Q5MPP0 (FA2H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids. Ref.1 Ref.4
Cofactor	Iron By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Detected in brain and skin (at protein level). Detected in brain white matter, cerebellum forebrain, stomach, kidney, skin and testis. Detected in oligodendrocytes. Ref.1 Ref.4
Developmental stage	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. Ref.1 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 caution	The sequence AAH46985.1 differs from that shown. Reason: Frameshift at position 34. The sequence AAI11913.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Lipid synthesis Transport
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5MPP0-1)

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.

Isoform 2 (identifier: Q5MPP0-2)

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

Isoform 3 (identifier: Q5MPP0-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	Fatty acid 2-hydroxylase		PRO_0000312351
Regions
	Transmembrane	168 – 188	21	Helical; Potential
	Transmembrane	213 – 233	21	Helical; Potential
	Transmembrane	268 – 288	21	Helical; Potential
	Transmembrane	290 – 310	21	Helical; Potential
	Domain	8 – 86	79	Cytochrome b5 heme-binding
Sites
	Metal binding	43	1	Iron (heme axial ligand) By similarity
	Metal binding	69	1	Iron (heme axial ligand) By similarity
Natural variations
	Alternative sequence	1 – 208	208	Missing in isoform 3.		VSP_029837
	Alternative sequence	267 – 325	59	Missing in isoform 2.		VSP_029838
	Natural variant	103	1	T → I in strain: C57BL/6J. Ref.1 Ref.2
	Natural variant	348	1	F → L in strain: C57BL/6J. Ref.1 Ref.2
	Natural variant	354	1	L → P in strain: C57BL/6J. Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 8E3311FE6491F088	FASTA	372	42,981
	10 20 30 40 50 60 MAPAPPPAAS FTPAEVQRRL AAGACWVRRG ASLYDLTSFV RHHPGGEQLL LARAGQDISA 70 80 90 100 110 120 DLDGPPHRHS DNARRWLEQY YVGELRADPQ DPTENGAVAS AETQKTDPAL EPQFKVVDWD 130 140 150 160 170 180 KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV 190 200 210 220 230 240 LYLSWSYYRT LTQDNIRLFA SLTREYSMMM PESVFIGLFV LGMLFWTFVE YVIHRFLFHM 250 260 270 280 290 300 KPPSNSHYLI MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IAFFYVFLRL ILPETVGGII 310 320 330 340 350 360 FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI STKLWDYFFH 370 TLIPEEAHPK MQ
	Isoform 2 [UniParc]. Checksum: E84CB7A709E01ED6	FASTA	313	36,428
	10 20 30 40 50 60 MAPAPPPAAS FTPAEVQRRL AAGACWVRRG ASLYDLTSFV RHHPGGEQLL LARAGQDISA 70 80 90 100 110 120 DLDGPPHRHS DNARRWLEQY YVGELRADPQ DPTENGAVAS AETQKTDPAL EPQFKVVDWD 130 140 150 160 170 180 KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV 190 200 210 220 230 240 LYLSWSYYRT LTQDNIRLFA SLTREYSMMM PESVFIGLFV LGMLFWTFVE YVIHRFLFHM 250 260 270 280 290 300 KPPSNSHYLI MLHFVMHGQH HKAPFDGSYL YNMKAHHVKH HFEYQKSGFG ISTKLWDYFF 310 HTLIPEEAHP KMQ
	Isoform 3 [UniParc]. Checksum: 67DB00281A4B380B	FASTA	164	19,207
	10 20 30 40 50 60 MMPESVFIGL FVLGMLFWTF VEYVIHRFLF HMKPPSNSHY LIMLHFVMHG QHHKAPFDGS 70 80 90 100 110 120 RLVFPPVPAS LVIAFFYVFL RLILPETVGG IIFAGGLLGY VLYDMTHYYL HFGSPHKGSY 130 140 150 160 LYNMKAHHVK HHFEYQKSGF GISTKLWDYF FHTLIPEEAH PKMQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15658937] [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: 16141072] [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: 15489334] [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: 16998236] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00225038. IPI00462412. IPI00877239.
RefSeq	NP_835187.2. NM_178086.3.
UniGene	Mm.41083.
3D structure databases
HSSP	HSSP built from PDB template 1AWP based on UniProtKB P04166.
ProteinModelPortal	Q5MPP0.
SMR	Q5MPP0. Positions 6-114.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5MPP0.
Proteomic databases
PRIDE	Q5MPP0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000038475; ENSMUSP00000043597; ENSMUSG00000033579. ENSMUST00000093130; ENSMUSP00000090818; ENSMUSG00000033579.
GeneID	338521.
KEGG	mmu:338521.
NMPDR	fig|10090.3.peg.19266.
UCSC	uc009nmf.2. mouse.
Organism-specific databases
CTD	79152.
MGI	MGI:2443327. Fa2h.
Phylogenomic databases
eggNOG	roNOG04473.
GeneTree	ENSGT00390000002142.
HOVERGEN	HBG054265.
OrthoDB	EOG4PK28C.
PhylomeDB	Q5MPP0.
Gene expression databases
ArrayExpress	Q5MPP0.
Bgee	Q5MPP0.
CleanEx	MM_FA2H. MM_FAAH.
Genevestigator	Q5MPP0.
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.
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	400217.
SOURCE	Search...

Entry information

Entry name

FA2H_MOUSE

Accession

Primary (citable) accession number: Q5MPP0
Secondary accession number(s): Q2M2M0 , Q5RL53, Q8BTH1, Q8R0M0, Q8R0V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	February 1, 2005
Last modified:	November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program