P80255 (HEMT2_HEDDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hemerythrin Alternative name(s): MP II Short name=MPII Non-metallothionein cadmium-binding protein Short name=CD-BP
Organism	Hediste diversicolor (Sandworm) (Nereis diversicolor)
Taxonomic identifier	126592 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Annelida › Polychaeta › Palpata › Aciculata › Phyllodocida › Nereididae › Hediste › Hediste diversicolor species group

Protein attributes

Sequence length	120 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	May act as a buffer to control the concentration and therefore the toxicity of cadmium. Also involved in defence towards bacteria growth by acting as an iron scavenger. Ref.1
Tissue specificity	Expressed and produced in a hematopoietic center that floats freely in the coelomic fluid before being stored in a particular hemocyte type: the granulocyte type 1. Ref.1
Sequence similarities	Belongs to the hemerythrin family.

Ontologies

Keywords
Biological process	Cadmium resistance
Ligand	Cadmium Iron Metal-binding
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	oxygen transport Inferred from electronic annotation. Source: GOC response to cadmium ion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: InterPro
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 Ref.3
	Chain	2 – 120	119	Hemerythrin		PRO_0000191834
Sites
	Metal binding	26	1	Iron 1 By similarity
	Metal binding	55	1	Iron 1 By similarity
	Metal binding	59	1	Iron 1 By similarity
	Metal binding	59	1	Iron 2 By similarity
	Metal binding	75	1	Iron 2 By similarity
	Metal binding	79	1	Iron 2 By similarity
	Metal binding	108	1	Iron 2 By similarity
	Metal binding	113	1	Iron 1 By similarity
	Metal binding	113	1	Iron 2 By similarity
Experimental info
	Sequence conflict	7	1	E → Q in S57799. Ref.4
	Sequence conflict	11	1	W → Q Ref.1
	Sequence conflict	27 – 28	2	KQ → GK in S57799. Ref.4
	Sequence conflict	43	1	D → G AA sequence Ref.2
	Sequence conflict	56	1	F → P in S57799. Ref.4
	Sequence conflict	58	1	D → E Ref.1
	Sequence conflict	63	1	M → L AA sequence Ref.2
	Sequence conflict	67	1	G → A AA sequence Ref.2
	Sequence conflict	99	1	N → D Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P80255 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: 93AA715E7E695422	FASTA	120	13,647
	10 20 30 40 50 60 MGFEIPEPYK WDESFQVFYE KLDEEHKQIF NAIFALCGGN NADNLKSLVD VTANHFADEE 70 80 90 100 110 120 AMMKASGSYG DFDSHKKKHE DFLAVIRGLG APVPQDKINY AKEWLVNHIK GTDFGYKGKL

References

[1]	"Antibacterial properties of hemerythrin of the sand worm Nereis diversicolor." Deloffre L., Salzet-Raveillon B., Vieau D., Andries J.-C., Salzet M. Neuroendocrinol. Lett. 24:39-45(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"Amino acid sequence of the small cadmium-binding protein (MP II) from Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin structure." Demuynck S., Li K.W., van der Schors R., Dhainaut-Courtois N. Eur. J. Biochem. 217:151-156(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-120.
[3]	"Homologies between hemerythrins of sipunculids and cadmium-binding metalloprotein (MP II) from a polychaete annelid, Nereis diversicolor." Demuynck S., Sautiere P., van Beeumen J., Dhainaut-Courtois N. C. R. Acad. Sci. III, Sci. Vie 312:317-322(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-34.
[4]	"Detection of mRNA encoding an antibacterial-metalloprotein (MPII) by in situ hybridization with a cDNA probe generated by polymerase chain reaction in the worm Nereis diversicolor." Salzet-Raveillon B., Rentier-Delrue F., Dhainaut A. Cell. Mol. Biol. 39:105-114(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-79.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S57799 mRNA. No translation available.
PIR	S38261.
3D structure databases
ProteinModelPortal	P80255.
SMR	P80255. Positions 2-120.
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. IPR012312. Haemerythrin/HHE_cat-bd_motif. IPR016131. Haemerythrin_Fe_BS. [Graphical view]
Pfam	PF01814. Hemerythrin. 1 hit. [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

HEMT2_HEDDI

Accession

Primary (citable) accession number: P80255

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	July 1, 2008
Last modified:	April 3, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)