Recombinant Human Fatty acid 2-hydroxylase (FA2H), Truncated

Uniprot Id

Q7L5A8

Target Species

Human

Target Name

FA2H

Target Full Name

Fatty acid 2-hydroxylase

Target Function

Catalyzes the hydroxylation of free fatty acids at the C-2 position to produce 2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis. FA2H is stereospecific for the production of (R)-2-hydroxy fatty acids. Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath. Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier. Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis. Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins.

Target Involvement

Spastic paraplegia 35, autosomal recessive (SPG35)

Target Subcellular Location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein.

Target Protein Families

Sterol desaturase family, SCS7 subfamily

Target Tissue Specificity

Detected in differentiating cultured keratinocytes (at protein level). Detected in epidermis and cultured keratinocytes. Highly expressed in brain and colon. Detected at lower levels in testis, prostate, pancreas and kidney.

Target Synonyms

FA2H; FAAH; FAXDC1; Fatty acid 2-hydroxylase; Fatty acid alpha-hydroxylase; Fatty acid hydroxylase domain-containing protein 1

Target Background

This gene encodes a protein that catalyzes the synthesis of 2-hydroxysphingolipids, a subset of sphingolipids that contain 2-hydroxy fatty acids. Sphingolipids play roles in many cellular processes and their structural diversity arises from modification of the hydrophobic ceramide moiety, such as by 2-hydroxylation of the N-acyl chain, and the existence of many different head groups. Mutations in this gene have been associated with leukodystrophy dysmyelinating with spastic paraparesis with or without dystonia.