NGB_DISMA
ID NGB_DISMA Reviewed; 159 AA.
AC P86881; D2EA91;
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:18814305, ECO:0000312|EMBL:CAR57911.1};
OS Dissostichus mawsoni (Antarctic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=36200;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC TISSUE=Retina {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).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAR57911.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-148.
RX PubMed=18814305; DOI=10.1002/iub.138;
RA Cheng C.H., di Prisco G., Verde C.;
RT "The 'icefish paradox.' Which is the task of neuroglobin in Antarctic
RT hemoglobin-less icefish?";
RL IUBMB Life 61:184-188(2009).
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 EMBL; FM204871; CAR57911.1; -; Genomic_DNA.
DR AlphaFoldDB; P86881; -.
DR SMR; P86881; -.
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_0000419966"
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; 17669 MW; 70E696FC1C10A98E CRC64;
MEKLSEKDKE LIRGSWESLG KNKVPHGVVM FSRLFELDPE LLTLFHYTTN CGSTQDCLSS
PEFLEHVTKV MLVIDAAVSN LDDLPSLEDF LLNLGRKHQA VGVNTQSFAE VGESLLHMLQ
CSLGQAYTAP LRQAWLNLYS IVVAAMSQGW AKNGEDKAD
