FAX1_ARATH
ID FAX1_ARATH Reviewed; 226 AA.
AC Q93V66; Q9M2L9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein FATTY ACID EXPORT 1, chloroplastic {ECO:0000303|PubMed:25646734};
DE Short=At-FAX1 {ECO:0000303|PubMed:25646734};
DE Flags: Precursor;
GN Name=FAX1 {ECO:0000303|PubMed:25646734};
GN OrderedLocusNames=At3g57280 {ECO:0000312|Araport:AT3G57280};
GN ORFNames=F28O9.130 {ECO:0000312|EMBL:CAB68134.1};
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 {ECO:0000312|EMBL:AAK96447.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 CLEAVAGE OF TRANSIT PEPTIDE AFTER SER-39, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [6]
RP INDUCTION BY SENESCENCE.
RX PubMed=22706448; DOI=10.1104/pp.112.196220;
RA Vogelmann K., Drechsel G., Bergler J., Subert C., Philippar K., Soll J.,
RA Engelmann J.C., Engelsdorf T., Voll L.M., Hoth S.;
RT "Early senescence and cell death in Arabidopsis saul1 mutants involves the
RT PAD4-dependent salicylic acid pathway.";
RL Plant Physiol. 159:1477-1487(2012).
RN [7]
RP FUNCTION, 3D-STRUCTURE MODELING, GENE FAMILY, NOMENCLATURE, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
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: Mediates the export of free fatty acid from the plastids.
CC Potentially prefers palmitic acid (C16:0) over oleic acid (C18:1) and
CC stearic acid (C18:0). Not involved in fatty acid activation. Required
CC for biogenesis of the outer pollen cell wall, in particular for the
CC assembly of exine and pollen coat and for the release of ketone wax
CC components. {ECO:0000269|PubMed:25646734}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:25646734}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, sepals and pollen.
CC {ECO:0000269|PubMed:25646734}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, with a peak
CC at early pollen development. {ECO:0000269|PubMed:25646734}.
CC -!- INDUCTION: Up-regulated upon induction of early leaf senescence.
CC {ECO:0000269|PubMed:22706448}.
CC -!- DISRUPTION PHENOTYPE: Reduced biomass and male sterility. Reduced size,
CC thinner inflorescence stalks and flowers producing short siliques
CC containing almost no seeds. Small vascular bundles with reduced
CC secondary cell walls and modified cuticular wax composition with
CC strongly reduced content in C29-ketone wax components.
CC {ECO:0000269|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=CAB68134.1; Type=Erroneous gene model prediction; 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; AL137080; CAB68134.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79635.1; -; Genomic_DNA.
DR EMBL; AY039525; AAK62581.1; -; mRNA.
DR EMBL; AY052733; AAK96447.1; -; mRNA.
DR EMBL; AY085316; AAM62547.1; -; mRNA.
DR PIR; T45806; T45806.
DR RefSeq; NP_567046.1; NM_115588.4.
DR AlphaFoldDB; Q93V66; -.
DR IntAct; Q93V66; 3.
DR STRING; 3702.AT3G57280.1; -.
DR TCDB; 2.A.126.2.4; the fatty acid exporter (fax) family.
DR PaxDb; Q93V66; -.
DR PRIDE; Q93V66; -.
DR ProteomicsDB; 230959; -.
DR EnsemblPlants; AT3G57280.1; AT3G57280.1; AT3G57280.
DR GeneID; 824895; -.
DR Gramene; AT3G57280.1; AT3G57280.1; AT3G57280.
DR KEGG; ath:AT3G57280; -.
DR Araport; AT3G57280; -.
DR TAIR; locus:2082578; AT3G57280.
DR eggNOG; KOG4267; Eukaryota.
DR HOGENOM; CLU_096652_0_1_1; -.
DR InParanoid; Q93V66; -.
DR OMA; ISACMLC; -.
DR OrthoDB; 1413005at2759; -.
DR PhylomeDB; Q93V66; -.
DR PRO; PR:Q93V66; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93V66; baseline and differential.
DR Genevisible; Q93V66; 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; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; 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; IGI:TAIR.
DR GO; GO:1902001; P:fatty acid transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IGI:TAIR.
DR GO; GO:0055088; P:lipid homeostasis; IMP:TAIR.
DR GO; GO:0071668; P:plant-type cell wall assembly; IMP:TAIR.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12766230"
FT CHAIN 40..226
FT /note="Protein FATTY ACID EXPORT 1, chloroplastic"
FT /id="PRO_0000432801"
FT TRANSMEM 130..150
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24347 MW; EFFC56EB5397E909 CRC64;
MASQISQLAC FSSTNRQFHF QSRSFPCPMI RPQSFVVKSV DGNSSETPAS LSYTAEVSKP
VVEKTSKPYS TVDETATNKE SITEPVEEDV ATQPIRAAKI HDFCFGIPYG GLVVSGGLLG
FAFSRNLTSL STGVLYGGGL LALSTLSLKI WREGKSSFPY ILGQAVLSAV VFWKNFTAYS
MTKKLFPAGV FAVISACMLC FYSYVVLSGG NPPPKKLKPS ATSPSY
