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NGB_RAT
ID   NGB_RAT                 Reviewed;         151 AA.
AC   Q99JA8; Q8VH38; Q99N62;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Neuroglobin;
GN   Name=Ngb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=11725647;
RA   Zhang C.G., Li L., Deng M.Y., Xie F., Wang C.L., Zhou W.Q., Wang H.Y.,
RA   He F.C.;
RT   "Coding region cDNA sequence cloning of rat neuroglobin gene, its
RT   polymorphism feature and tissue expression profile analysis.";
RL   Yi Chuan Xue Bao 28:997-1001(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11820779; DOI=10.1006/bbrc.2002.6360;
RA   Zhang C.G., Wang C.L., Deng M.Y., Li L., Wang H.Y., Fan M., Xu W.L.,
RA   Meng F.W., Qian L., He F.C.;
RT   "Full-length cDNA cloning of human neuroglobin and tissue expression of rat
RT   neuroglobin.";
RL   Biochem. Biophys. Res. Commun. 290:1411-1419(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Parthasarathy S.N., Parthasarathy L., Parthasarathy R.;
RT   "Molecular cloning and sequencing of rat brain neuroglobin.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RA   Lee H.-M., Greeley G.H., Englander E.W.;
RT   "Rattus norvegicus mRNA for neuroglobin.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-119.
RA   Wang H., Gao X., Wang B., Huang Y., Han J.;
RT   "Rat neuroglobin (NGB) cDNA, partial sequence.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Widely distributed throughout the adult brain,
CC       including cerebral cortex, hippocampus, thalamus, hypothalamus,
CC       olfactory bulb, and cerebellum. {ECO:0000269|PubMed:11820779}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AF333245; AAK15763.1; -; mRNA.
DR   EMBL; AF334379; AAG59898.1; -; mRNA.
DR   EMBL; AY066001; AAL47568.1; -; mRNA.
DR   EMBL; AB056655; BAB39149.1; -; mRNA.
DR   RefSeq; NP_203523.2; NM_033359.3.
DR   AlphaFoldDB; Q99JA8; -.
DR   SMR; Q99JA8; -.
DR   STRING; 10116.ENSRNOP00000016057; -.
DR   PaxDb; Q99JA8; -.
DR   GeneID; 85382; -.
DR   KEGG; rno:85382; -.
DR   UCSC; RGD:621461; rat.
DR   CTD; 58157; -.
DR   RGD; 621461; Ngb.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; Q99JA8; -.
DR   OrthoDB; 1529889at2759; -.
DR   PhylomeDB; Q99JA8; -.
DR   Reactome; R-RNO-8981607; Intracellular oxygen transport.
DR   PRO; PR:Q99JA8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:RGD.
DR   GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR   GO; GO:0015671; P:oxygen transport; ISO:RGD.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IMP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR   GO; GO:0007601; P:visual perception; IMP:RGD.
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_0000053396"
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   CONFLICT        4
FT                   /note="P -> L (in Ref. 4; AAL47568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  16981 MW;  3F3616A0E231CB7D CRC64;
     MERPESELIR QSWRAVSRSP LEHGTVLFSR LFALEPSLLP LFQYNGRQFS SPEDCLSSPE
     FLDHIRKVML VIDAAVTNVE DLSSLEEYLA TLGRKHRAVG VRLSSFSTVG ESLLYMLEKC
     LGPDFTPATR TAWSQLYGAV VQAMSRGWDG E
 
 
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