| Tag |
Content |
LipidDB ID |
LipidDB-10116-01269 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
8.56 |
Molecular Weight |
34174.64 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
NADH-cytochrome b5 reductase 3 soluble form |
Protein Synonyms/Alias |
B5R; Cytochrome b5 reductase; 1.6.2.2; Diaphorase-1; |
Gene Name |
Cyb5r3 |
Gene Synonyms/Alias |
Dia1; |
Created Date |
01-FEB-1991 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGAQLSTLS | [2][3] | N-Myristoylation | 298 | Canonical | VGHPKERCFTF**** | [1] | S-Palmitoylation |
|
Organism |
Rattus norvegicus (Rat) |
NCBI Taxa ID |
10116 |
Reference |
[1] Predicted from GPS-Lipid
[2] Borgese N, Aggujaro D, Carrera P, Pietrini G, Bassetti M. A role forN-myristoylation in protein targeting: NADH-cytochrome b5 reductase requiresmyristic acid for association with outer mitochondrial but not ER membranes. JCell Biol. 1996 Dec;135(6 Pt 1):1501-13.[ PMID:8978818]
[3] Murakami K, Yubisui T, Takeshita M, Miyata T. The NH2-terminal structures ofhuman and rat liver microsomal NADH-cytochrome b5 reductases. J Biochem. 1989Feb;105(2):312-7.[ PMID:2498303]
|
Functional Description |
Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. |
Sequence Annotation |
Domain: 40 152 FAD-binding FR-type.
Nucleotide-binding: 132 147 FAD.
Nucleotide-binding: 171 206 FAD.
Modified residue: 42 42 N6-acetyllysine.
Modified residue: 43 43 Phosphotyrosine.
Modified residue: 50 50 N6-acetyllysine.
Modified residue: 120 120 N6-acetyllysine.
|
Protein Length |
301 AA. |
Protein Sequence
(Canonical) |
MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF 60
RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK 120
FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG 180
GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD 240
KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT 300
F 301
MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF 60
RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK 120
FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG 180
GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD 240
KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT 300
F 301
|
FASTA
(Canonical) |
>LipidDB-10116-01269|P20070
MGAQLSTLSRVVLSPVWFVYSLFMKLFQRSSPAITLENPDIKYPLRLIDKEIISHDTRRF
RFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFKDTHPK
FPAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFAIRADKKSNPVVRTVKSVGMIAG
GTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVD
KAPDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQFACLPNLERVGHPKERCFT
F
MGAQLSTLSRVVLSPVWFVYSLFMKLFQRSSPAITLENPDIKYPLRLIDKEIISHDTRRF
RFALPSPQHILGLPIGQHIYLSTRIDGNLVIRPYTPVSSDDDKGFVDLVVKVYFKDTHPK
FPAGGKMSQYLENMNIGDTIEFRGPNGLLVYQGKGKFAIRADKKSNPVVRTVKSVGMIAG
GTGITPMLQVIRAVLKDPNDHTVCYLLFANQSEKDILLRPELEELRNEHSSRFKLWYTVD
KAPDAWDYSQGFVNEEMIRDHLPPPGEETLILMCGPPPMIQFACLPNLERVGHPKERCFT
F
|
Gene Ontology |
GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl GO:0005811; C:lipid particle; IEA:Ensembl GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-KW GO:0043531; F:ADP binding; IDA:RGD GO:0016208; F:AMP binding; IDA:RGD GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:RGD GO:0071949; F:FAD binding; IEA:Ensembl GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD GO:0051287; F:NAD binding; IDA:RGD GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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