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Cytochrome b5, type A

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CYB5A

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2I96

Identifiers

CYB5A, CYB5, MCB5, Cytochrome b5, type A, cytochrome b5 type A, METAG

External IDs

OMIM: 613218; MGI: 1926952; HomoloGene: 41475; GeneCards: CYB5A; OMA:CYB5A - orthologs

Gene location (Human)

Chr.	Chromosome 18 (human)^[1]

Band	18q22.3	Start	74,250,846 bp^[1]
Band	18q22.3	End	74,291,973 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[2]

Band	18 E4\|18 57.53 cM	Start	84,856,829 bp^[2]
Band	18 E4\|18 57.53 cM	End	84,897,996 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

kidney tubule

right lobe of liver

renal medulla

glomerulus

pancreatic ductal cell

jejunal mucosa

metanephric glomerulus

body of pancreas

gallbladder

human kidney

Top expressed in

right kidney

olfactory epithelium

proximal tubule

gallbladder

transitional epithelium of urinary bladder

human kidney

gastrula

iris

left lobe of liver

decidua

More reference expression data


More reference expression data

Gene ontology
Molecular function	cytochrome-c oxidase activity aldo-keto reductase (NADP) activity metal ion binding heme binding enzyme binding
Cellular component	organelle membrane integral component of membrane endoplasmic reticulum membrane membrane intracellular membrane-bounded organelle mitochondrial outer membrane endoplasmic reticulum mitochondrion extracellular exosome cytoplasm cytosol
Biological process	response to cadmium ion L-ascorbic acid metabolic process proton transmembrane transport electron transport chain
Sources:Amigo / QuickGO

Species

Human

Mouse


1528


109672


ENSG00000166347


ENSMUSG00000024646


P00167


P56395

RefSeq (mRNA)


NM_001190807 NM_001914 NM_148923


NM_025797 NM_001348159

RefSeq (protein)


NP_001177736 NP_001905 NP_683725


NP_080073 NP_001335088

Location (UCSC)

Chr 18: 74.25 – 74.29 Mb

Chr 18: 84.86 – 84.9 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Cytochrome b5, form A (gene name CYB5A), is a human microsomal cytochrome b5.^[5]

Cytochrome b5 is a membrane bound hemoprotein which functions as an electron carrier for several membrane bound oxygenases. It has two isoforms produced by alternative splicing. Isoform 1 is bound to the cytoplasmic side of the endoplasmic reticulum. It has a C-terminal transmembrane alpha-helix. Isoform 2 was found in cytoplasm. Defects in CYB5A are the cause of type IV hereditary methemoglobinemia.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000166347 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024646 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: CYB5A Cytochrome b5, form A".

