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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: (3R)-3-hydroxyacyl-CoA dehydrogenase

UniprotKB/SwissProt ID: P50171 (P50171)

Gene Name: Hsd17b8

Organism: Mus musculus (Mouse)

Function: Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex, acts as scaffold protein, required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference, this enzymatic activity is not needed for the KAR function. Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+)(H). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (By similarity). NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. It efficiently catalyzes the oxidation of estradiol (E2), testosterone, and dihydrotestosterone. Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active estradiol (E2) (PubMed:9712896)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion matrix

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

The S-nitrosylation sites of P50171

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 192 ARELGRHGIR C NSVLPGFIAT  CCHHHHHHHH H HHHHCCCCCH  4.15% 21278135
2 39 LAAEGAAVAA C DLDGAAAQDT  CCHHHHHHHH H HHHHCCCCCH  3.73% 21278135