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P80255

- HEMT2_HEDDI

UniProt

P80255 - HEMT2_HEDDI

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Protein

Hemerythrin

Gene
N/A
Organism
Hediste diversicolor (Sandworm) (Nereis diversicolor)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Iron 1 By similarity
Metal bindingi55 – 551Iron 1 By similarity
Metal bindingi59 – 591Iron 1 By similarity
Metal bindingi59 – 591Iron 2 By similarity
Metal bindingi75 – 751Iron 2 By similarity
Metal bindingi79 – 791Iron 2 By similarity
Metal bindingi108 – 1081Iron 2 By similarity
Metal bindingi113 – 1131Iron 1 By similarity
Metal bindingi113 – 1131Iron 2 By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. oxygen transporter activity Source: InterPro

GO - Biological processi

  1. response to cadmium ion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cadmium resistance

Keywords - Ligandi

Cadmium, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemerythrin
Alternative name(s):
MP II
Short name:
MPII
Non-metallothionein cadmium-binding protein
Short name:
CD-BP
OrganismiHediste diversicolor (Sandworm) (Nereis diversicolor)
Taxonomic identifieri126592 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaPalpataAciculataPhyllodocidaNereididaeHedisteHediste diversicolor species group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 120119HemerythrinPRO_0000191834Add
BLAST

Expressioni

Tissue specificityi

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 1.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP80255.
SMRiP80255. Positions 2-120.

Family & Domainsi

Sequence similaritiesi

Belongs to the hemerythrin family.

Family and domain databases

Gene3Di1.20.120.50. 1 hit.
InterProiIPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR012312. Haemerythrin/HHE_cat-bd_motif.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view]
PfamiPF01814. Hemerythrin. 1 hit.
[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.

P80255-1 [UniParc]FASTAAdd to Basket

« Hide

MGFEIPEPYK WDESFQVFYE KLDEEHKQIF NAIFALCGGN NADNLKSLVD    50
VTANHFADEE AMMKASGSYG DFDSHKKKHE DFLAVIRGLG APVPQDKINY 100
AKEWLVNHIK GTDFGYKGKL 120
Length:120
Mass (Da):13,647
Last modified:July 1, 2008 - v2
Checksum:i93AA715E7E695422
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71E → Q in S57799. 1 Publication
Sequence conflicti11 – 111W → Q1 Publication
Sequence conflicti27 – 282KQ → GK in S57799. 1 Publication
Sequence conflicti43 – 431D → G AA sequence 1 Publication
Sequence conflicti56 – 561F → P in S57799. 1 Publication
Sequence conflicti58 – 581D → E1 Publication
Sequence conflicti63 – 631M → L AA sequence 1 Publication
Sequence conflicti67 – 671G → A AA sequence 1 Publication
Sequence conflicti99 – 991N → D1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S57799 mRNA. No translation available.
PIRiS38261.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S57799 mRNA. No translation available.
PIRi S38261.

3D structure databases

ProteinModelPortali P80255.
SMRi P80255. Positions 2-120.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.20.120.50. 1 hit.
InterProi IPR002063. Haemerythrin.
IPR012827. Haemerythrin-like_metal-bd.
IPR012312. Haemerythrin/HHE_cat-bd_motif.
IPR016131. Haemerythrin_Fe_BS.
[Graphical view ]
Pfami PF01814. Hemerythrin. 1 hit.
[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. "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.

Entry informationi

Entry nameiHEMT2_HEDDI
AccessioniPrimary (citable) accession number: P80255
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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