FAD3E_ARATH
ID FAD3E_ARATH Reviewed; 386 AA.
AC P48623; Q0WM09;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Acyl-lipid omega-3 desaturase (cytochrome b5), endoplasmic reticulum {ECO:0000303|PubMed:8029334};
DE EC=1.14.19.25 {ECO:0000269|PubMed:8029334};
DE AltName: Full=Omega-3 fatty acid desaturase 3, endoplasmic reticulum {ECO:0000303|PubMed:8029334};
GN Name=FAD3 {ECO:0000303|PubMed:8029334};
GN OrderedLocusNames=At2g29980 {ECO:0000312|Araport:AT2G29980};
GN ORFNames=F23F1.10 {ECO:0000312|EMBL:AAC31854.1};
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 [GENOMIC DNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8029334; DOI=10.1104/pp.103.2.467;
RA Yadav N.S., Wierzbicki A., Aegerter M., Caster C.S., Perez-Grau L.,
RA Kinney A.J., Hitz W.D., Booth J.R. Jr., Schweiger B., Stecca K.L.,
RA Allen S.M., Blackwell M., Reiter R.S., Carlson T.J., Russell S.H.,
RA Feldmann K.A., Pierce J., Browse J.;
RT "Cloning of higher plant omega-3 fatty acid desaturases.";
RL Plant Physiol. 103:467-476(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RA Watahiki M.C., Yamamoto K.T.;
RT "cDNA cloning of fatty acid desaturase from Arabidopsis thaliana.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8066143; DOI=10.1104/pp.105.2.767;
RA Nishiuchi T., Nishimura M., Arondel V., Iba K.;
RT "Genomic nucleotide sequence of a gene encoding a microsomal omega-3 fatty
RT acid desaturase from Arabidopsis thaliana.";
RL Plant Physiol. 105:767-768(1994).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-386.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=8102138; DOI=10.1016/s0021-9258(19)85427-3;
RA Browse J., McConn M., James D. Jr., Miquel M.;
RT "Mutants of Arabidopsis deficient in the synthesis of alpha-linolenate.
RT Biochemical and genetic characterization of the endoplasmic reticulum
RT linoleoyl desaturase.";
RL J. Biol. Chem. 268:16345-16351(1993).
CC -!- FUNCTION: Microsomal (ER) omega-3 fatty acid desaturase introduces the
CC third double bond in the biosynthesis of 18:3 fatty acids, important
CC constituents of plant membranes. It is thought to use cytochrome b5 as
CC an electron donor and to act on fatty acids esterified to
CC phosphatidylcholine and, possibly, other phospholipids.
CC {ECO:0000269|PubMed:8029334, ECO:0000269|PubMed:8102138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46404, 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:88351,
CC ChEBI:CHEBI:90078; EC=1.14.19.25;
CC Evidence={ECO:0000269|PubMed:8029334};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:8029334}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:8029334}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=P48623-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Abundant in leaves and seedlings. Barely detectable
CC in root tissue. {ECO:0000269|PubMed:8029334}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; L22931; AAA61778.1; -; Genomic_DNA.
DR EMBL; D17579; BAA04505.1; -; mRNA.
DR EMBL; D26508; BAA05514.1; -; Genomic_DNA.
DR EMBL; AC004680; AAC31854.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08330.1; -; Genomic_DNA.
DR EMBL; AY063966; AAL36322.1; -; mRNA.
DR EMBL; AY096462; AAM20102.1; -; mRNA.
DR EMBL; AK230026; BAF01848.1; -; mRNA.
DR PIR; JQ2335; JQ2335.
DR RefSeq; NP_180559.1; NM_128552.4. [P48623-1]
DR AlphaFoldDB; P48623; -.
DR BioGRID; 2898; 6.
DR IntAct; P48623; 3.
DR STRING; 3702.AT2G29980.1; -.
DR PaxDb; P48623; -.
DR ProteomicsDB; 222521; -. [P48623-1]
DR EnsemblPlants; AT2G29980.1; AT2G29980.1; AT2G29980. [P48623-1]
DR GeneID; 817548; -.
DR Gramene; AT2G29980.1; AT2G29980.1; AT2G29980. [P48623-1]
DR KEGG; ath:AT2G29980; -.
DR Araport; AT2G29980; -.
DR TAIR; locus:2005508; AT2G29980.
DR eggNOG; ENOG502QTIC; Eukaryota.
DR HOGENOM; CLU_033094_1_0_1; -.
DR InParanoid; P48623; -.
DR OMA; PYDCWRR; -.
DR PhylomeDB; P48623; -.
DR BioCyc; ARA:AT2G29980-MON; -.
DR BioCyc; MetaCyc:AT2G29980-MON; -.
DR BRENDA; 1.14.19.25; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:P48623; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P48623; baseline and differential.
DR Genevisible; P48623; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP: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:0102872; F:1-16:0-2-18:2-phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102859; F:1-18:1-2-18:2-phosphatidylcholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0102856; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102862; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0042389; F:omega-3 fatty acid desaturase activity; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:TAIR.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Acyl-lipid omega-3 desaturase (cytochrome b5),
FT endoplasmic reticulum"
FT /id="PRO_0000185411"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..105
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 137..141
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 304..308
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 44077 MW; 6A7EA2A692B85164 CRC64;
MVVAMDQRTN VNGDPGAGDR KKEERFDPSA QPPFKIGDIR AAIPKHCWVK SPLRSMSYVV
RDIIAVAALA IAAVYVDSWF LWPLYWAAQG TLFWAIFVLG HDCGHGSFSD IPLLNSVVGH
ILHSFILVPY HGWRISHRTH HQNHGHVEND ESWVPLPERV YKKLPHSTRM LRYTVPLPML
AYPLYLCYRS PGKEGSHFNP YSSLFAPSER KLIATSTTCW SIMFVSLIAL SFVFGPLAVL
KVYGVPYIIF VMWLDAVTYL HHHGHDEKLP WYRGKEWSYL RGGLTTIDRD YGIFNNIHHD
IGTHVIHHLF PQIPHYHLVD ATKAAKHVLG RYYREPKTSG AIPIHLVESL VASIKKDHYV
SDTGDIVFYE TDPDLYVYAS DKSKIN
