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Protein

Fatty acid 2-hydroxylase

Gene

Fa2h

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids.1 Publication

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi69 – 691Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid 2-hydroxylase (EC:1.-.-.-)
Alternative name(s):
Fatty acid alpha-hydroxylase
Gene namesi
Name:Fa2h
Synonyms:Faah
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1310347. Fa2h.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei168 – 18821HelicalSequence analysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence analysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence analysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Fatty acid 2-hydroxylasePRO_0000312352Add
BLAST

Proteomic databases

PaxDbiQ2LAM0.
PRIDEiQ2LAM0.

Expressioni

Tissue specificityi

Detected in oligodendrocytes (at protein level). Detected in sciatic nerve.2 Publications

Developmental stagei

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.1 Publication

Inductioni

Up-regulated in sciatic nerve during myelination. Up-regulated in differentiating cultured Schwann cells.1 Publication

Gene expression databases

GenevisibleiQ2LAM0. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025625.

Structurei

3D structure databases

ProteinModelPortaliQ2LAM0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8679Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0539. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
HOVERGENiHBG054265.
InParanoidiQ2LAM0.
KOiK19703.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ2LAM0.
TreeFamiTF314955.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Scs7.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2LAM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPAPPPAAS FTSAEVQRRL AAGACWVRRG ASLYDLTGFV RHHPGGEQLL
60 70 80 90 100
LARAGQDISA DLDGPPHKHS DNARRWLEQY YVGELRADPQ DPTENGAGAP
110 120 130 140 150
AETQKTDAAI EPQFKVVDWD KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA
160 170 180 190 200
RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV LYLSWSYYRT LTQDNIRLFA
210 220 230 240 250
SFTRDYSLVV PESVFIGLFV LGMLIWTLVE YLIHRFLFHM KPPSNSHYLI
260 270 280 290 300
MLHFVMHGQH HKAPFDGSRL VFPPVPASVV VAFFYVFLRL ILPEAVAGIL
310 320 330 340 350
FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI
360 370
STKLWDYFFH TLIPEEADPK MQ
Length:372
Mass (Da):42,673
Last modified:December 4, 2007 - v2
Checksum:iAC02C568DF1BF7A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ339484 mRNA. Translation: ABC71132.1.
CO396956 mRNA. No translation available.
RefSeqiNP_001129055.1. NM_001135583.1.
UniGeneiRn.67886.

Genome annotation databases

EnsembliENSRNOT00000025625; ENSRNOP00000025625; ENSRNOG00000018950.
GeneIDi307855.
KEGGirno:307855.
UCSCiRGD:1310347. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ339484 mRNA. Translation: ABC71132.1.
CO396956 mRNA. No translation available.
RefSeqiNP_001129055.1. NM_001135583.1.
UniGeneiRn.67886.

3D structure databases

ProteinModelPortaliQ2LAM0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025625.

Proteomic databases

PaxDbiQ2LAM0.
PRIDEiQ2LAM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025625; ENSRNOP00000025625; ENSRNOG00000018950.
GeneIDi307855.
KEGGirno:307855.
UCSCiRGD:1310347. rat.

Organism-specific databases

CTDi79152.
RGDi1310347. Fa2h.

Phylogenomic databases

eggNOGiKOG0539. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
HOVERGENiHBG054265.
InParanoidiQ2LAM0.
KOiK19703.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ2LAM0.
TreeFamiTF314955.

Enzyme and pathway databases

ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

PROiQ2LAM0.

Gene expression databases

GenevisibleiQ2LAM0. RN.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Scs7.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFA2H_RAT
AccessioniPrimary (citable) accession number: Q2LAM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: June 8, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.