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CYGB_MOUSE
ID   CYGB_MOUSE              Reviewed;         190 AA.
AC   Q9CX80;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Cytoglobin;
DE   AltName: Full=Histoglobin;
DE            Short=HGb;
GN   Name=Cygb;
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=11919282; DOI=10.1093/oxfordjournals.molbev.a004096;
RA   Burmester T., Ebner B., Weich B., Hankeln T.;
RT   "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate
RT   tissues.";
RL   Mol. Biol. Evol. 19:416-421(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May have a protective function during conditions of oxidative
CC       stress. May be involved in intracellular oxygen storage or transfer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AJ315163; CAC86187.1; -; mRNA.
DR   EMBL; AK019410; BAB31709.1; -; mRNA.
DR   EMBL; BC055040; AAH55040.1; -; mRNA.
DR   CCDS; CCDS25673.1; -.
DR   RefSeq; NP_084482.1; NM_030206.4.
DR   AlphaFoldDB; Q9CX80; -.
DR   SMR; Q9CX80; -.
DR   BioGRID; 227897; 4.
DR   STRING; 10090.ENSMUSP00000021166; -.
DR   iPTMnet; Q9CX80; -.
DR   PhosphoSitePlus; Q9CX80; -.
DR   MaxQB; Q9CX80; -.
DR   PaxDb; Q9CX80; -.
DR   PRIDE; Q9CX80; -.
DR   ProteomicsDB; 277936; -.
DR   Antibodypedia; 2901; 326 antibodies from 32 providers.
DR   DNASU; 114886; -.
DR   Ensembl; ENSMUST00000021166; ENSMUSP00000021166; ENSMUSG00000020810.
DR   GeneID; 114886; -.
DR   KEGG; mmu:114886; -.
DR   UCSC; uc007mlv.1; mouse.
DR   CTD; 114757; -.
DR   MGI; MGI:2149481; Cygb.
DR   VEuPathDB; HostDB:ENSMUSG00000020810; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000155004; -.
DR   HOGENOM; CLU_003827_10_1_1; -.
DR   InParanoid; Q9CX80; -.
DR   OMA; ETQRAWT; -.
DR   OrthoDB; 1379813at2759; -.
DR   PhylomeDB; Q9CX80; -.
DR   TreeFam; TF332967; -.
DR   Reactome; R-MMU-203615; eNOS activation.
DR   Reactome; R-MMU-8981607; Intracellular oxygen transport.
DR   BioGRID-ORCS; 114886; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Cygb; mouse.
DR   PRO; PR:Q9CX80; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9CX80; protein.
DR   Bgee; ENSMUSG00000020810; Expressed in interventricular septum and 237 other tissues.
DR   ExpressionAtlas; Q9CX80; baseline and differential.
DR   Genevisible; Q9CX80; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0004096; F:catalase activity; ISO:MGI.
DR   GO; GO:0047888; F:fatty acid peroxidase activity; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; ISO:MGI.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; ISO:MGI.
DR   GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR013314; Globin_lamprey/hagfish.
DR   PANTHER; PTHR46783; PTHR46783; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR01906; FISHGLOBIN.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Heme; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..190
FT                   /note="Cytoglobin"
FT                   /id="PRO_0000053385"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          17..167
FT                   /note="Globin"
FT   BINDING         81
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         113
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"
SQ   SEQUENCE   190 AA;  21466 MW;  6B1A50403F790FF7 CRC64;
     MEKVPGDMEI ERRERSEELS EAERKAVQAT WARLYANCED VGVAILVRFF VNFPSAKQYF
     SQFRHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE
     PMYFKILSGV ILEVIAEEFA NDFPVETQKA WAKLRGLIYS HVTAAYKEVG WVQQVPNTTT
     PPATLPSSGP
 
 
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