Further reading

Ng S, Smith MB, Smith HT, Millett F (1977). "Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5". Biochemistry. 16 (23): 4975–8. doi:10.1021/bi00642a006. PMID 199233.
Dailey HA, Strittmatter P (1979). "Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase". J. Biol. Chem. 254 (12): 5388–96. doi:10.1016/S0021-9258(18)50608-6. PMID 221468.
Mitoma J, Ito A (1992). "The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum". EMBO J. 11 (11): 4197–203. doi:10.1002/j.1460-2075.1992.tb05513.x. PMC 556930. PMID 1396600.
Giordano SJ, Steggles AW (1991). "The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene". Biochem. Biophys. Res. Commun. 178 (1): 38–44. doi:10.1016/0006-291X(91)91776-9. PMID 1712589.
Shephard EA, Povey S, Spurr NK, Phillips IR (1992). "Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome". Genomics. 11 (2): 302–8. doi:10.1016/0888-7543(91)90136-3. PMID 1840560.
Strittmatter P, Hackett CS, Korza G, Ozols J (1991). "Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase". J. Biol. Chem. 265 (35): 21709–13. doi:10.1016/S0021-9258(18)45798-5. PMID 2123873.
Ozols J (1989). "Structure of cytochrome b5 and its topology in the microsomal membrane". Biochim. Biophys. Acta. 997 (1–2): 121–30. doi:10.1016/0167-4838(89)90143-X. PMID 2752049.
Yoo M, Steggles AW (1988). "The complete nucleotide sequence of human liver cytochrome b5 mRNA". Biochem. Biophys. Res. Commun. 156 (1): 576–80. doi:10.1016/S0006-291X(88)80881-7. PMID 3178851.
Hegesh E, Hegesh J, Kaftory A (1986). "Congenital methemoglobinemia with a deficiency of cytochrome b5". N. Engl. J. Med. 314 (12): 757–61. doi:10.1056/NEJM198603203141206. PMID 3951505.
Abe K, Kimura S, Kizawa R, et al. (1985). "Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5". J. Biochem. 97 (6): 1659–68. doi:10.1093/oxfordjournals.jbchem.a135224. PMID 4030743.
Strittmatter P, Spatz L, Corcoran D, et al. (1975). "Purification and properties of rat liver microsomal stearyl coenzyme A desaturase". Proc. Natl. Acad. Sci. U.S.A. 71 (11): 4565–9. doi:10.1073/pnas.71.11.4565. PMC 433928. PMID 4373719.
Rashid MA, Hagihara B, Kobayashi M, et al. (1974). "Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5". J. Biochem. 74 (5): 985–1002. PMID 4770377.
Nóbrega FG, Ozols J (1971). "Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes of human, monkey, porcine, and chicken liver". J. Biol. Chem. 246 (6): 1706–17. doi:10.1016/S0021-9258(18)62368-3. PMID 4993957.
Ozols J (1972). "Cytochrome b 5 from a normal human liver. Isolation and the partial amino acid sequence". J. Biol. Chem. 247 (7): 2242–5. doi:10.1016/S0021-9258(19)45520-8. PMID 5062820.
Dailey HA, Strittmatter P (1980). "Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase". J. Biol. Chem. 255 (11): 5184–9. doi:10.1016/S0021-9258(19)70768-6. PMID 6102994.
De Silvestris M, D'Arrigo A, Borgese N (1995). "The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region". FEBS Lett. 370 (1–2): 69–74. doi:10.1016/0014-5793(95)00797-D. PMID 7649306. S2CID 26031756.
Li XR, Giordano SJ, Yoo M, Steggles AW (1995). "The isolation and characterization of the human cytochrome b5 gene". Biochem. Biophys. Res. Commun. 209 (3): 894–900. doi:10.1006/bbrc.1995.1582. PMID 7733981.
Giordano SJ, Yoo M, Ward DC, et al. (1994). "The human cytochrome b5 gene and two of its pseudogenes are located on chromosomes 18q23, 14q31-32.1 and 20p11.2, respectively". Hum. Genet. 92 (6): 615–8. doi:10.1007/BF00420948. PMID 8262522. S2CID 28828499.
Guengerich FP, Johnson WW (1998). "Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems". Biochemistry. 36 (48): 14741–50. doi:10.1021/bi9719399. PMID 9398194.
Lee-Robichaud P, Akhtar ME, Akhtar M (1998). "Control of androgen biosynthesis in the human through the interaction of Arg347 and Arg358 of CYP17 with cytochrome b5". Biochem. J. 332. ( Pt 2) (2): 293–6. doi:10.1042/bj3320293. PMC 1219480. PMID 9601054.

PDB gallery

1cyo: BOVINE CYTOCHROME B(5)
1do9: SOLUTION STRUCTURE OF OXIDIZED MICROSOMAL RABBIT CYTOCHROME B5. FACTORS DETERMINING THE HETEROGENEOUS BINDING OF THE HEME.
1ehb: CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5
1es1: CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5
1f03: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C
1f04: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C
1i5u: SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE MUTANT (E48A/E56A/D60A)
1j0q: Solution Structure of Oxidized Bovine Microsomal Cytochrome b5 mutant V61H
1lqx: Crystal structure of V45E mutant of cytochrome b5
1lr6: Crystal structure of V45Y mutant of cytochrome b5
1m20: Crystal Structure of F35Y Mutant of Trypsin-solubilized Fragment of Cytochrome b5
1m2i: Crystal structure of E44A/E56A mutant of cytochrome b5
1m2m: Crystal structure of E44A/E48A/E56A/D60A mutant of cytochrome b5
1m59: Crystal Structure of P40V Mutant of Trypsin-solubilized Fragment of Cytochrome b5
1nx7: Solution Structure of Oxidized Bovine Microsomal Cytochrome B5
1sh4: Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H
1u9m: Crystal structure of F58W mutant of cytochrome b5
1u9u: Crystal structure of F58Y mutant of cytochrome b5

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