ID   NGB_HUMAN      STANDARD;      PRT;   151 AA.
AC   Q9NPG2;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   18-APR-2006, entry version 34.
DE   Neuroglobin.
GN   Name=NGB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20479975; 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 [MRNA].
RX   MEDLINE=21678907; 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
RT   of rat neuroglobin.";
RL   Biochem. Biophys. Res. Commun. 290:1411-1419(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22459283; PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [5]
RP   CHARACTERIZATION.
RX   MEDLINE=21486399; PubMed=11473128; DOI=10.1074/jbc.M106438200;
RA   Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V.,
RA   Aerts T., Marden M.C., Caubergs R., Moens L.;
RT   "Biochemical characterization and ligand binding properties of
RT   neuroglobin, a novel member of the globin family.";
RL   J. Biol. Chem. 276:38949-38955(2001).
RN   [6]
RP   DISULFIDE BOND.
RX   PubMed=15036292; DOI=10.1016/j.micron.2003.10.019;
RA   Hamdane D., Kiger L., Dewilde S., Green B.N., Pesce A., Uzan J.,
RA   Burmester T., Hankeln T., Bolognesi M., Moens L., Marden M.C.;
RT   "Coupling of the heme and an internal disulfide bond in human
RT   neuroglobin.";
RL   Micron 35:59-62(2004).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   MEDLINE=22238041; PubMed=12351835; DOI=10.1107/S090744490201260X;
RA   Pesce A., Nardini M., Dewilde S., Ascenzi P., Burmester T.,
RA   Hankeln T., Moens L., Bolognesi M.;
RT   "Human neuroglobin: crystals and preliminary X-ray diffraction
RT   analysis.";
RL   Acta Crystallogr. D 58:1848-1850(2002).
CC   -!- FUNCTION: Involved in oxygen transport in the brain.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain, the
CC       strongest expression is seen in the frontal lobe, the subthalamic
CC       nucleus and the thalamus.
CC   -!- SIMILARITY: Belongs to the globin family.
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DR   EMBL; AJ245944; CAC12994.1; -; Genomic_DNA.
DR   EMBL; AJ245946; CAC11133.1; -; mRNA.
DR   EMBL; AF422796; AAL98923.1; -; Genomic_DNA.
DR   EMBL; AF422797; AAL98924.1; -; mRNA.
DR   EMBL; AC007375; AAF63183.1; -; Genomic_DNA.
DR   EMBL; AC007954; AAF62557.1; -; Genomic_DNA.
DR   EMBL; BC032509; AAH32509.1; -; mRNA.
DR   UniGene; Hs.274363; -.
DR   PDB; 1OJ6; X-ray; A/B/C/D=1-151.
DR   Ensembl; ENSG00000165553; Homo sapiens.
DR   HGNC; HGNC:14077; NGB.
DR   MIM; 605304; gene.
DR   GO; GO:0005833; C:hemoglobin complex; NAS.
DR   GO; GO:0005344; F:oxygen transporter activity; TAS.
DR   GO; GO:0015671; P:oxygen transport; NAS.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   InterPro; IPR013316; Globin_worm.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR01907; WORMGLOBIN.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   3D-structure; Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   CHAIN         1    151       Neuroglobin.
FT                                /FTId=PRO_0000053390.
FT   REGION        1    149       Globin.
FT   METAL        64     64       Iron (heme distal ligand) (By
FT                                similarity).
FT   METAL        96     96       Iron (heme proximal ligand) (By
FT                                similarity).
FT   DISULFID     46     55
FT   HELIX         6     17
FT   TURN         18     18
FT   STRAND       19     19
FT   HELIX        20     34
FT   HELIX        36     41
FT   STRAND       45     46
FT   STRAND       50     51
FT   HELIX        52     55
FT   TURN         56     57
FT   HELIX        59     77
FT   TURN         78     80
FT   HELIX        82     98
FT   TURN         99    100
FT   TURN        103    104
FT   HELIX       105    124
FT   STRAND      125    125
FT   HELIX       127    147
SQ   SEQUENCE   151 AA;  16933 MW;  45A292A7D77B9CE3 CRC64;
     MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE
     FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC
     LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E
//