Fatty acid 2-hydroxylase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q2LAM0 (FA2H_RAT)

Last modified June 16, 2009. Version 30. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fatty acid 2-hydroxylase
    EC=1.-.-.-
Alternative name(s):
    Fatty acid alpha-hydroxylase

Gene names

Name:	Fa2h
Synonyms:	Faah

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.4 Ref.3
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 SCS7 family. Contains 1 cytochrome b5 heme-binding domain.

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Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Lipid synthesis Transport
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW sphingolipid metabolic process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 372

372

Fatty acid 2-hydroxylase

PRO_0000312352

Regions

Transmembrane

168 – 188

Potential

Transmembrane

213 – 233

Potential

Transmembrane

268 – 288

Potential

Transmembrane

290 – 310

Potential

Domain

8 – 86

Cytochrome b5 heme-binding

Sites

Metal binding

Iron (heme axial ligand) By similarity

Metal binding

Iron (heme axial ligand) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q2LAM0-1 [UniParc].

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

372

42,673

        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

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References

	« Hide 'large scale' referencesShow '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.

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Cross-references

Sequence databases
	DQ339484 mRNA. Translation: ABC71132.1. CO396956 mRNA. No translation available.
IPI	IPI00359657.
RefSeq	NP_001129055.1.
UniGene	Rn.67886
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000018950. Rattus norvegicus. [Contig view]
GeneID	307855.
KEGG	rno:307855.
NMPDR	fig\|10116.3.peg.15027.
Organism-specific databases
RGD	1310347. Fa2h.
Phylogenomic databases
HOVERGEN	Q2LAM0.
OMA	Q2LAM0. NKPLLMQ.
Gene expression databases
ArrayExpress	Q2LAM0.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR006694. Fatty_acid_hydroxylase. IPR014430. Ino-phos-ceramide-B_Hydrxlase. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. PF04116. FA_hydroxylase. 1 hit. [Graphical view]
PIRSF	PIRSF005149. IPC-B_HD. 1 hit.
PRINTS	PR00363. CYTOCHROMEB5.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	658001.

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Entry information

Entry name

FA2H_RAT

Accession

Primary (citable) accession number: Q2LAM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 30 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents