FA2H_MOUSE
ID FA2H_MOUSE Reviewed; 372 AA.
AC Q5MPP0; Q2M2M0; Q5RL53; Q8BTH1; Q8R0M0; Q8R0V1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fatty acid 2-hydroxylase {ECO:0000303|PubMed:15658937, ECO:0000303|PubMed:18815260, ECO:0000303|PubMed:21628453, ECO:0000303|PubMed:22517924};
DE EC=1.14.18.- {ECO:0000269|PubMed:22517924};
DE AltName: Full=Fatty acid alpha-hydroxylase;
GN Name=Fa2h {ECO:0000303|PubMed:15658937, ECO:0000303|PubMed:18815260,
GN ECO:0000303|PubMed:21628453, ECO:0000312|MGI:MGI:2443327}; Synonyms=Faah;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-103; LEU-348 AND
RP PRO-354, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=FVB/N;
RX PubMed=15658937; DOI=10.1042/bj20041451;
RA Eckhardt M., Yaghootfam A., Fewou S.N., Zoeller I., Gieselmann V.;
RT "A mammalian fatty acid hydroxylase responsible for the formation of alpha-
RT hydroxylated galactosylceramide in myelin.";
RL Biochem. J. 388:245-254(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-103;
RP LEU-348 AND PRO-354.
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16998236; DOI=10.1194/jlr.m600362-jlr200;
RA Alderson N.L., Maldonado E.N., Kern M.J., Bhat N.R., Hama H.;
RT "FA2H-dependent fatty acid 2-hydroxylation in postnatal mouse brain.";
RL J. Lipid Res. 47:2772-2780(2006).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND PATHWAY.
RX PubMed=18815260; DOI=10.1523/jneurosci.0458-08.2008;
RA Zoeller I., Meixner M., Hartmann D., Buessow H., Meyer R., Gieselmann V.,
RA Eckhardt M.;
RT "Absence of 2-hydroxylated sphingolipids is compatible with normal neural
RT development but causes late-onset axon and myelin sheath degeneration.";
RL J. Neurosci. 28:9741-9754(2008).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21628453; DOI=10.1074/jbc.m111.231977;
RA Maier H., Meixner M., Hartmann D., Sandhoff R., Wang-Eckhardt L.,
RA Zoeller I., Gieselmann V., Eckhardt M.;
RT "Normal fur development and sebum production depends on fatty acid 2-
RT hydroxylase expression in sebaceous glands.";
RL J. Biol. Chem. 286:25922-25934(2011).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22517924; DOI=10.1194/jlr.m025742;
RA Guo L., Zhang X., Zhou D., Okunade A.L., Su X.;
RT "Stereospecificity of fatty acid 2-hydroxylase and differential functions
RT of 2-hydroxy fatty acid enantiomers.";
RL J. Lipid Res. 53:1327-1335(2012).
CC -!- FUNCTION: Catalyzes the hydroxylation of free fatty acids at the C-2
CC position to produce 2-hydroxy fatty acids, which are building blocks of
CC sphingolipids and glycosphingolipids common in neural tissue and
CC epidermis (PubMed:15658937, PubMed:16998236, PubMed:22517924). FA2H is
CC stereospecific for the production of (R)-2-hydroxy fatty acids
CC (PubMed:22517924). Plays an essential role in the synthesis of
CC galactosphingolipids of the myelin sheath (PubMed:15658937,
CC PubMed:18815260). Responsible for the synthesis of sphingolipids and
CC glycosphingolipids involved in the formation of epidermal lamellar
CC bodies critical for skin permeability barrier (By similarity).
CC Participates in the synthesis of glycosphingolipids and a fraction of
CC type II wax diesters in sebaceous gland, specifically regulating hair
CC follicle homeostasis (PubMed:21628453). Involved in the synthesis of
CC sphingolipids of plasma membrane rafts, controlling lipid raft mobility
CC and trafficking of raft-associated proteins (PubMed:22517924).
