ID   NGB_CHAAC               Reviewed;         159 AA.
AC   P86880;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Neuroglobin {ECO:0000303|PubMed:21445852};
OS   Chaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Chaenocephalus.
OX   NCBI_TaxID=36190;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC   TISSUE=Brain {ECO:0000269|PubMed:21445852};
RX   PubMed=21445852; DOI=10.1002/iub.444;
RA   Boron I., Russo R., Boechi L., Cheng C.H., di Prisco G., Estrin D.A.,
RA   Verde C., Nadra A.D.;
RT   "Structure and dynamics of Antarctic fish neuroglobin assessed by computer
RT   simulations.";
RL   IUBMB Life 63:206-213(2011).
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. Capable of penetrating cell membranes (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NPG2}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NPG2}.
CC   -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q90YJ2}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q90YJ2}. Note=Located in the soma
CC       (perikaryon) of most nerve cells in brain. Has ability to penetrate
CC       cell membranes and translocate into cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q90YJ2}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P86880; -.
DR   SMR; P86880; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm; Disulfide bond; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..159
FT                   /note="Neuroglobin"
FT                   /id="PRO_0000419965"
FT   REGION          4..153
FT                   /note="Globin"
FT                   /evidence="ECO:0000255"
FT   BINDING         66
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:0000250|UniProtKB:Q9NPG2,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         98
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:0000250|UniProtKB:Q9NPG2,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   DISULFID        51..57
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPG2"
SQ   SEQUENCE   159 AA;  17718 MW;  BF1DA666F375A989 CRC64;
     MEKLSEKDKE LIRGSWESLG KNKVPHGVVM FSRLFELDPE LLTLFHYTTN CGSTQDCLSS
     PEFLEHVTKV MLVIDAAVSH LDDLPSLEDF LLNLGRKHQA VGVNTQSFAE VGESLLYMLQ
     CSLGQAYTAP LRQAWLNLYS IVVAAMSQGW AKNGEDKAD