SBH2_ARATH
ID SBH2_ARATH Reviewed; 259 AA.
AC Q9AST3; Q9M9T3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sphinganine C4-monooxygenase 2;
DE EC=1.14.18.5 {ECO:0000269|PubMed:11297741};
DE AltName: Full=Sphingoid C4-hydroxylase 2;
DE AltName: Full=Sphingoid base hydroxylase 2;
GN Name=SBH2; OrderedLocusNames=At1g14290; ORFNames=F14L17.4, F14L17.5;
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 SBH1. 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=AAF43928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC012188; AAF43928.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29139.1; -; Genomic_DNA.
DR EMBL; AF361856; AAK32868.1; -; mRNA.
DR EMBL; BT001128; AAN64519.1; -; mRNA.
DR PIR; A86277; A86277.
DR RefSeq; NP_563944.1; NM_101295.5.
DR AlphaFoldDB; Q9AST3; -.
DR SMR; Q9AST3; -.
DR BioGRID; 23230; 1.
DR IntAct; Q9AST3; 1.
DR STRING; 3702.AT1G14290.1; -.
DR PaxDb; Q9AST3; -.
DR PRIDE; Q9AST3; -.
DR ProteomicsDB; 228131; -.
DR EnsemblPlants; AT1G14290.1; AT1G14290.1; AT1G14290.
DR GeneID; 837990; -.
DR Gramene; AT1G14290.1; AT1G14290.1; AT1G14290.
DR KEGG; ath:AT1G14290; -.
DR Araport; AT1G14290; -.
DR TAIR; locus:2012512; AT1G14290.
DR eggNOG; KOG0874; Eukaryota.
DR HOGENOM; CLU_043293_1_0_1; -.
DR OMA; ASTTQHF; -.
DR OrthoDB; 1321777at2759; -.
DR PhylomeDB; Q9AST3; -.
DR BioCyc; ARA:AT1G14290-MON; -.
DR BioCyc; MetaCyc:AT1G14290-MON; -.
DR BRENDA; 1.14.18.5; 399.
DR UniPathway; UPA00786; -.
DR PRO; PR:Q9AST3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9AST3; baseline and differential.
DR Genevisible; Q9AST3; 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..259
FT /note="Sphinganine C4-monooxygenase 2"
FT /id="PRO_0000413167"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 98..234
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 113..117
FT /note="Histidine box-1"
FT MOTIF 127..131
FT /note="Histidine box-2"
FT MOTIF 206..212
FT /note="Histidine box-3"
SQ SEQUENCE 259 AA; 29831 MW; DA20B5DC0F0F30EE CRC64;
MMSFVISDEF LGTFVPILVY WVYSGMYICL GSLDKYRLHS KIDEDEKNLV SKSAVVKGVL
LQQTLQAIIS VILFKITGSD ADAATTQQFS ILLLARQFII AMLVIDTWQY FIHRYMHLNK
FLYKHIHSQH HRLIVPYSYG ALYNHPLEGL LLDTIGGALS FLFSGMSPRT AIFFFSFATI
KTVDDHCGLW LPGNPFHIFF SNNSAYHDVH HQLYGTKYNF SQPFFVMWDR ILGTYLPYSL
EKRANGGFET RPIKVSKDE
