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 04-NOV-2026, entry version 149. 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}; GN 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] + O2 + 2 CC H(+) = 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=hexadecanoate + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (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=octadecanoate + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (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] + O2 + 2 H(+) = 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=tetracosanoate + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (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:15658937, PubMed:18815260). 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 FunCoup; Q5MPP0; 438. DR STRING; 10090.ENSMUSP00000043597; -. DR ChEMBL; CHEMBL6196099; -. DR SwissLipids; SLP:000000363; -. DR PhosphoSitePlus; Q5MPP0; -. DR PaxDb; 10090-ENSMUSP00000043597; -. DR ProteomicsDB; 275834; -. [Q5MPP0-1] DR ProteomicsDB; 275835; -. [Q5MPP0-2] DR ProteomicsDB; 275836; -. [Q5MPP0-3] DR Antibodypedia; 30274; 244 antibodies from 32 providers. DR DNASU; 338521; -. DR Ensembl; ENSMPUT00000010067; ENSMPUP00000009907; ENSMPUG00000009982. DR Ensembl; ENSMUST00000038475.9; ENSMUSP00000043597.9; ENSMUSG00000033579.17. [Q5MPP0-1] DR GeneID; 338521; -. DR KEGG; mmu:338521; -. DR UCSC; uc009nmf.2; mouse. [Q5MPP0-1] DR AGR; MGI:2443327; -. 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; AAFFCCC; -. DR OrthoDB; 2204368at2759; -. DR PhylomeDB; Q5MPP0; -. 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 79 CRISPR screens. DR PRO; PR:Q5MPP0; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q5MPP0; protein. DR Bgee; ENSMUSG00000033579; Expressed in skin of external ear and 144 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0120521; F:4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase activity; ISO:GO_Central. DR GO; GO:0080132; F:fatty acid 2-hydroxylase activity; IDA:MGI. DR GO; GO:0120520; F:free fatty acid 2-hydroxylase activity; ISO:GO_Central. DR GO; GO:0020037; F:heme 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: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:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0042634; P:regulation of hair cycle; IMP:MGI. DR GO; GO:0001949; P:sebaceous gland cell differentiation; IMP:MGI. DR FunFam; 3.10.120.10:FF:000011; Fatty acid 2-hydroxylase; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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:SF1; FATTY ACID 2-HYDROXYLASE; 1. DR PANTHER; PTHR12863; FATTY ACID HYDROXYLASE; 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; Cytochrome b5-like heme/steroid binding domain; 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 //