CC {ECO:0000250|UniProtKB:Q7L5A8, ECO:0000269|PubMed:15658937,
CC ECO:0000269|PubMed:16998236, ECO:0000269|PubMed:18815260,
CC ECO:0000269|PubMed:21628453, ECO:0000269|PubMed:22517924}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-saturated fatty acid + 2 Fe(II)-[cytochrome b5] + 2 H(+)
CC + O2 = a (R)-2-hydroxy fatty acid + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:38855, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:76177,
CC ChEBI:CHEBI:83955; Evidence={ECO:0000269|PubMed:22517924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38856;
CC Evidence={ECO:0000269|PubMed:22517924};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoate + O2 = (R)-
CC 2-hydroxyhexadecanoate + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:38551, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:75927; Evidence={ECO:0000269|PubMed:22517924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38552;
CC Evidence={ECO:0000269|PubMed:22517924};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoate = (R)-
CC 2-hydroxyoctadecanoate + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:39815, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57562; Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39816;
CC Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoate + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 2-
CC hydroxydocosanoate + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:39819, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:76722; Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39820;
CC Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + tetracosanoate = (R)-
CC 2-hydroxytetracosanoate + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:38559, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31014,
CC ChEBI:CHEBI:75935; Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38560;
CC Evidence={ECO:0000250|UniProtKB:Q7L5A8};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q03529};
CC Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic
CC dimetal center. {ECO:0000250|UniProtKB:Q03529};
CC -!- PATHWAY: Sphingolipid metabolism; galactosylceramide biosynthesis.
CC {ECO:0000269|PubMed:15658937, ECO:0000269|PubMed:18815260}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:15658937, ECO:0000305|PubMed:18815260}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15658937}. Microsome membrane
CC {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15658937}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5MPP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5MPP0-2; Sequence=VSP_029838;
CC Name=3;
CC IsoId=Q5MPP0-3; Sequence=VSP_029837;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:16998236). Detected in cerebellum and forebrain
CC (PubMed:18815260, PubMed:15658937). Expression in the white matter is
CC mainly restricted in oligodendrocytes (PubMed:15658937). Expressed in
CC stomach, kidney, skin and testis (PubMed:15658937). Expressed in
CC sebaceous gland (PubMed:21628453). {ECO:0000269|PubMed:15658937,
CC ECO:0000269|PubMed:16998236, ECO:0000269|PubMed:18815260,
CC ECO:0000269|PubMed:21628453}.
CC -!- DEVELOPMENTAL STAGE: Levels increase rapidly in brains from newborns,
CC in parallel with myelination in the central nervous system. Present at
CC very low levels in newborns. Levels are highest at 2 to 3 weeks, and
CC then decrease slightly to reach an constant, intermediate level after 4
CC months. Constitutively expressed at an intermediate level throughout
CC adult life. {ECO:0000269|PubMed:15658937, ECO:0000269|PubMed:16998236}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- DOMAIN: The N-terminal cytochrome b5 heme-binding domain is essential
CC for catalytic activity. {ECO:0000250|UniProtKB:Q7L5A8}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice have normal oligodentrocyte
CC differentiation and develope structural and functional normal myelin up
CC to early adulthood. However, aged knockout mice show a massive axon and
CC myelin sheath degeneration in the spinal cord (PubMed:18815260).
CC Knockout mice show delayed fur development and a cyclic alopecia
CC (PubMed:21628453). {ECO:0000269|PubMed:18815260,
CC ECO:0000269|PubMed:21628453}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46985.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI11913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY660882; AAV70494.1; -; mRNA.
DR EMBL; AK090338; BAC41174.1; -; mRNA.
DR EMBL; AK161502; BAE36428.1; -; mRNA.
DR EMBL; BC026400; AAH26400.1; -; mRNA.
DR EMBL; BC026629; AAH26629.1; -; mRNA.
DR EMBL; BC046985; AAH46985.1; ALT_FRAME; mRNA.
DR EMBL; BC111912; AAI11913.1; ALT_INIT; mRNA.
