FAD4_ARATH
ID FAD4_ARATH Reviewed; 323 AA.
AC Q9SZ42; Q94EW9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fatty acid desaturase 4, chloroplastic {ECO:0000303|PubMed:19682287};
DE EC=1.14.19.43 {ECO:0000269|PubMed:19682287};
DE AltName: Full=Fatty acid desaturase A {ECO:0000303|PubMed:17796728};
DE Flags: Precursor;
GN Name=FAD4 {ECO:0000303|PubMed:19682287};
GN Synonyms=FADA {ECO:0000303|PubMed:17796728}; OrderedLocusNames=At4g27030;
GN ORFNames=F10M23.370;
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] OF 164-323.
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, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=17796728; DOI=10.1126/science.227.4688.763;
RA Browse J., McCourt P., Somerville C.R.;
RT "A mutant of Arabidopsis lacking a chloroplast-specific lipid.";
RL Science 227:763-765(1985).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Col-2;
RX PubMed=19682287; DOI=10.1111/j.1365-313x.2009.04001.x;
RA Gao J., Ajjawi I., Manoli A., Sawin A., Xu C., Froehlich J.E., Last R.L.,
RA Benning C.;
RT "FATTY ACID DESATURASE4 of Arabidopsis encodes a protein distinct from
RT characterized fatty acid desaturases.";
RL Plant J. 60:832-839(2009).
CC -!- FUNCTION: Fatty acid desaturase involved in the production of
CC chloroplast-specific phosphatidylglycerol molecular species containing
CC 16:1(3E). Catalyzes the formation of a trans double bond introduced
CC close to the carboxyl group of palmitic acid, which is specifically
CC esterified to the sn-2 glyceryl carbon of phosphatidylglycerol.
CC {ECO:0000269|PubMed:17796728, ECO:0000269|PubMed:19682287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced
CC [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(3E)-hexadec-3-enoyl]-
CC glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46764, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:86999,
CC ChEBI:CHEBI:87002; EC=1.14.19.43;
CC Evidence={ECO:0000269|PubMed:19682287};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:17796728}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:19682287}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but missing a chloroplast-
CC specific phosphatidylglycerol molecular species that carries a delta 3-
CC trans-hexadecenoic acid in the sn-2 position of its core glyceryl
CC moiety. {ECO:0000269|PubMed:17796728, ECO:0000269|PubMed:19682287}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase CarF family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK63863.1; 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; AL035440; CAB36549.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79558.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85286.1; -; Genomic_DNA.
DR EMBL; AF389291; AAK63863.1; ALT_INIT; mRNA.
DR EMBL; BT002250; AAN72261.1; -; mRNA.
DR PIR; T04826; T04826.
DR RefSeq; NP_194433.1; NM_118837.2.
DR AlphaFoldDB; Q9SZ42; -.
DR STRING; 3702.AT4G27030.1; -.
DR PaxDb; Q9SZ42; -.
DR PRIDE; Q9SZ42; -.
DR ProteomicsDB; 222441; -.
DR DNASU; 828811; -.
DR EnsemblPlants; AT4G27030.1; AT4G27030.1; AT4G27030.
DR GeneID; 828811; -.
DR Gramene; AT4G27030.1; AT4G27030.1; AT4G27030.
DR KEGG; ath:AT4G27030; -.
DR Araport; AT4G27030; -.
DR TAIR; locus:2116352; AT4G27030.
DR eggNOG; KOG3011; Eukaryota.
DR HOGENOM; CLU_065233_0_0_1; -.
DR InParanoid; Q9SZ42; -.
DR OMA; PSLKSTW; -.
DR OrthoDB; 1421561at2759; -.
DR PhylomeDB; Q9SZ42; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9SZ42; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ42; baseline and differential.
DR Genevisible; Q9SZ42; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102654; F:1-18:1-2-16:0-phosphatidylglycerol trans-3 desaturase activity; IDA:UniProtKB.
DR GO; GO:0102851; F:1-18:2-2-16:0-phosphatidylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0052637; F:delta 3-trans-hexadecenoic acid phosphatidylglycerol desaturase activity; IMP:TAIR.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:TAIR.
DR InterPro; IPR019547; Lipid_desat.
DR Pfam; PF10520; Lipid_desat; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 78..323
FT /note="Fatty acid desaturase 4, chloroplastic"
FT /id="PRO_0000429927"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 170..173
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 229..233
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 258..262
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36380 MW; DC0CFD8C6A57DA1F CRC64;
MAVSLPTKYP LRPITNIPKS HRPSLLRVRV TCSVTTTKPQ PNREKLLVEQ RTVNLPLSND
QSLQSTKPRP NREKLVVEQR LASPPLSNDP TLKSTWTHRL WVAAGCTTLF VSLAKSVIGG
FDSHLCLEPA LAGYAGYILA DLGSGVYHWA IDNYGDESTP VVGTQIEAFQ GHHKWPWTIT
RRQFANNLHA LAQVITFTVL PLDLAFNDPV FHGFVCTFAF CILFSQQFHA WAHGTKSKLP
PLVVALQDMG LLVSRRQHAE HHRAPYNNNY CIVSGAWNNV LDESKVFEAL EMVFYFQLGV
RPRSWSEPNS DWIEETEISN NQA
