FAX3_ARATH
ID FAX3_ARATH Reviewed; 335 AA.
AC Q9ZVH7; Q8LCL4; Q94CA2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein FATTY ACID EXPORT 3, chloroplastic {ECO:0000303|PubMed:25646734};
DE Short=At-FAX3 {ECO:0000303|PubMed:25646734};
DE Flags: Precursor;
GN Name=FAX3 {ECO:0000303|PubMed:25646734};
GN OrderedLocusNames=At2g38550 {ECO:0000312|Araport:AT2G38550};
GN ORFNames=T6A23.25 {ECO:0000312|EMBL:AAC67363.2};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, NOMENCLATURE, AND DEVELOPMENTAL STAGE.
RX PubMed=25646734; DOI=10.1371/journal.pbio.1002053;
RA Li N., Guegel I.L., Giavalisco P., Zeisler V., Schreiber L., Soll J.,
RA Philippar K.;
RT "FAX1, a novel membrane protein mediating plastid fatty acid export.";
RL PLoS Biol. 13:E1002053-E1002053(2015).
CC -!- FUNCTION: May be involved in free fatty acids export from the plastids.
CC {ECO:0000250|UniProtKB:Q93V66}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during seed development and
CC germination. {ECO:0000305|PubMed:25646734}.
CC -!- MISCELLANEOUS: For all TMEM14 proteins, 4 hydrophobic alpha-helical
CC domains are predicted. However, NMR structure determination of the
CC human TMEM14A showed that only 3 of these helices are membrane-spaning
CC while the amphiphilic N-terminal helix is probably located at the lipid
CC micelle-water interface. {ECO:0000305|PubMed:25646734}.
CC -!- SIMILARITY: Belongs to the TMEM14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005499; AAC67363.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09549.1; -; Genomic_DNA.
DR EMBL; AY035020; AAK59525.1; -; mRNA.
DR EMBL; AY133772; AAM91706.1; -; mRNA.
DR EMBL; AY086533; AAM63598.1; ALT_INIT; mRNA.
DR PIR; D84806; D84806.
DR RefSeq; NP_565892.1; NM_129412.4.
DR AlphaFoldDB; Q9ZVH7; -.
DR STRING; 3702.AT2G38550.1; -.
DR PaxDb; Q9ZVH7; -.
DR PRIDE; Q9ZVH7; -.
DR ProteomicsDB; 230961; -.
DR EnsemblPlants; AT2G38550.1; AT2G38550.1; AT2G38550.
DR GeneID; 818437; -.
DR Gramene; AT2G38550.1; AT2G38550.1; AT2G38550.
DR KEGG; ath:AT2G38550; -.
DR Araport; AT2G38550; -.
DR TAIR; locus:2064206; AT2G38550.
DR eggNOG; ENOG502QQ5P; Eukaryota.
DR HOGENOM; CLU_062320_0_0_1; -.
DR InParanoid; Q9ZVH7; -.
DR OMA; YIYRIVL; -.
DR OrthoDB; 1381286at2759; -.
DR PhylomeDB; Q9ZVH7; -.
DR PRO; PR:Q9ZVH7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVH7; baseline and differential.
DR Genevisible; Q9ZVH7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA: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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0015908; P:fatty acid transport; IGI:TAIR.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IMP:TAIR.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:TAIR.
DR Gene3D; 1.10.10.1740; -; 1.
DR InterPro; IPR005349; TMEM14.
DR InterPro; IPR044890; TMEM14_sf.
DR PANTHER; PTHR12668; PTHR12668; 1.
DR Pfam; PF03647; Tmemb_14; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Coiled coil; Membrane; Plastid; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..335
FT /note="Protein FATTY ACID EXPORT 3, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432803"
FT TRANSMEM 205..225
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT REGION 82..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..160
FT /evidence="ECO:0000255"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 36701 MW; 4554BBA24BC254AE CRC64;
MMSIPMELMS IRNPNSTLLY RAHSRPPVKL CAPPRSLLPS RRHFSAPRAV VSYPGIRFGF
TSPEVLLNRS VVAFAASHED SGESGVEVGK EKSDIDVEDD TSKEAWKQTL ESFKEQVSKM
QSVSSEAYSV NSQKAMTVLK ETSEQLRIQA EKAKEELGTK AKVVSEEGRE YILKAAEESP
SDVKEIVEAF ASTEDLKNVS RANDFHVGIP YGLLLLVGGF INFMVSGSIP AIRFGVILGG
ALFALSLASL KSHRKGESST KFLKGQMAIV AIIFLRELRL LLSQKSTFLG FFTTLTSGGV
LGFYLYKMVV KREKGPTLED GGEDESSDGF VRSEG
