ID CYGB_HUMAN Reviewed; 190 AA. AC Q8WWM9; Q541Y7; Q8N2X5; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 175. DE RecName: Full=Cytoglobin {ECO:0000303|PubMed:11919282}; DE AltName: Full=Histoglobin {ECO:0000303|PubMed:11893755}; DE Short=HGb {ECO:0000303|PubMed:11893755}; DE AltName: Full=Nitric oxygen dioxygenase CYGB {ECO:0000305|PubMed:20511233}; DE Short=NOD {ECO:0000303|PubMed:20511233}; DE EC=1.14.12.- {ECO:0000269|PubMed:20511233}; DE AltName: Full=Nitrite reductase CYGB {ECO:0000305|PubMed:29128400}; DE EC=1.7.-.- {ECO:0000269|PubMed:29128400}; DE AltName: Full=Pseudoperoxidase CYGB {ECO:0000305|PubMed:12359339}; DE EC=1.11.1.- {ECO:0000269|PubMed:12359339}; DE AltName: Full=Stellate cell activation-associated protein {ECO:0000303|PubMed:12359339}; DE AltName: Full=Superoxide dismutase CYGB {ECO:0000305|PubMed:34930834}; DE EC=1.15.1.1 {ECO:0000269|PubMed:34930834}; GN Name=CYGB {ECO:0000312|HGNC:HGNC:16505}; GN Synonyms=STAP {ECO:0000303|PubMed:12359339}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. 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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Heart; RX PubMed=12359339; DOI=10.1016/s0167-4781(02)00477-3; RA Asahina K., Kawada N., Kristensen D.B., Nakatani K., Seki S., Shiokawa M., RA Tateno C., Obara M., Yoshizato K.; RT "Characterization of human stellate cell activation-associated protein and RT its expression in human liver."; RL Biochim. Biophys. Acta 1577:471-475(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11893755; DOI=10.1074/jbc.m201934200; RA Trent J.T. III, Hargrove M.S.; RT "A ubiquitously expressed human hexacoordinate hemoglobin."; RL J. Biol. Chem. 277:19538-19545(2002). RN [7] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=14660570; DOI=10.1074/jbc.m310540200; RA Schmidt M., Gerlach F., Avivi A., Laufs T., Wystub S., Simpson J.C., RA Nevo E., Saaler-Reinhardt S., Reuss S., Hankeln T., Burmester T.; RT "Cytoglobin is a respiratory protein in connective tissue and neurons, RT which is up-regulated by hypoxia."; RL J. Biol. Chem. 279:8063-8069(2004). RN [8] RP FUNCTION. RX PubMed=15299006; DOI=10.1074/jbc.m407126200; RA Fago A., Hundahl C., Dewilde S., Gilany K., Moens L., Weber R.E.; RT "Allosteric regulation and temperature dependence of oxygen binding in RT human neuroglobin and cytoglobin. Molecular mechanisms and physiological RT significance."; RL J. Biol. Chem. 279:44417-44426(2004). RN [9] RP FUNCTION. RX PubMed=19147491; DOI=10.1074/jbc.m808231200; RA Halligan K.E., Jourd'heuil F.L., Jourd'heuil D.; RT "Cytoglobin is expressed in the vasculature and regulates cell respiration RT and proliferation via nitric oxide dioxygenation."; RL J. Biol. Chem. 284:8539-8547(2009). RN [10] RP FUNCTION, SUBUNIT, AND DISULFIDE BOND. RX PubMed=20553503; DOI=10.1111/j.1742-464x.2010.07686.x; RA Lechauve C., Chauvierre C., Dewilde S., Moens L., Green B.N., Marden M.C., RA Celier C., Kiger L.; RT "Cytoglobin conformations and disulfide bond formation."; RL FEBS J. 277:2696-2704(2010). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20511233; DOI=10.1074/jbc.m110.132340; RA Gardner A.M., Cook M.R., Gardner P.R.; RT "Nitric-oxide dioxygenase function of human cytoglobin with cellular RT reductants and in rat hepatocytes."; RL J. Biol. Chem. 285:23850-23857(2010). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=28671819; DOI=10.1021/acs.biochem.7b00224; RA Amdahl M.B., Sparacino-Watkins C.E., Corti P., Gladwin M.T., Tejero J.; RT "Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome RT b5/Cytochrome b5 Reductase/NADH System."; RL Biochemistry 56:3993-4004(2017). