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P80255 (HEMT2_HEDDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemerythrin
Alternative name(s):
MP II
Short name=MPII
Non-metallothionein cadmium-binding protein
Short name=CD-BP
OrganismHediste diversicolor (Sandworm) (Nereis diversicolor)
Taxonomic identifier126592 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaPalpataAciculataPhyllodocidaNereididaeHedisteHediste diversicolor species group

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCadmium resistance
   LigandCadmium
Iron
Metal-binding
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processresponse to cadmium ion

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

oxygen transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 120119Hemerythrin
PRO_0000191834

Sites

Metal binding261Iron 1 By similarity
Metal binding551Iron 1 By similarity
Metal binding591Iron 1 By similarity
Metal binding591Iron 2 By similarity
Metal binding751Iron 2 By similarity
Metal binding791Iron 2 By similarity
Metal binding1081Iron 2 By similarity
Metal binding1131Iron 1 By similarity
Metal binding1131Iron 2 By similarity

Experimental info

Sequence conflict71E → Q in S57799. Ref.4
Sequence conflict111W → Q Ref.1
Sequence conflict27 – 282KQ → GK in S57799. Ref.4
Sequence conflict431D → G AA sequence Ref.2
Sequence conflict561F → P in S57799. Ref.4
Sequence conflict581D → E Ref.1
Sequence conflict631M → L AA sequence Ref.2
Sequence conflict671G → A AA sequence Ref.2
Sequence conflict991N → D Ref.1

Sequences

Sequence LengthMass (Da)Tools
P80255 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 93AA715E7E695422

FASTA12013,647
        10         20         30         40         50         60 
MGFEIPEPYK WDESFQVFYE KLDEEHKQIF NAIFALCGGN NADNLKSLVD VTANHFADEE 

        70         80         90        100        110        120 
AMMKASGSYG DFDSHKKKHE DFLAVIRGLG APVPQDKINY AKEWLVNHIK GTDFGYKGKL 

« Hide

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.
PIRS38261.

3D structure databases

ProteinModelPortalP80255.
SMRP80255. Positions 2-120.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.120.50. 1 hit.
InterProIPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR012312. Haemerythrin/HHE_cat-bd_motif.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view]
PfamPF01814. Hemerythrin. 1 hit.
[Graphical view]
PIRSFPIRSF002033. Hemerythrin. 1 hit.
PRINTSPR00186. HEMERYTHRIN.
SUPFAMSSF47188. SSF47188. 1 hit.
TIGRFAMsTIGR02481. hemeryth_dom. 1 hit.
TIGR00058. Hemerythrin. 1 hit.
PROSITEPS00550. HEMERYTHRINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEMT2_HEDDI
AccessionPrimary (citable) accession number: P80255
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families