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Cytoglobin

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(Redirected from CYGB (gene)) Mammalian protein found in Homo sapiens
CYGB
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1UMO, 1URV, 1URY, 1UT0, 1UX9, 1V5H, 2DC3, 3AG0, 4B3W

Identifiers
AliasesCYGB, HGB, STAP, cytoglobin
External IDsOMIM: 608759; MGI: 2149481; HomoloGene: 12706; GeneCards: CYGB; OMA:CYGB - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)
Chromosome 17 (human)Genomic location for CYGBGenomic location for CYGB
Band17q25.1Start76,527,356 bp
End76,551,175 bp
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)
Chromosome 11 (mouse)Genomic location for CYGBGenomic location for CYGB
Band11|11 E2Start116,536,421 bp
End116,545,139 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cardiac muscle tissue of right atrium

  • myocardium of left ventricle

  • right auricle

  • apex of heart

  • subcutaneous adipose tissue

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • gastric mucosa

  • canal of the cervix

  • mucosa of ileum
Top expressed in
  • interventricular septum

  • aortic valve

  • ascending aorta

  • habenula

  • dorsal tegmental nucleus

  • ankle

  • lateral hypothalamus

  • central gray substance of midbrain

  • neural layer of retina

  • medial vestibular nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

114757

114886

Ensembl

ENSG00000161544

ENSMUSG00000020810

UniProt

Q8WWM9

Q9CX80

RefSeq (mRNA)

NM_134268

NM_030206

RefSeq (protein)

NP_599030

NP_084482

Location (UCSC)Chr 17: 76.53 – 76.55 MbChr 11: 116.54 – 116.55 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Cytoglobin is the protein product of CYGB, a human and mammalian gene.

Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001 in hepatic stellate cells during liver fibrosis. Thus, it was originally called "stellate cell activated protein" or STAP. It received its current name in 2002. It is thought to help in the distribution and storage of oxygen as well as protect against hypoxia by scavenging reactive oxygen species . The predicted function of cytoglobin is the facilitation of oxygen among tissues that don't express myoglobin.

Function

Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or reactive oxygen species, or serve a protective function during oxidative stress.

Structure

Cytoglobin has 30-40% sequence homology with myoglobin, and has a similar oxygen binding affinity. One of the major differences is the presence of a 20 amino acids extension at both the n and c terminus.

Cytoglobin is a hexacoordinate heme protein. The heme iron in coordinated with histidine residues on both sides, HisF8 and HisE7. The HisE7 is considered to be an "endogenous ligand." In order for oxygen or another gaseous ligand to bind, the HisE7 must dissociate from the iron, making the binding kinetics relatively slow.

Diagram of how the heme group in cytoglobin interacts with the surrounding amino acids of the globin protein. Normally, the iron is coordinated with histidine residues on both sides. The HisE7 must be dissociated in order for oxygen to bind.

In an oxidizing environment, a disulfide bond between Cys38 and Cys83 of the protein forms and causes a conformational change to move HisE7 out of the way, allowing oxygen to bind. Thus, oxygen binding is dependent on the redox state of the tissue.

Applications

CYGB expression can be used as a specific marker with which hepatic stellate cells can be distinguished from portal myofibroblasts in the damaged human liver.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000161544Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020810Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: CYGB cytoglobin".
  6. Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K (Jul 2001). "Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells". The Journal of Biological Chemistry. 276 (27): 25318–23. doi:10.1074/jbc.M102630200. PMID 11320098.
  7. Pesce, Alessandra; Bolognesi, Martino; Bocedi, Alessio; Ascenzi, Paolo; Dewilde, Sylvia; Moens, Luc; Hankeln, Thomas; Burmester, Thorsten (December 2002). "Neuroglobin and cytoglobin: Fresh blood for the vertebrate globin family". EMBO Reports. 3 (12): 1146–1151. doi:10.1093/embo-reports/kvf248. ISSN 1469-221X. PMC 1308314. PMID 12475928.
  8. Burmester T, Ebner B, Weich B, Hankeln T (Apr 2002). "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues". Molecular Biology and Evolution. 19 (4): 416–21. doi:10.1093/oxfordjournals.molbev.a004096. PMID 11919282.
  9. "Why Diving Marine Mammals Resist Brain Damage from Low Oxygen". ScienceDaily. 20 December 2007.
  10. Trent JT, Hargrove MS (May 2002). "A ubiquitously expressed human hexacoordinate hemoglobin". The Journal of Biological Chemistry. 277 (22): 19538–45. doi:10.1074/jbc.M201934200. PMID 11893755.
  11. ^ Keller, T. C. Stevenson; Lechauve, Christophe; Keller, Alexander S.; Brooks, Steven; Weiss, Mitchell J.; Columbus, Linda; Ackerman, Hans; Cortese-Krott, Miriam M.; Isakson, Brant E. (2022-04-01). "The role of globins in cardiovascular physiology". Physiological Reviews. 102 (2): 859–892. doi:10.1152/physrev.00037.2020. ISSN 0031-9333. PMC 8799389. PMID 34486392.
  12. Hankeln, Thomas; Ebner, Bettina; Fuchs, Christine; Gerlach, Frank; Haberkamp, Mark; Laufs, Tilmann L.; Roesner, Anja; Schmidt, Marc; Weich, Bettina; Wystub, Sylvia; Saaler-Reinhardt, Sigrid; Reuss, Stefan; Bolognesi, Martino; Sanctis, Daniele De; Marden, Michael C. (2005-01-01). "Neuroglobin and cytoglobin in search of their role in the vertebrate globin family". Journal of Inorganic Biochemistry. Heme-diatomic interactions, Part 1. 99 (1): 110–119. doi:10.1016/j.jinorgbio.2004.11.009. ISSN 0162-0134. PMID 15598495.
  13. Motoyama H, Komiya T, Thuy le TT, Tamori A, Enomoto M, Morikawa H, Iwai S, Uchida-Kobayashi S, Fujii H, Hagihara A, Kawamura E, Murakami Y, Yoshizato K, Kawada N (Feb 2014). "Cytoglobin is expressed in hepatic stellate cells, but not in myofibroblasts, in normal and fibrotic human liver". Laboratory Investigation. 94 (2): 192–207. doi:10.1038/labinvest.2013.135. PMID 24296877.

Further reading

External links

PDB gallery
  • 1umo: THE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN 1umo: THE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN
  • 1urv: CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION 1urv: CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION
  • 1ury: CYTOGLOBIN CAVITIES 1ury: CYTOGLOBIN CAVITIES
  • 1ut0: CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION 1ut0: CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION
  • 1ux9: MAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATION 1ux9: MAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATION
  • 1v5h: Crystal Structure of Human Cytoglobin (Ferric Form) 1v5h: Crystal Structure of Human Cytoglobin (Ferric Form)
  • 2dc3: Crystal structure of human cytoglobin at 1.68 angstroms resolution 2dc3: Crystal structure of human cytoglobin at 1.68 angstroms resolution
Proteins that contain heme (hemoproteins)
Globins
Hemoglobin
Subunits
Alpha locus on 16:
Beta locus on 11:
Tetramers
stages of
development:
Embryonic
Fetal
Adult
pathology:
Compounds
Other human
Nonhuman
Other
human:
plant:
Other
see also disorders of globin and globulin proteins


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