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28393874; DOI=10.1038/ncomms14807; RA Liu X., El-Mahdy M.A., Boslett J., Varadharaj S., Hemann C., RA Abdelghany T.M., Ismail R.S., Little S.C., Zhou D., Thuy L.T., Kawada N., RA Zweier J.L.; RT "Cytoglobin regulates blood pressure and vascular tone through nitric oxide RT metabolism in the vascular wall."; RL Nat. Commun. 8:14807-14807(2017). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, AND MUTAGENESIS OF CYS-38 AND RP CYS-83. RX PubMed=29128400; DOI=10.1016/j.niox.2017.11.004; RA Reeder B.J., Ukeri J.; RT "Strong modulation of nitrite reductase activity of cytoglobin by disulfide RT bond oxidation: Implications for nitric oxide homeostasis."; RL Nitric Oxide 72:16-23(2018). RN [15] RP FUNCTION. RX PubMed=33576020; DOI=10.1002/hep.31752; RA Dat N.Q., Thuy L.T.T., Hieu V.N., Hai H., Hoang D.V., Thi Thanh Hai N., RA Thuy T.T.V., Komiya T., Rombouts K., Dong M.P., Hanh N.V., Hoang T.H., RA Sato-Matsubara M., Daikoku A., Kadono C., Oikawa D., Yoshizato K., RA Tokunaga F., Pinzani M., Kawada N.; RT "Hexa Histidine-Tagged Recombinant Human Cytoglobin Deactivates Hepatic RT Stellate Cells and Inhibits Liver Fibrosis by Scavenging Reactive Oxygen RT Species."; RL Hepatology 73:2527-2545(2021). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=34930834; DOI=10.1073/pnas.2105053118; RA Zweier J.L., Hemann C., Kundu T., Ewees M.G., Khaleel S.A., Samouilov A., RA Ilangovan G., El-Mahdy M.A.; RT "Cytoglobin has potent superoxide dismutase function."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [17] {ECO:0007744|PDB:1URY, ECO:0007744|PDB:1UX9} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT SER-38 AND SER-83, AND RP SUBUNIT. RX PubMed=15044115; DOI=10.1016/j.bbrc.2004.03.007; RA de Sanctis D., Dewilde S., Pesce A., Moens L., Ascenzi P., Hankeln T., RA Burmester T., Bolognesi M.; RT "Mapping protein matrix cavities in human cytoglobin through Xe atom RT binding."; RL Biochem. Biophys. Res. Commun. 316:1217-1221(2004). RN [18] {ECO:0007744|PDB:1UMO, ECO:0007744|PDB:1URV, ECO:0007744|PDB:1UT0} RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT SER-38 AND SER-83, SUBUNIT, RP AND MUTAGENESIS OF CYS-38 AND CYS-83. RX PubMed=15095869; DOI=10.1016/j.jmb.2003.12.063; RA de Sanctis D., Dewilde S., Pesce A., Moens L., Ascenzi P., Hankeln T., RA Burmester T., Bolognesi M.; RT "Crystal structure of cytoglobin: the fourth globin type discovered in man RT displays heme hexa-coordination."; RL J. Mol. Biol. 336:917-927(2004). RN [19] {ECO:0007744|PDB:1V5H} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF FERRIC FORM, FUNCTION, SUBUNIT, RP DISULFIDE BOND, AND MUTAGENESIS OF CYS-38 AND CYS-83. RX PubMed=15165856; DOI=10.1016/j.jmb.2004.04.024; RA Sugimoto H., Makino M., Sawai H., Kawada N., Yoshizato K., Shiro Y.; RT "Structural basis of human cytoglobin for ligand binding."; RL J. Mol. Biol. 339:873-885(2004). RN [20] {ECO:0007744|PDB:2DC3} RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS. RX PubMed=16699195; DOI=10.1107/s0907444906013813; RA Makino M., Sugimoto H., Sawai H., Kawada N., Yoshizato K., Shiro Y.; RT "High-resolution structure of human cytoglobin: identification of extra RT N- and C-termini and a new dimerization mode."; RL Acta Crystallogr. D 62:671-677(2006). CC -!