NGB_MOUSE
ID NGB_MOUSE Reviewed; 151 AA.
AC Q9ER97;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Neuroglobin;
GN Name=Ngb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11029004; DOI=10.1038/35035093;
RA Burmester T., Weich B., Reinhardt S., Hankeln T.;
RT "A vertebrate globin expressed in the brain.";
RL Nature 407:520-522(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=11473111; DOI=10.1074/jbc.m103907200;
RA Couture M., Burmester T., Hankeln T., Rousseau D.L.;
RT "The heme environment of mouse neuroglobin. Evidence for the presence of
RT two conformations of the heme pocket.";
RL J. Biol. Chem. 276:36377-36382(2001).
RN [4]
RP FUNCTION, QUATERNARY STRUCTURE, AND MUTAGENESIS OF HIS-64.
RX PubMed=11473128; DOI=10.1074/jbc.m106438200;
RA Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T.,
RA Marden M.C., Caubergs R., Moens L.;
RT "Biochemical characterization and ligand binding properties of neuroglobin,
RT a novel member of the globin family.";
RL J. Biol. Chem. 276:38949-38955(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=22659017; DOI=10.1016/j.neuroscience.2012.05.054;
RA Yu Z., Xu J., Liu N., Wang Y., Li X., Pallast S., van Leyen K., Wang X.;
RT "Mitochondrial distribution of neuroglobin and its response to oxygen-
RT glucose deprivation in primary-cultured mouse cortical neurons.";
RL Neuroscience 218:235-242(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CARBON MONOXIDE AND
RP HEME.
RX PubMed=15548613; DOI=10.1073/pnas.0407633101;
RA Vallone B., Nienhaus K., Matthes A., Brunori M., Nienhaus G.U.;
RT "The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism
RT for control of ligand affinity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17351-17356(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN A HEXACOORDINATED FE(3+)-BOUND
RP FORM.
RX PubMed=15162488; DOI=10.1002/prot.20113;
RA Vallone B., Nienhaus K., Brunori M., Nienhaus G.U.;
RT "The structure of murine neuroglobin: Novel pathways for ligand migration
RT and binding.";
RL Proteins 56:85-92(2004).
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.
CC The deoxygenated form exhibits nitrite reductase activity inhibiting
CC cellular respiration via NO-binding to cytochrome c oxidase. Involved
CC in neuroprotection during oxidative stress. May exert its anti-
CC apoptotic activity by acting to reset the trigger level of
CC mitochondrial cytochrome c release necessary to commit the cells to
CC apoptosis. {ECO:0000269|PubMed:11473111, ECO:0000269|PubMed:11473128}.
CC -!- SUBUNIT: Monomer. Homodimer and homotetramer; disulfide-linked
CC (Probable). Interacts with 14-3-3 (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:22659017}. Mitochondrion
CC {ECO:0000269|PubMed:22659017}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC -!- PTM: A redox disulfide bond regulates the heme pocket coordination and
CC the rate of nitrite reduction to NO. {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during
CC hypoxia. Phosphorylation increases nitrite reductase activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ245945; CAC11135.1; -; mRNA.
DR EMBL; BC024263; AAH24263.1; -; mRNA.
DR CCDS; CCDS36501.1; -.
DR RefSeq; NP_071859.1; NM_022414.2.
DR PDB; 1Q1F; X-ray; 1.50 A; A=1-151.
DR PDB; 1W92; X-ray; 1.70 A; A=1-151.
DR PDB; 2VRY; X-ray; 1.87 A; A=1-151.
DR PDB; 3GK9; X-ray; 1.80 A; A=1-151.
DR PDB; 3GKT; X-ray; 1.86 A; A=1-151.
DR PDB; 3GLN; X-ray; 2.26 A; A=1-151.
DR PDB; 4MU5; X-ray; 1.80 A; A=1-151.
DR PDB; 4NZI; X-ray; 2.10 A; A=1-151.
