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Sphinganine C4-monooxygenase 2 (EC 1.14.18.5) (Sphingoid C4-hydroxylase 2) (Sphingoid base hydroxylase 2)

 SBH2_ARATH              Reviewed;         259 AA.
Q9AST3; Q9M9T3;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-APR-2018, entry version 97.
RecName: Full=Sphinganine C4-monooxygenase 2;
EC=1.14.18.5 {ECO:0000269|PubMed:11297741};
AltName: Full=Sphingoid C4-hydroxylase 2;
AltName: Full=Sphingoid base hydroxylase 2;
Name=SBH2; OrderedLocusNames=At1g14290; ORFNames=F14L17.4, F14L17.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11297741; DOI=10.1016/S0014-5793(01)02332-8;
Sperling P., Ternes P., Moll H., Franke S., Zaehringer U., Heinz E.;
"Functional characterization of sphingolipid C4-hydroxylase genes from
Arabidopsis thaliana.";
FEBS Lett. 494:90-94(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=18612100; DOI=10.1105/tpc.107.057851;
Chen M., Markham J.E., Dietrich C.R., Jaworski J.G., Cahoon E.B.;
"Sphingolipid long-chain base hydroxylation is important for growth
and regulation of sphingolipid content and composition in
Arabidopsis.";
Plant Cell 20:1862-1878(2008).
-!- FUNCTION: Involved in sphingolipid trihydroxy long-chain base (4-
hydroxysphinganine) biosynthesis. Can use C18- and C20-sphinganine
as substrates to produce C18- and C20-phytosphinganines (D-ribo-2-
amino-1,3,4-trihydroxyoctadecane and -eicosane).
{ECO:0000269|PubMed:11297741, ECO:0000269|PubMed:18612100}.
-!- CATALYTIC ACTIVITY: A dihydroceramide + 2 ferrocytochrome b5 +
O(2) + 2 H(+) = a (4R)-4-hydroxysphinganine ceramide + 2
ferricytochrome b5 + H(2)O. {ECO:0000269|PubMed:11297741}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18612100}; Multi-pass membrane protein
{ECO:0000269|PubMed:18612100}.
-!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in flowers and
roots. {ECO:0000269|PubMed:18612100}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding.
-!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy
with SBH1. Sbh1 and sbh2 double mutants are severely dwarfed, do
not progress from vegetative to reproductive growth and have
enhanced expression of programmed cell death associated-genes.
{ECO:0000269|PubMed:18612100}.
-!- SIMILARITY: Belongs to the sterol desaturase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF43928.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC012188; AAF43928.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE29139.1; -; Genomic_DNA.
EMBL; AF361856; AAK32868.1; -; mRNA.
EMBL; BT001128; AAN64519.1; -; mRNA.
PIR; A86277; A86277.
RefSeq; NP_563944.1; NM_101295.5.
UniGene; At.28722; -.
ProteinModelPortal; Q9AST3; -.
BioGrid; 23230; 1.
STRING; 3702.AT1G14290.1; -.
PaxDb; Q9AST3; -.
EnsemblPlants; AT1G14290.1; AT1G14290.1; AT1G14290.
GeneID; 837990; -.
Gramene; AT1G14290.1; AT1G14290.1; AT1G14290.
KEGG; ath:AT1G14290; -.
Araport; AT1G14290; -.
TAIR; locus:2012512; AT1G14290.
eggNOG; KOG0874; Eukaryota.
eggNOG; COG3000; LUCA.
HOGENOM; HOG000203350; -.
KO; K04713; -.
OMA; ASTTQHF; -.
OrthoDB; EOG09360LJ6; -.
PhylomeDB; Q9AST3; -.
BioCyc; ARA:AT1G14290-MONOMER; -.
BioCyc; MetaCyc:AT1G14290-MONOMER; -.
BRENDA; 1.14.13.169; 399.
UniPathway; UPA00786; -.
PRO; PR:Q9AST3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9AST3; baseline and differential.
Genevisible; Q9AST3; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
GO; GO:0046520; P:sphingoid biosynthetic process; IMP:TAIR.
InterPro; IPR006694; Fatty_acid_hydroxylase.
Pfam; PF04116; FA_hydroxylase; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Lipid biosynthesis;
Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 259 Sphinganine C4-monooxygenase 2.
/FTId=PRO_0000413167.
TRANSMEM 10 30 Helical. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255}.
TRANSMEM 91 111 Helical. {ECO:0000255}.
MOTIF 113 117 Histidine box-1.
MOTIF 127 131 Histidine box-2.
MOTIF 206 212 Histidine box-3.
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


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