- FUNCTION: Probable multifunctional globin with a hexacoordinated heme CC iron required for the catalysis of various reactions depending on redox CC condition of the cell as well as oxygen availability (PubMed:12359339, CC PubMed:11893755, PubMed:19147491, PubMed:20511233, PubMed:28671819, CC PubMed:28393874, PubMed:29128400, PubMed:33576020, PubMed:34930834, CC PubMed:15165856). Has a nitric oxide dioxygenase (NOD) activity and is CC most probably involved in cell-mediated and oxygen-dependent nitric CC oxide consumption (PubMed:19147491, PubMed:20511233, PubMed:28671819, CC PubMed:28393874). By scavenging this second messenger may regulate CC several biological processes including endothelium-mediated CC vasodilation and vascular tone (PubMed:19147491, PubMed:28393874). CC Under normoxic conditions functions as a nitric oxide dioxygenase (NOD) CC but under hypoxic conditions the globin may switch its function to that CC of a nitrite (NO2) reductase (NiR), generating nitric oxide CC (PubMed:29128400). Could also have peroxidase and superoxide dismutase CC activities, detoxifying reactive oxygen species and protecting cells CC against oxidative stress (PubMed:12359339, PubMed:33576020, CC PubMed:34930834). Also binds dioxygen with low affinity and could CC function as an oxygen sensor but has probably no function as a CC respiratory oxygen carrier (PubMed:11893755, PubMed:15299006, CC PubMed:20553503). {ECO:0000269|PubMed:11893755, CC ECO:0000269|PubMed:12359339, ECO:0000269|PubMed:15165856, CC ECO:0000269|PubMed:15299006, ECO:0000269|PubMed:19147491, CC ECO:0000269|PubMed:20511233, ECO:0000269|PubMed:20553503, CC ECO:0000269|PubMed:28393874, ECO:0000269|PubMed:28671819, CC ECO:0000269|PubMed:29128400, ECO:0000269|PubMed:33576020, CC ECO:0000269|PubMed:34930834}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe(II)-heme b-[protein] + nitric oxide + O2 = Fe(III)-heme b- CC [protein] + nitrate; Xref=Rhea:RHEA:78091, Rhea:RHEA-COMP:18975, CC Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, CC ChEBI:CHEBI:17632, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; CC Evidence={ECO:0000269|PubMed:20511233, ECO:0000269|PubMed:28393874, CC ECO:0000269|PubMed:28671819}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78092; CC Evidence={ECO:0000269|PubMed:28393874}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b- CC [protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA- CC COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, CC ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; CC Evidence={ECO:0000269|PubMed:29128400}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; CC Evidence={ECO:0000305|PubMed:29128400}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:18421; EC=1.15.1.1; CC Evidence={ECO:0000269|PubMed:34930834}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697; CC Evidence={ECO:0000269|PubMed:34930834}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:17499; Evidence={ECO:0000305|PubMed:12359339}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30276; CC Evidence={ECO:0000305|PubMed:12359339}; CC -!- ACTIVITY REGULATION: The nitric oxide dioxygenase activity is activated CC by a reducing system composed of cytochrome b5, its upstream reductase CC CYB5R3 and NADH. {ECO:0000269|PubMed:28671819}. CC -!- SUBUNIT: Monomeric (PubMed:20553503). Homodimer; disulfide-linked in CC vitro (PubMed:15044115, PubMed:15165856, PubMed:16699195). Also CC homooligomeric in vitro (PubMed:15165856). CC {ECO:0000269|PubMed:15044115, ECO:0000269|PubMed:15165856, CC ECO:0000269|PubMed:16699195, ECO:0000269|PubMed:20553503}. CC -!- INTERACTION: CC Q8WWM9; O43488: AKR7A2; NbExp=3; IntAct=EBI-6309037, EBI-748855; CC Q8WWM9; P85298-4: ARHGAP8; NbExp=3; IntAct=EBI-6309037, EBI-9523517; CC Q8WWM9; Q8WTU0: DDI1; NbExp=6; IntAct=EBI-6309037, EBI-748248; CC Q8WWM9; Q96KN4: LRATD1; NbExp=3; IntAct=EBI-6309037, EBI-11477916; CC Q8WWM9; Q08AG7: MZT1; NbExp=3; IntAct=EBI-6309037, EBI-2637198; CC Q8WWM9; B1AHC3: PRR5-ARHGAP8; NbExp=3; IntAct=EBI-6309037, EBI-17437404; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14660570, CC ECO:0000269|PubMed:34930834}. Nucleus {ECO:0000269|PubMed:14660570}. CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in heart, CC stomach, bladder and small intestine. {ECO:0000269|PubMed:11893755, CC ECO:0000269|PubMed:11919282, ECO:0000269|PubMed:14660570}. CC -!