DR PDB; 4O1T; X-ray; 1.60 A; A=1-151.
DR PDB; 4O2G; X-ray; 2.70 A; A=1-151.
DR PDB; 4O35; X-ray; 1.80 A; A=1-151.
DR PDB; 4O4T; X-ray; 1.90 A; A=1-151.
DR PDB; 4O4Z; X-ray; 1.70 A; A=1-151.
DR PDB; 5EET; X-ray; 2.00 A; A=3-150.
DR PDB; 5EOH; X-ray; 1.90 A; A=3-150.
DR PDB; 5EQM; X-ray; 2.05 A; A=3-150.
DR PDB; 5EU2; X-ray; 2.00 A; A=3-150.
DR PDB; 5EV5; X-ray; 2.00 A; A=3-150.
DR PDB; 5EYJ; X-ray; 2.40 A; A=3-150.
DR PDB; 5EYS; X-ray; 1.75 A; A=3-150.
DR PDB; 5F0B; X-ray; 2.15 A; A=3-151.
DR PDB; 5F2A; X-ray; 2.10 A; A=1-151.
DR PDB; 5MJC; X-ray; 1.62 A; A=3-150.
DR PDB; 5MJD; X-ray; 1.70 A; A=3-150.
DR PDB; 5NVI; X-ray; 1.60 A; A=3-150.
DR PDB; 5NW6; X-ray; 1.70 A; A=3-150.
DR PDB; 5O17; X-ray; 1.80 A; A=3-150.
DR PDB; 5O18; X-ray; 1.86 A; A=3-150.
DR PDB; 5O1K; X-ray; 2.05 A; A=3-150.
DR PDB; 5O27; X-ray; 2.31 A; A=3-150.
DR PDB; 6EYE; X-ray; 1.70 A; A=1-151.
DR PDB; 6H5Z; X-ray; 1.80 A; A=4-149.
DR PDB; 6H6C; X-ray; 1.75 A; A=1-151.
DR PDB; 6H6I; X-ray; 1.60 A; A=1-151.
DR PDB; 6H6J; X-ray; 2.60 A; A=1-150.
DR PDB; 6I3T; X-ray; 2.00 A; A=1-150.
DR PDB; 6I40; X-ray; 1.90 A; A=1-150.
DR PDB; 6R1Q; X-ray; 1.95 A; A=3-150.
DR PDB; 6RA6; X-ray; 2.30 A; A=1-148.
DR PDBsum; 1Q1F; -.
DR PDBsum; 1W92; -.
DR PDBsum; 2VRY; -.
DR PDBsum; 3GK9; -.
DR PDBsum; 3GKT; -.
DR PDBsum; 3GLN; -.
DR PDBsum; 4MU5; -.
DR PDBsum; 4NZI; -.
DR PDBsum; 4O1T; -.
DR PDBsum; 4O2G; -.
DR PDBsum; 4O35; -.
DR PDBsum; 4O4T; -.
DR PDBsum; 4O4Z; -.
DR PDBsum; 5EET; -.
DR PDBsum; 5EOH; -.
DR PDBsum; 5EQM; -.
DR PDBsum; 5EU2; -.
DR PDBsum; 5EV5; -.
DR PDBsum; 5EYJ; -.
DR PDBsum; 5EYS; -.
DR PDBsum; 5F0B; -.
DR PDBsum; 5F2A; -.
DR PDBsum; 5MJC; -.
DR PDBsum; 5MJD; -.
DR PDBsum; 5NVI; -.
DR PDBsum; 5NW6; -.
DR PDBsum; 5O17; -.
DR PDBsum; 5O18; -.
DR PDBsum; 5O1K; -.
DR PDBsum; 5O27; -.
DR PDBsum; 6EYE; -.
DR PDBsum; 6H5Z; -.
DR PDBsum; 6H6C; -.
