ID   HEMTN_HIRME             Reviewed;         120 AA.
AC   Q674M7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Neurohemerythrin;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-13, INDUCTION, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15258158; DOI=10.1074/jbc.m403073200;
RA   Vergote D., Sautiere P.-E., Vandenbulcke F., Vieau D., Mitta G.,
RA   Macagno E.R., Salzet M.;
RT   "Up-regulation of neurohemerythrin expression in the central nervous system
RT   of the medicinal leech, Hirudo medicinalis, following septic injury.";
RL   J. Biol. Chem. 279:43828-43837(2004).
CC   -!- FUNCTION: May play a role in the innate immune response of the leech
CC       nervous system to bacterial invasion. The oxygen-binding site in each
CC       chain contains two iron atoms (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central nervous system. Detected
CC       in the pair of large glia within the ganglionic neuropile, in the six
CC       packet glia that surround neuronal somata in each central ganglion, and
CC       in the bilateral pair of glia that separate axonal fascicles in the
CC       interganglionic connective nerves (at protein level).
CC       {ECO:0000269|PubMed:15258158}.
CC   -!- INDUCTION: Up-regulated after septic shoc.
CC       {ECO:0000269|PubMed:15258158}.
CC   -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR   EMBL; AY521548; AAS49167.1; -; mRNA.
DR   AlphaFoldDB; Q674M7; -.
DR   SMR; Q674M7; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProt.
DR   CDD; cd12107; Hemerythrin; 1.
DR   Gene3D; 1.20.120.50; -; 1.
DR   InterPro; IPR002063; Haemerythrin.
DR   InterPro; IPR016131; Haemerythrin_Fe_BS.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR035938; Hemerythrin-like_sf.
DR   InterPro; IPR012827; Hemerythrin_metal-bd.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   PIRSF; PIRSF002033; Hemerythrin; 1.
DR   PRINTS; PR00186; HEMERYTHRIN.
DR   SUPFAM; SSF47188; SSF47188; 1.
DR   TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR   TIGRFAMs; TIGR00058; Hemerythrin; 1.
DR   PROSITE; PS00550; HEMERYTHRINS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15258158"
FT   CHAIN           2..120
FT                   /note="Neurohemerythrin"
FT                   /id="PRO_0000343354"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         75
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
SQ   SEQUENCE   120 AA;  13814 MW;  3A017244704FF2A7 CRC64;
     MGFEIPEPYV WDESFKVFYE NLDEEHKGLF QAIFNLSKSP ADNGALKHLS KVIDEHFSHE
     EDMMKKASYS DFDNHKKAHV DFQASLGGLS SPVANDKVHW AKDWLVNHIK GTDFLYKGKL