- PTM: The formation of an intramolecular disulfide bond between CC cysteines Cys-38 and Cys-83 specifically enhances the nitrite reductase CC activity. {ECO:0000269|PubMed:29128400}. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ315162; CAC86186.1; -; mRNA. DR EMBL; AB057769; BAB87840.1; -; mRNA. DR EMBL; AK098057; BAC05223.1; -; mRNA. DR EMBL; CH471099; EAW89406.1; -; Genomic_DNA. DR EMBL; BC029798; AAH29798.1; -; mRNA. DR CCDS; CCDS11746.1; -. DR RefSeq; NP_599030.1; NM_134268.4. DR PDB; 1UMO; X-ray; 2.59 A; A/B=1-190. DR PDB; 1URV; X-ray; 2.00 A; A/B=1-190. DR PDB; 1URY; X-ray; 2.40 A; A/B=1-190. DR PDB; 1UT0; X-ray; 2.10 A; A/B=1-190. DR PDB; 1UX9; X-ray; 2.40 A; A/B=1-190. DR PDB; 1V5H; X-ray; 2.40 A; A=1-190. DR PDB; 2DC3; X-ray; 1.68 A; A/B=1-190. DR PDB; 3AG0; X-ray; 2.60 A; A=1-190. DR PDB; 4B3W; X-ray; 2.80 A; A/B=1-190. DR PDBsum; 1UMO; -. DR PDBsum; 1URV; -. DR PDBsum; 1URY; -. DR PDBsum; 1UT0; -. DR PDBsum; 1UX9; -. DR PDBsum; 1V5H; -. DR PDBsum; 2DC3; -. DR PDBsum; 3AG0; -. DR PDBsum; 4B3W; -. DR AlphaFoldDB; Q8WWM9; -. DR SMR; Q8WWM9; -. DR BioGRID; 125335; 12. DR IntAct; Q8WWM9; 11. DR STRING; 9606.ENSP00000293230; -. DR TCDB; 1.A.107.1.5; the pore-forming globin (globin) family. DR iPTMnet; Q8WWM9; -. DR PhosphoSitePlus; Q8WWM9; -. DR BioMuta; CYGB; -. DR DMDM; 21263504; -. DR jPOST; Q8WWM9; -. DR MassIVE; Q8WWM9; -. DR MaxQB; Q8WWM9; -. DR PaxDb; 9606-ENSP00000293230; -. DR PeptideAtlas; Q8WWM9; -. DR ProteomicsDB; 74913; -. DR Antibodypedia; 2901; 366 antibodies from 32 providers. DR DNASU; 114757; -. DR Ensembl; ENST00000293230.10; ENSP00000293230.4; ENSG00000161544.10. DR GeneID; 114757; -. DR KEGG; hsa:114757; -. DR MANE-Select; ENST00000293230.10; ENSP00000293230.4; NM_134268.5; NP_599030.1. DR UCSC; uc002jru.3; human. DR AGR; HGNC:16505; -. DR CTD; 114757; -. DR DisGeNET; 114757; -. DR GeneCards; CYGB; -. DR HGNC; HGNC:16505; CYGB. DR HPA; ENSG00000161544; Tissue enhanced (heart). DR MalaCards; CYGB; -. DR MIM; 608759; gene. DR neXtProt; NX_Q8WWM9; -. DR OpenTargets; ENSG00000161544; -. DR PharmGKB; PA27080; -. DR VEuPathDB; HostDB:ENSG00000161544; -. DR eggNOG; KOG3378; Eukaryota. DR GeneTree; ENSGT00940000155004; -. DR HOGENOM; CLU_003827_10_1_1; -. DR InParanoid; Q8WWM9; -. DR OMA; ETQRAWT; -. DR OrthoDB; 5347904at2759; -. DR PhylomeDB; Q8WWM9; -. DR TreeFam; TF332967; -. DR PathwayCommons; Q8WWM9; -. DR Reactome; R-HSA-203615; eNOS activation. DR Reactome; R-HSA-8981607; Intracellular oxygen transport. DR SignaLink; Q8WWM9; -. DR SIGNOR; Q8WWM9; -. DR BioGRID-ORCS; 114757; 11 hits in 1145 CRISPR screens. DR ChiTaRS; CYGB; human. DR EvolutionaryTrace; Q8WWM9; -. DR GeneWiki; Cytoglobin; -. DR GenomeRNAi; 114757; -. DR Pharos; Q8WWM9; Tbio. DR PRO; PR:Q8WWM9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8WWM9; Protein. DR Bgee; ENSG00000161544; Expressed in cardiac muscle of right atrium and 151 other cell types or tissues. DR ExpressionAtlas; Q8WWM9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0070025; F:carbon monoxide binding; IDA:UniProtKB. DR GO; GO:0004096; F:catalase activity; IEA:Ensembl. DR GO; GO:0047888; F:fatty acid peroxidase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0098809; F:nitrite reductase activity; IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0016675; F:oxidoreductase activity, acting on a heme group of donors; IDA:UniProtKB. DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB. DR