themiste

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the hemerythrin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Iron Metal-binding
Technical term	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
	Chain	1 – 113	113	Hemerythrin		PRO_0000191843
Sites
	Metal binding	25	1	Iron 1 By similarity
	Metal binding	54	1	Iron 1 By similarity
	Metal binding	58	1	Iron 1 By similarity
	Metal binding	58	1	Iron 2 By similarity
	Metal binding	73	1	Iron 2 By similarity
	Metal binding	77	1	Iron 2 By similarity
	Metal binding	101	1	Iron 2 By similarity
	Metal binding	106	1	Iron 1 By similarity
	Metal binding	106	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P02245 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D44982F4C55654B1	FASTA	113	13,421
	10 20 30 40 50 60 GFPIPDPYGW DPSFRTFYSI IDDEHKTLFN GIFHLAIDDN ADNLGELRRC TGKHFLNQEV 70 80 90 100 110 LMQASQYQFY DEHKKAHEEF IRALDNWKGD VKWAKSWLVN HIKTIDFKYK GKI

References

[1]	"Structural studies on Dendrostomum pyroides hemerythrin." Ferrell R.E., Kitto G.B. Biochemistry 10:2923-2929(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases
PIR	HRTH. A02571.
3D structure databases
ProteinModelPortal	P02245.
SMR	P02245. Positions 1-113.
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...

Entry information

Entry name

HEMT_THEHE

Accession

Primary (citable) accession number: P02245

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)