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Q2LAM0 (FA2H_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fatty acid 2-hydroxylase

EC=1.-.-.-
Alternative name(s):
Fatty acid alpha-hydroxylase
Gene names
Name:Fa2h
Synonyms:Faah
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids. Ref.4

Cofactor

Iron By similarity.

Subcellular location

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

Tissue specificity

Detected in oligodendrocytes (at protein level). Detected in sciatic nerve. Ref.3 Ref.4

Developmental stage

Detected at low levels in sciatic nerve from newborns. Levels increase strongly during the first 3 weeks, and decrease thereafter to reach a low, constitutive level in 4 week olds. Expressed at a low, constitutive level in adults. Ref.4

Induction

Up-regulated in sciatic nerve during myelination. Up-regulated in differentiating cultured Schwann cells. Ref.4

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similarities

Belongs to the sterol desaturase family. SCS7 subfamily.

Contains 1 cytochrome b5 heme-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Fatty acid 2-hydroxylase
PRO_0000312352

Regions

Transmembrane168 – 18821Helical; Potential
Transmembrane213 – 23321Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane290 – 31021Helical; Potential
Domain8 – 8679Cytochrome b5 heme-binding

Sites

Metal binding431Iron (heme axial ligand) By similarity
Metal binding691Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LAM0 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: AC02C568DF1BF7A6

FASTA37242,673
        10         20         30         40         50         60 
MAPAPPPAAS FTSAEVQRRL AAGACWVRRG ASLYDLTGFV RHHPGGEQLL LARAGQDISA 

        70         80         90        100        110        120 
DLDGPPHKHS DNARRWLEQY YVGELRADPQ DPTENGAGAP AETQKTDAAI EPQFKVVDWD 

       130        140        150        160        170        180 
KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV 

       190        200        210        220        230        240 
LYLSWSYYRT LTQDNIRLFA SFTRDYSLVV PESVFIGLFV LGMLIWTLVE YLIHRFLFHM 

       250        260        270        280        290        300 
KPPSNSHYLI MLHFVMHGQH HKAPFDGSRL VFPPVPASVV VAFFYVFLRL ILPEAVAGIL 

       310        320        330        340        350        360 
FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI STKLWDYFFH 

       370 
TLIPEEADPK MQ 

« Hide

References

« Hide 'large scale' references
[1]Molto E., Bonzon-Kulichenko E., Gallardo N., Andres A.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-347.
Strain: Wistar.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-372.
[3]"FA2H-dependent fatty acid 2-hydroxylation in postnatal mouse brain."
Alderson N.L., Maldonado E.N., Kern M.J., Bhat N.R., Hama H.
J. Lipid Res. 47:2772-2780(2006) [PubMed: 16998236] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"FA2H is responsible for the formation of 2-hydroxy galactolipids in peripheral nervous system myelin."
Maldonado E.N., Alderson N.L., Monje P.V., Wood P.M., Hama H.
J. Lipid Res. 49:153-161(2008) [PubMed: 17901466] [Abstract]
Cited for: FUNCTION, INDUCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ339484 mRNA. Translation: ABC71132.1.
CO396956 mRNA. No translation available.
IPIIPI00359657.
RefSeqNP_001129055.1. NM_001135583.1.
UniGeneRn.67886.

3D structure databases

ProteinModelPortalQ2LAM0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2LAM0.

Proteomic databases

PRIDEQ2LAM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025625; ENSRNOP00000025625; ENSRNOG00000018950.
GeneID307855.
KEGGrno:307855.
NMPDRfig|10116.3.peg.15027.

Organism-specific databases

CTD79152.
RGD1310347. Fa2h.

Phylogenomic databases

eggNOGroNOG04473.
GeneTreeENSGT00390000002142.
HOVERGENHBG054265.
InParanoidQ2LAM0.
OMALGYVLYD.
OrthoDBEOG4PK28C.
PhylomeDBQ2LAM0.

Gene expression databases

GenevestigatorQ2LAM0.

Family and domain databases

InterProIPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Ino-phos-ceramide-B_Hydrxlase.
[Graphical view]
Gene3DG3DSA:3.10.120.10. Cyt_B5. 1 hit.
PfamPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFPIRSF005149. IPC-B_HD. 1 hit.
PRINTSPR00363. CYTOCHROMEB5.
SUPFAMSSF55856. Cyt_B5. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio658001.

Entry information

Entry nameFA2H_RAT
AccessionPrimary (citable) accession number: Q2LAM0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: September 21, 2011
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families