DR EMBL; BC128080; AAI28081.1; -; mRNA.
DR EMBL; BC128081; AAI28082.1; -; mRNA.
DR CCDS; CCDS22674.1; -. [Q5MPP0-1]
DR RefSeq; NP_835187.2; NM_178086.3. [Q5MPP0-1]
DR AlphaFoldDB; Q5MPP0; -.
DR SMR; Q5MPP0; -.
DR BioGRID; 237231; 1.
DR STRING; 10090.ENSMUSP00000043597; -.
DR SwissLipids; SLP:000000363; -.
DR PhosphoSitePlus; Q5MPP0; -.
DR PaxDb; Q5MPP0; -.
DR PRIDE; Q5MPP0; -.
DR ProteomicsDB; 275834; -. [Q5MPP0-1]
DR ProteomicsDB; 275835; -. [Q5MPP0-2]
DR ProteomicsDB; 275836; -. [Q5MPP0-3]
DR Antibodypedia; 30274; 224 antibodies from 30 providers.
DR DNASU; 338521; -.
DR Ensembl; ENSMUST00000038475; ENSMUSP00000043597; ENSMUSG00000033579. [Q5MPP0-1]
DR GeneID; 338521; -.
DR KEGG; mmu:338521; -.
DR UCSC; uc009nmf.2; mouse. [Q5MPP0-1]
DR CTD; 79152; -.
DR MGI; MGI:2443327; Fa2h.
DR VEuPathDB; HostDB:ENSMUSG00000033579; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG0539; Eukaryota.
DR GeneTree; ENSGT00390000002142; -.
DR HOGENOM; CLU_034756_2_0_1; -.
DR InParanoid; Q5MPP0; -.
DR OMA; HFADYEN; -.
DR OrthoDB; 1049908at2759; -.
DR PhylomeDB; Q5MPP0; -.
DR TreeFam; TF314955; -.
DR BRENDA; 1.14.18.6; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00787; -.
DR BioGRID-ORCS; 338521; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fa2h; mouse.
DR PRO; PR:Q5MPP0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q5MPP0; protein.
DR Bgee; ENSMUSG00000033579; Expressed in skin of external ear and 142 other tissues.
DR Genevisible; Q5MPP0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IDA:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0032286; P:central nervous system myelin maintenance; IMP:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:MGI.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IDA:MGI.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
DR GO; GO:0044857; P:plasma membrane raft organization; IMP:UniProtKB.
DR GO; GO:1904697; P:regulation of acinar cell proliferation; IMP:MGI.
DR GO; GO:0042634; P:regulation of hair cycle; IMP:MGI.
DR GO; GO:1904002; P:regulation of sebum secreting cell proliferation; IMP:MGI.
DR GO; GO:0001949; P:sebaceous gland cell differentiation; IMP:MGI.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863; PTHR12863; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR PIRSF; PIRSF005149; IPC-B_HD; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Oxidoreductase; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..372
FT /note="Fatty acid 2-hydroxylase"
FT /id="PRO_0000312351"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 8..86
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 219..361
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029837"
FT VAR_SEQ 267..325
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029838"
FT VARIANT 103
FT /note="T -> I (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15658937,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 348
FT /note="F -> L (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15658937,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 354
FT /note="L -> P (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15658937,
FT ECO:0000269|PubMed:16141072"
SQ SEQUENCE 372 AA; 42981 MW; 8E3311FE6491F088 CRC64;
MAPAPPPAAS FTPAEVQRRL AAGACWVRRG ASLYDLTSFV RHHPGGEQLL LARAGQDISA
DLDGPPHRHS DNARRWLEQY YVGELRADPQ DPTENGAVAS AETQKTDPAL EPQFKVVDWD
KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV
LYLSWSYYRT LTQDNIRLFA SLTREYSMMM PESVFIGLFV LGMLFWTFVE YVIHRFLFHM
KPPSNSHYLI MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IAFFYVFLRL ILPETVGGII
FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI STKLWDYFFH
TLIPEEAHPK MQ
