FAH1_ARATH
ID FAH1_ARATH Reviewed; 237 AA.
AC O48916;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Dihydroceramide fatty acyl 2-hydroxylase FAH1 {ECO:0000305};
DE EC=1.14.18.7 {ECO:0000269|PubMed:22635113};
DE AltName: Full=Fatty acid 2-hydroxylase 1 {ECO:0000303|PubMed:19054355};
DE Short=AtFAH1 {ECO:0000303|PubMed:19054355};
GN Name=FAH1 {ECO:0000303|PubMed:19054355};
GN OrderedLocusNames=At2g34770 {ECO:0000312|Araport:AT2G34770};
GN ORFNames=T29F13.2 {ECO:0000312|EMBL:AAC16270.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9353282; DOI=10.1074/jbc.272.45.28281;
RA Mitchell A.G., Martin C.E.;
RT "Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its
RT Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both
RT function in the alpha-hydroxylation of sphingolipid-associated very long
RT chain fatty acids.";
RL J. Biol. Chem. 272:28281-28288(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INTERACTION WITH CYTB5-A; CYTB5-B; CYTB5-C AND CYTB5-D.
RX PubMed=19054355; DOI=10.1111/j.1365-313x.2008.03765.x;
RA Nagano M., Ihara-Ohori Y., Imai H., Inada N., Fujimoto M., Tsutsumi N.,
RA Uchimiya H., Kawai-Yamada M.;
RT "Functional association of cell death suppressor, Arabidopsis Bax
RT inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b(5).";
RL Plant J. 58:122-134(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP CYTB5-D, AND INDUCTION BY H(2)O(2).
RC STRAIN=cv. Columbia;
RX PubMed=22635113; DOI=10.1104/pp.112.199547;
RA Nagano M., Takahara K., Fujimoto M., Tsutsumi N., Uchimiya H.,
RA Kawai-Yamada M.;
RT "Arabidopsis sphingolipid fatty acid 2-hydroxylases (AtFAH1 and AtFAH2) are
RT functionally differentiated in fatty acid 2-hydroxylation and stress
RT responses.";
RL Plant Physiol. 159:1138-1148(2012).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22918503; DOI=10.4161/psb.21825;
RA Nagano M., Uchimiya H., Kawai-Yamada M.;
RT "Plant sphingolipid fatty acid 2-hydroxylases have unique characters unlike
RT their animal and fungus counterparts.";
RL Plant Signal. Behav. 7:1388-1392(2012).
CC -!- FUNCTION: Fatty acid 2-hydroxylase involved in the alpha-hydroxylation
CC of sphingolipid-associated very long-chain fatty acids (VLCFA).
CC Probably involved in the resistance response to oxidative stress.
CC {ECO:0000269|PubMed:22635113, ECO:0000269|PubMed:9353282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(1,2-saturated acyl)sphinganine + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = an N-[(2'R)-hydroxyacyl]sphinganine + 2 Fe(III)-
CC [cytochrome b5] + H2O; Xref=Rhea:RHEA:46512, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:86265, ChEBI:CHEBI:86266; EC=1.14.18.7;
CC Evidence={ECO:0000269|PubMed:22635113};
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 -!- SUBUNIT: Interacts with CYTB5-A, CYTB5-B, CYTB5-C and CYTB5-D.
CC Interacts indirectly with BI-1 via CYTB5-D.
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22635113}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22635113}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22635113}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers and seeds.
CC {ECO:0000269|PubMed:22918503}.
CC -!- INDUCTION: Up-regulated by H(2)O(2) treatment.
CC {ECO:0000269|PubMed:22635113}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AF021804; AAB94072.1; -; mRNA.
DR EMBL; AC003096; AAC16270.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09019.1; -; Genomic_DNA.
DR EMBL; AY050326; AAK91343.1; -; mRNA.
DR EMBL; BT000482; AAN18051.1; -; mRNA.
DR PIR; T01359; T01359.
DR RefSeq; NP_181023.1; NM_129030.2.
DR AlphaFoldDB; O48916; -.
DR SMR; O48916; -.
DR BioGRID; 3388; 1.
DR IntAct; O48916; 1.
DR STRING; 3702.AT2G34770.1; -.
DR PaxDb; O48916; -.
DR PRIDE; O48916; -.
DR ProteomicsDB; 230954; -.
DR EnsemblPlants; AT2G34770.1; AT2G34770.1; AT2G34770.
DR GeneID; 818042; -.
DR Gramene; AT2G34770.1; AT2G34770.1; AT2G34770.
DR KEGG; ath:AT2G34770; -.
DR Araport; AT2G34770; -.
DR TAIR; locus:2061564; AT2G34770.
DR eggNOG; KOG0539; Eukaryota.
DR HOGENOM; CLU_034756_1_0_1; -.
DR InParanoid; O48916; -.
DR OMA; GVHHDYP; -.
DR OrthoDB; 1049908at2759; -.
DR PhylomeDB; O48916; -.
DR BioCyc; ARA:AT2G34770-MON; -.
DR BioCyc; MetaCyc:AT2G34770-MON; -.
DR BRENDA; 1.14.18.7; 399.
DR PRO; PR:O48916; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48916; baseline and differential.
DR Genevisible; O48916; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0080132; F:fatty acid alpha-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102771; F:sphingolipid very long chain fatty acid alpha-hydroxylase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:TAIR.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863; PTHR12863; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..237
FT /note="Dihydroceramide fatty acyl 2-hydroxylase FAH1"
FT /id="PRO_0000419656"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
SQ SEQUENCE 237 AA; 27422 MW; 9EF58769FEBCA5C7 CRC64;
MVAQGFTVDL KKPLVFQVGH LGEDYEEWVH QPIATKEGPR FFQSDFWEFL TLTVWWAVPV
IWLPVVVWCI SRSVSMGCSL PEIVPIVVMG IFIWTFFEYV LHRFVFHIKT KSYWGNTAHY
LIHGCHHKHP MDHLRLVFPP TATAILCFPF WNIAKAISTP STAPALFGGG MLGYVMYDVT
HYYLHHAQPT RPVTKNLKKY HLNHHFRIQD KGFGITSSLW DIVFGTLPTT KAPRKEQ
