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Protein

Fatty acid 2-hydroxylase

Gene

Fa2h

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids.2 Publications

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

  • fatty acid alpha-hydroxylase activity Source: MGI
  • heme binding Source: InterPro
  • iron ion binding Source: InterPro

GO - Biological processi

  • central nervous system myelin maintenance Source: MGI
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • fatty acid metabolic process Source: MGI
  • lipid modification Source: MGI
  • peripheral nervous system myelin maintenance Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of hair cycle Source: MGI
  • sebaceous gland cell differentiation Source: MGI
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-MMU-1660661. Sphingolipid de novo biosynthesis.

Chemistry

SwissLipidsiSLP:000000363.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2443327. 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_0000312351Add
BLAST

Proteomic databases

MaxQBiQ5MPP0.
PaxDbiQ5MPP0.
PRIDEiQ5MPP0.

Expressioni

Tissue specificityi

Detected in brain and skin (at protein level). Detected in brain white matter, cerebellum forebrain, stomach, kidney, skin and testis. Detected in oligodendrocytes.2 Publications

Developmental stagei

Levels increase rapidly in brains from newborns, in parallel with myelination in the central nervous system. Present at very low levels in newborns. Levels are highest at 2 to 3 weeks, and then decrease slightly to reach an constant, intermediate level after 4 months. Constitutively expressed at an intermediate level throughout adult life.2 Publications

Gene expression databases

BgeeiQ5MPP0.
CleanExiMM_FA2H.
MM_FAAH.
GenevisibleiQ5MPP0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043597.

Structurei

3D structure databases

ProteinModelPortaliQ5MPP0.
SMRiQ5MPP0. Positions 11-88, 105-372.
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.
InParanoidiQ5MPP0.
KOiK19703.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ5MPP0.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5MPP0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPAPPPAAS FTPAEVQRRL AAGACWVRRG ASLYDLTSFV RHHPGGEQLL
60 70 80 90 100
LARAGQDISA DLDGPPHRHS DNARRWLEQY YVGELRADPQ DPTENGAVAS
110 120 130 140 150
AETQKTDPAL EPQFKVVDWD KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA
160 170 180 190 200
RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV LYLSWSYYRT LTQDNIRLFA
210 220 230 240 250
SLTREYSMMM PESVFIGLFV LGMLFWTFVE YVIHRFLFHM KPPSNSHYLI
260 270 280 290 300
MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IAFFYVFLRL ILPETVGGII
310 320 330 340 350
FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI
360 370
STKLWDYFFH TLIPEEAHPK MQ
Length:372
Mass (Da):42,981
Last modified:February 1, 2005 - v1
Checksum:i8E3311FE6491F088
GO
Isoform 2 (identifier: Q5MPP0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-325: Missing.

Show »
Length:313
Mass (Da):36,428
Checksum:iE84CB7A709E01ED6
GO
Isoform 3 (identifier: Q5MPP0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-208: Missing.

Show »
Length:164
Mass (Da):19,207
Checksum:i67DB00281A4B380B
GO

Sequence cautioni

The sequence AAH46985.1 differs from that shown. Reason: Frameshift at position 34. Curated
The sequence AAI11913.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031T → I in strain: C57BL/6J. 2 Publications
Natural varianti348 – 3481F → L in strain: C57BL/6J. 2 Publications
Natural varianti354 – 3541L → P in strain: C57BL/6J. 2 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 208208Missing in isoform 3. 1 PublicationVSP_029837Add
BLAST
Alternative sequencei267 – 32559Missing in isoform 2. 1 PublicationVSP_029838Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY660882 mRNA. Translation: AAV70494.1.
AK090338 mRNA. Translation: BAC41174.1.
AK161502 mRNA. Translation: BAE36428.1.
BC026400 mRNA. Translation: AAH26400.1.
BC026629 mRNA. Translation: AAH26629.1.
BC046985 mRNA. Translation: AAH46985.1. Frameshift.
BC111912 mRNA. Translation: AAI11913.1. Different initiation.
BC128080 mRNA. Translation: AAI28081.1.
BC128081 mRNA. Translation: AAI28082.1.
CCDSiCCDS22674.1. [Q5MPP0-1]
RefSeqiNP_835187.2. NM_178086.3. [Q5MPP0-1]
UniGeneiMm.41083.

Genome annotation databases

EnsembliENSMUST00000038475; ENSMUSP00000043597; ENSMUSG00000033579. [Q5MPP0-1]
GeneIDi338521.
KEGGimmu:338521.
UCSCiuc009nmf.2. mouse. [Q5MPP0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY660882 mRNA. Translation: AAV70494.1.
AK090338 mRNA. Translation: BAC41174.1.
AK161502 mRNA. Translation: BAE36428.1.
BC026400 mRNA. Translation: AAH26400.1.
BC026629 mRNA. Translation: AAH26629.1.
BC046985 mRNA. Translation: AAH46985.1. Frameshift.
BC111912 mRNA. Translation: AAI11913.1. Different initiation.
BC128080 mRNA. Translation: AAI28081.1.
BC128081 mRNA. Translation: AAI28082.1.
CCDSiCCDS22674.1. [Q5MPP0-1]
RefSeqiNP_835187.2. NM_178086.3. [Q5MPP0-1]
UniGeneiMm.41083.

3D structure databases

ProteinModelPortaliQ5MPP0.
SMRiQ5MPP0. Positions 11-88, 105-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043597.

Chemistry

SwissLipidsiSLP:000000363.

Proteomic databases

MaxQBiQ5MPP0.
PaxDbiQ5MPP0.
PRIDEiQ5MPP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038475; ENSMUSP00000043597; ENSMUSG00000033579. [Q5MPP0-1]
GeneIDi338521.
KEGGimmu:338521.
UCSCiuc009nmf.2. mouse. [Q5MPP0-1]

Organism-specific databases

CTDi79152.
MGIiMGI:2443327. Fa2h.

Phylogenomic databases

eggNOGiKOG0539. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
HOVERGENiHBG054265.
InParanoidiQ5MPP0.
KOiK19703.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ5MPP0.
TreeFamiTF314955.

Enzyme and pathway databases

ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

PROiQ5MPP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ5MPP0.
CleanExiMM_FA2H.
MM_FAAH.
GenevisibleiQ5MPP0. MM.

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. "A mammalian fatty acid hydroxylase responsible for the formation of alpha-hydroxylated galactosylceramide in myelin."
    Eckhardt M., Yaghootfam A., Fewou S.N., Zoeller I., Gieselmann V.
    Biochem. J. 388:245-254(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-103; LEU-348 AND PRO-354, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: FVB/N.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-103; LEU-348 AND PRO-354.
    Strain: C57BL/6J.
    Tissue: Diencephalon and Testis.
  3. "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] (ISOFORMS 1; 2 AND 3).
    Strain: FVB/N.
    Tissue: Colon.
  4. "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: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFA2H_MOUSE
AccessioniPrimary (citable) accession number: Q5MPP0
Secondary accession number(s): Q2M2M0
, Q5RL53, Q8BTH1, Q8R0M0, Q8R0V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 102 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.