FAX6_ARATH
ID FAX6_ARATH Reviewed; 119 AA.
AC Q9LJU6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein FATTY ACID EXPORT 6 {ECO:0000303|PubMed:25646734};
DE Short=At-FAX6 {ECO:0000303|PubMed:25646734};
GN Name=FAX6 {ECO:0000303|PubMed:25646734};
GN OrderedLocusNames=At3g20510 {ECO:0000312|Araport:AT3G20510};
GN ORFNames=K10D20.5 {ECO:0000312|EMBL:BAB01160.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, NOMENCLATURE, AND 3D-STRUCTURE MODELING.
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.
CC {ECO:0000250|UniProtKB:Q93V66}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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}.
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DR EMBL; AP000410; BAB01160.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76389.1; -; Genomic_DNA.
DR EMBL; BT010505; AAQ65128.1; -; mRNA.
DR EMBL; AK176567; BAD44330.1; -; mRNA.
DR EMBL; AK176851; BAD44614.1; -; mRNA.
DR RefSeq; NP_188687.1; NM_112943.5.
DR AlphaFoldDB; Q9LJU6; -.
DR IntAct; Q9LJU6; 9.
DR STRING; 3702.AT3G20510.1; -.
DR PaxDb; Q9LJU6; -.
DR PRIDE; Q9LJU6; -.
DR ProteomicsDB; 231011; -.
DR EnsemblPlants; AT3G20510.1; AT3G20510.1; AT3G20510.
DR GeneID; 821597; -.
DR Gramene; AT3G20510.1; AT3G20510.1; AT3G20510.
DR KEGG; ath:AT3G20510; -.
DR Araport; AT3G20510; -.
DR TAIR; locus:2085780; AT3G20510.
DR eggNOG; KOG4267; Eukaryota.
DR HOGENOM; CLU_096652_5_0_1; -.
DR InParanoid; Q9LJU6; -.
DR OMA; TYNRYLM; -.
DR OrthoDB; 1642026at2759; -.
DR PhylomeDB; Q9LJU6; -.
DR PRO; PR:Q9LJU6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJU6; baseline and differential.
DR Genevisible; Q9LJU6; AT.
DR GO; GO:0009706; C:chloroplast inner membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; TAS: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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
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 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..119
FT /note="Protein FATTY ACID EXPORT 6"
FT /id="PRO_0000432806"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 119 AA; 12511 MW; 68B1F641BC424EAC CRC64;
MHDFCFTIPY GMLLIGGGFI GYMKKGSITS FAGGAGTGLL LILAGYISLK AFEKKKNSTI
AMVLQTVIAA ALTLVMGQRY LLTGKIMPAG LVAGISALMT CFYVYKIATG GNKFPAKAE
