ID   NGB_RABIT               Reviewed;         151 AA.
AC   Q6EV97;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Neuroglobin;
GN   Name=NGB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=15793311; DOI=10.1074/jbc.m501338200;
RA   Bentmann A., Schmidt M., Reuss S., Wolfrum U., Hankeln T., Burmester T.;
RT   "Divergent distribution in vascular and avascular mammalian retinae links
RT   neuroglobin to cellular respiration.";
RL   J. Biol. Chem. 280:20660-20665(2005).
CC   -!- FUNCTION: Involved in oxygen transport in the brain. Hexacoordinate
CC       globin, displaying competitive binding of oxygen or the distal His
CC       residue to the iron atom. Not capable of penetrating cell membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer and homotetramer; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AJ781214; CAH03123.1; -; mRNA.
DR   RefSeq; NP_001075602.1; NM_001082133.2.
DR   AlphaFoldDB; Q6EV97; -.
DR   SMR; Q6EV97; -.
DR   STRING; 9986.ENSOCUP00000004997; -.
DR   GeneID; 100008868; -.
DR   KEGG; ocu:100008868; -.
DR   CTD; 58157; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; Q6EV97; -.
DR   OrthoDB; 1529889at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Heme; Iron; Metal-binding; Oxygen transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..151
FT                   /note="Neuroglobin"
FT                   /id="PRO_0000240277"
FT   REGION          1..149
FT                   /note="Globin"
FT   BINDING         64
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         96
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   DISULFID        46..55
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  17040 MW;  A0DBA9CAB5EF9F2D CRC64;
     MERPEQELIR QSWRAVSRSP LEHGTVLFAR LFDLEPDLLP LFQYNCRQFS SPEDCLSSPE
     FLDHIRKVML VIDAAVTNVE DLSSLEEYLA GLGRKHRAVG VRFSSFSTVG ESLLYMLEKC
     LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E