DR PDBsum; 6H6I; -.
DR PDBsum; 6H6J; -.
DR PDBsum; 6I3T; -.
DR PDBsum; 6I40; -.
DR PDBsum; 6R1Q; -.
DR PDBsum; 6RA6; -.
DR AlphaFoldDB; Q9ER97; -.
DR BMRB; Q9ER97; -.
DR SMR; Q9ER97; -.
DR BioGRID; 211041; 4.
DR STRING; 10090.ENSMUSP00000021420; -.
DR PaxDb; Q9ER97; -.
DR PRIDE; Q9ER97; -.
DR ProteomicsDB; 287505; -.
DR Antibodypedia; 25998; 301 antibodies from 30 providers.
DR DNASU; 64242; -.
DR Ensembl; ENSMUST00000021420; ENSMUSP00000021420; ENSMUSG00000021032.
DR GeneID; 64242; -.
DR KEGG; mmu:64242; -.
DR UCSC; uc007oii.1; mouse.
DR CTD; 58157; -.
DR MGI; MGI:2151886; Ngb.
DR VEuPathDB; HostDB:ENSMUSG00000021032; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00510000048375; -.
DR HOGENOM; CLU_003827_13_5_1; -.
DR InParanoid; Q9ER97; -.
DR OMA; MQRGWET; -.
DR PhylomeDB; Q9ER97; -.
DR TreeFam; TF333247; -.
DR Reactome; R-MMU-8981607; Intracellular oxygen transport.
DR BioGRID-ORCS; 64242; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Gtpbp4; mouse.
DR EvolutionaryTrace; Q9ER97; -.
DR PRO; PR:Q9ER97; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ER97; protein.
DR Bgee; ENSMUSG00000021032; Expressed in interventricular septum and 60 other tissues.
DR ExpressionAtlas; Q9ER97; baseline and differential.
DR Genevisible; Q9ER97; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0015671; P:oxygen transport; IDA:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Disulfide bond; Heme; Iron;
KW Metal-binding; Mitochondrion; Oxygen transport; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..151
FT /note="Neuroglobin"
FT /id="PRO_0000053392"
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:0000269|PubMed:15162488,
FT ECO:0007744|PDB:1Q1F, ECO:0007744|PDB:2VRY,
FT ECO:0007744|PDB:3GK9, ECO:0007744|PDB:3GKT,
FT ECO:0007744|PDB:3GLN, ECO:0007744|PDB:4MU5,
FT ECO:0007744|PDB:4NZI, ECO:0007744|PDB:4O1T,
FT ECO:0007744|PDB:4O4T, ECO:0007744|PDB:4O4Z"
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:0000269|PubMed:15162488,
FT ECO:0000269|PubMed:15548613, ECO:0007744|PDB:1Q1F,
FT ECO:0007744|PDB:1W92, ECO:0007744|PDB:2VRY,
FT ECO:0007744|PDB:3GK9, ECO:0007744|PDB:3GKT,
FT ECO:0007744|PDB:3GLN, ECO:0007744|PDB:4MU5,
FT ECO:0007744|PDB:4NZI, ECO:0007744|PDB:4O1T,
FT ECO:0007744|PDB:4O2G, ECO:0007744|PDB:4O35,
FT ECO:0007744|PDB:4O4T, ECO:0007744|PDB:4O4Z"
FT MUTAGEN 64
FT /note="H->L: Improved binding of dioxygen and carbon
FT monoxide to the iron atom."
FT /evidence="ECO:0000269|PubMed:11473128"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4O1T"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:1Q1F"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4O1T"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:1Q1F"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1Q1F"
SQ SEQUENCE 151 AA; 17037 MW; 377BBE4BF723CCF1 CRC64;
MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS SPEDCLSSPE
FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG VRLSSFSTVG ESLLYMLEKC
LGPDFTPATR TAWSRLYGAV VQAMSRGWDG E
