SBH1_ARATH
ID SBH1_ARATH Reviewed; 260 AA.
AC Q8VYI1; Q9FWZ2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Sphinganine C4-monooxygenase 1;
DE EC=1.14.18.5 {ECO:0000269|PubMed:11297741};
DE AltName: Full=Sphingoid C4-hydroxylase 1;
DE AltName: Full=Sphingoid base hydroxylase 1;
GN Name=SBH1; OrderedLocusNames=At1g69640; ORFNames=F24J1.22, T6C23.16;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11297741; DOI=10.1016/s0014-5793(01)02332-8;
RA Sperling P., Ternes P., Moll H., Franke S., Zaehringer U., Heinz E.;
RT "Functional characterization of sphingolipid C4-hydroxylase genes from
RT Arabidopsis thaliana.";
RL FEBS Lett. 494:90-94(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18612100; DOI=10.1105/tpc.107.057851;
RA Chen M., Markham J.E., Dietrich C.R., Jaworski J.G., Cahoon E.B.;
RT "Sphingolipid long-chain base hydroxylation is important for growth and
RT regulation of sphingolipid content and composition in Arabidopsis.";
RL Plant Cell 20:1862-1878(2008).
CC -!- FUNCTION: Involved in sphingolipid trihydroxy long-chain base (4-
CC hydroxysphinganine) biosynthesis. Can use C18- and C20-sphinganine as
CC substrates to produce C18- and C20-phytosphinganines (D-ribo-2-amino-
CC 1,3,4-trihydroxyoctadecane and -eicosane).
CC {ECO:0000269|PubMed:11297741, ECO:0000269|PubMed:18612100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dihydroceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC phytoceramide + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:55808, 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:139048,
CC ChEBI:CHEBI:139051; EC=1.14.18.5;
CC Evidence={ECO:0000269|PubMed:11297741};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18612100}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18612100}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in flowers and
CC roots. {ECO:0000269|PubMed:18612100}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC SBH2. Sbh1 and sbh2 double mutants are severely dwarfed, do not
CC progress from vegetative to reproductive growth and have enhanced
CC expression of programmed cell death associated-genes.
CC {ECO:0000269|PubMed:18612100}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG12703.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG52550.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013289; AAG52550.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC021046; AAG12703.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE34958.1; -; Genomic_DNA.
DR EMBL; AY070765; AAL50102.1; -; mRNA.
DR EMBL; AY143918; AAN28857.1; -; mRNA.
DR PIR; B96718; B96718.
DR RefSeq; NP_177122.2; NM_105632.5.
DR AlphaFoldDB; Q8VYI1; -.
DR SMR; Q8VYI1; -.
DR BioGRID; 28521; 15.
DR IntAct; Q8VYI1; 15.
DR STRING; 3702.AT1G69640.1; -.
DR PaxDb; Q8VYI1; -.
DR PRIDE; Q8VYI1; -.
DR ProteomicsDB; 228153; -.
DR EnsemblPlants; AT1G69640.1; AT1G69640.1; AT1G69640.
DR GeneID; 843300; -.
DR Gramene; AT1G69640.1; AT1G69640.1; AT1G69640.
DR KEGG; ath:AT1G69640; -.
DR Araport; AT1G69640; -.
DR TAIR; locus:2026756; AT1G69640.
DR eggNOG; KOG0874; Eukaryota.
DR HOGENOM; CLU_043293_1_0_1; -.
DR InParanoid; Q8VYI1; -.
DR OMA; LFHVFFK; -.
DR OrthoDB; 1321777at2759; -.
DR PhylomeDB; Q8VYI1; -.
DR BioCyc; ARA:AT1G69640-MON; -.
DR BioCyc; MetaCyc:AT1G69640-MON; -.
DR UniPathway; UPA00786; -.
DR PRO; PR:Q8VYI1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYI1; baseline and differential.
DR Genevisible; Q8VYI1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0046520; P:sphingoid biosynthetic process; IMP:TAIR.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..260
FT /note="Sphinganine C4-monooxygenase 1"
FT /id="PRO_0000413166"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 99..235
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 114..118
FT /note="Histidine box-1"
FT MOTIF 128..132
FT /note="Histidine box-2"
FT MOTIF 207..213
FT /note="Histidine box-3"
SQ SEQUENCE 260 AA; 29819 MW; 77A4C672A2691418 CRC64;
MMMGFAVSDE LLGTVAPIVV YWLYSGIYVA LSSLESYRLH SKVEEEEKNL VSKSSVVKGV
LVQQVVQAVV AILLFTVTGS DAEADKAQQF SFLVLARQFV TAMIVLDTWQ YFMHRYMHQN
KFLYKHIHSQ HHRLIVPYAY GALYNHPVEG LLLDTIGGAL SFLVSGMSPR TSIFFFSFAT
IKTVDDHCGL WLPGNLFHMV FKNNSAYHDI HHQLYGTKYN FSQPFFVMWD RILGTYMPYS
LEKREDGGFE ARPTKEFKDD
