FAH2_ARATH
ID FAH2_ARATH Reviewed; 237 AA.
AC Q9SUC5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dihydroceramide fatty acyl 2-hydroxylase FAH2 {ECO:0000305};
DE EC=1.14.18.7 {ECO:0000269|PubMed:22635113};
DE AltName: Full=Fatty acid 2-hydroxylase 2 {ECO:0000303|PubMed:19054355};
DE Short=AtFAH2 {ECO:0000303|PubMed:19054355};
GN Name=FAH2 {ECO:0000303|PubMed:19054355};
GN OrderedLocusNames=At4g20870 {ECO:0000312|Araport:AT4G20870};
GN ORFNames=T13K14.30 {ECO:0000312|EMBL:CAB45882.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYTB5-A; CYTB5-B;
RP 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP 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 [6]
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 the long-chain fatty acid (LCFA) palmitic acid. Probably involved in
CC the resistance response to oxidative stress.
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22635113}.
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 {ECO:0000269|PubMed:19054355}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19054355}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19054355}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers and seeds.
CC {ECO:0000269|PubMed:22918503}.
CC -!- INDUCTION: Not induced by H(2)O(2) treatment.
CC {ECO:0000269|PubMed:22635113}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22635113}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {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; AL080282; CAB45882.1; -; Genomic_DNA.
DR EMBL; AL161553; CAB79087.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84370.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67123.1; -; Genomic_DNA.
DR EMBL; AY044315; AAK73256.1; -; mRNA.
DR EMBL; AY058151; AAL25567.1; -; mRNA.
DR EMBL; AY101538; AAM26659.1; -; mRNA.
DR PIR; T10629; T10629.
DR RefSeq; NP_001328972.1; NM_001341459.1.
DR RefSeq; NP_193819.1; NM_118205.2.
DR AlphaFoldDB; Q9SUC5; -.
DR SMR; Q9SUC5; -.
DR BioGRID; 13126; 1.
DR IntAct; Q9SUC5; 1.
DR STRING; 3702.AT4G20870.1; -.
DR PaxDb; Q9SUC5; -.
DR PRIDE; Q9SUC5; -.
DR ProteomicsDB; 230955; -.
DR DNASU; 827835; -.
DR EnsemblPlants; AT4G20870.1; AT4G20870.1; AT4G20870.
DR EnsemblPlants; AT4G20870.2; AT4G20870.2; AT4G20870.
DR GeneID; 827835; -.
DR Gramene; AT4G20870.1; AT4G20870.1; AT4G20870.
DR Gramene; AT4G20870.2; AT4G20870.2; AT4G20870.
DR KEGG; ath:AT4G20870; -.
DR Araport; AT4G20870; -.
DR TAIR; locus:2133054; AT4G20870.
DR eggNOG; KOG0539; Eukaryota.
DR HOGENOM; CLU_034756_1_0_1; -.
DR InParanoid; Q9SUC5; -.
DR OMA; IQEVALM; -.
DR OrthoDB; 1049908at2759; -.
DR PhylomeDB; Q9SUC5; -.
DR BioCyc; ARA:AT4G20870-MON; -.
DR BRENDA; 1.14.18.7; 399.
DR PRO; PR:Q9SUC5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUC5; baseline and differential.
DR Genevisible; Q9SUC5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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 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 FAH2"
FT /id="PRO_0000419657"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
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; 27311 MW; B89B31208E5AE87C CRC64;
MVAERYTVDL NKPLVFQVGH LGEEYQEWIH QPIVCVEGPR FFESDFWEFL TRTVWWAIPT
IWLPVVCYVL SISASKGLTF PQIGLIVAFG VLTWTLLEYT LHRFLFHIQT KSYWANTAHY
LLHGCHHKHP QDGLRLVFPP TATAILLVPL WKLLHLLATP ATAPAILGGI LFGYVMYDIT
HYYLHHGQPK EPTFKHLKKY HLNHHFRIQD KGYGITSSLW DKVFGTLPGI KAAAKKS
