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P80255

- HEMT2_HEDDI

UniProt

P80255 - HEMT2_HEDDI

Protein

Hemerythrin

Gene
N/A
Organism
Hediste diversicolor (Sandworm) (Nereis diversicolor)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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 1By similarity
    Metal bindingi55 – 551Iron 1By similarity
    Metal bindingi59 – 591Iron 1By similarity
    Metal bindingi59 – 591Iron 2By similarity
    Metal bindingi75 – 751Iron 2By similarity
    Metal bindingi79 – 791Iron 2By similarity
    Metal bindingi108 – 1081Iron 2By similarity
    Metal bindingi113 – 1131Iron 1By similarity
    Metal bindingi113 – 1131Iron 2By 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the hemerythrin family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71E → Q in S57799. 1 PublicationCurated
    Sequence conflicti11 – 111W → Q(PubMed:12743530)Curated
    Sequence conflicti27 – 282KQ → GK in S57799. 1 PublicationCurated
    Sequence conflicti43 – 431D → G AA sequence (PubMed:8223553)Curated
    Sequence conflicti56 – 561F → P in S57799. 1 PublicationCurated
    Sequence conflicti58 – 581D → E(PubMed:12743530)Curated
    Sequence conflicti63 – 631M → L AA sequence (PubMed:8223553)Curated
    Sequence conflicti67 – 671G → A AA sequence (PubMed:8223553)Curated
    Sequence conflicti99 – 991N → D(PubMed:12743530)Curated

    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: October 1, 2014
    This is version 64 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