Документ взят из кэша поисковой машины. Адрес оригинального документа : http://kodomo.cmm.msu.ru/~mikhail88/term2/psiblast.files/NGB_HUMAN.txt Дата изменения: Mon May 8 10:36:52 2006 Дата индексирования: Sat Dec 22 07:10:29 2007 Кодировка:

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
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