GO; GO:0005344; F:oxygen carrier activity; NAS:UniProtKB. DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB. DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl. DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl. DR GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; IEA:Ensembl. DR GO; GO:0046210; P:nitric oxide catabolic process; IDA:UniProtKB. DR GO; GO:0015671; P:oxygen transport; NAS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; IDA:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB. DR CDD; cd08924; Cygb; 1. DR Gene3D; 1.10.490.10; Globins; 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; CYTOGLOBIN; 1. DR PANTHER; PTHR46783:SF1; CYTOGLOBIN; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR01906; FISHGLOBIN. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. DR Genevisible; Q8WWM9; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Disulfide bond; Heme; Iron; Metal-binding; KW Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1..190 FT /note="Cytoglobin" FT /id="PRO_0000053384" 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 ECO:0000269|PubMed:15044115, ECO:0000269|PubMed:15095869, FT ECO:0000269|PubMed:15165856, ECO:0000269|PubMed:16699195, FT ECO:0007744|PDB:1URV, ECO:0007744|PDB:1URY, FT ECO:0007744|PDB:1UT0, ECO:0007744|PDB:1UX9, FT ECO:0007744|PDB:1V5H, ECO:0007744|PDB:2DC3" 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, FT ECO:0000269|PubMed:15044115, ECO:0000269|PubMed:15095869, FT ECO:0000269|PubMed:15165856, ECO:0000269|PubMed:16699195, FT ECO:0007744|PDB:1UMO, ECO:0007744|PDB:1URV, FT ECO:0007744|PDB:1URY, ECO:0007744|PDB:1UT0, FT ECO:0007744|PDB:1UX9, ECO:0007744|PDB:1V5H, FT ECO:0007744|PDB:2DC3" FT DISULFID 38..83 FT /note="Redox-active; in monomeric form" FT /evidence="ECO:0000269|PubMed:16699195, FT ECO:0007744|PDB:2DC3" FT DISULFID 38 FT /note="Interchain (with C-83); in dimeric form" FT /evidence="ECO:0000269|PubMed:16699195, FT ECO:0007744|PDB:2DC3" FT DISULFID 83 FT /note="Interchain (with C-38); in dimeric form" FT /evidence="ECO:0000269|PubMed:16699195, FT ECO:0007744|PDB:2DC3" FT MUTAGEN 38 FT /note="C->R: Decreased nitrite reductase activity; when FT associated with R-83." FT /evidence="ECO:0000269|PubMed:29128400" FT MUTAGEN 38 FT /note="C->S: Loss of interchain disulfide bond and loss of FT solubility but no effect on homodimerization; when FT associated with S-83." FT /evidence="ECO:0000269|PubMed:15095869, FT ECO:0000269|PubMed:15165856" FT MUTAGEN 83 FT /note="C->R: Decreased nitrite reductase activity; when FT associated with R-38." FT /evidence="ECO:0000269|PubMed:29128400" FT MUTAGEN 83 FT /note="C->S: Loss of interchain disulfide bond and loss of FT solubility but no effect on homodimerization; when FT associated with S-38." FT /evidence="ECO:0000269|PubMed:15095869" FT CONFLICT 37 FT /note="N -> S (in Ref. 5; AAH29798)" FT /evidence="ECO:0000305" FT HELIX 7..15 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 21..35 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 38..52 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 54..59 FT /evidence="ECO:0007829|PDB:2DC3" FT TURN 61..65 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 76..94 FT /evidence="ECO:0007829|PDB:2DC3" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 99..115 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 121..138 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:2DC3" FT HELIX 145..168 FT /evidence="ECO:0007829|PDB:2DC3" SQ SEQUENCE 190 AA; 21405 MW; B5D7F9976D0BA118 CRC64; MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYANCED VGVAILVRFF VNFPSAKQYF SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT PPATLPSSGP //