FAX7_ARATH
ID FAX7_ARATH Reviewed; 108 AA.
AC O64847;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Protein FATTY ACID EXPORT 7 {ECO:0000303|PubMed:25646734};
DE Short=At-FAX7 {ECO:0000303|PubMed:25646734};
GN Name=FAX7 {ECO:0000303|PubMed:25646734};
GN OrderedLocusNames=At2g26240 {ECO:0000312|Araport:AT2G26240};
GN ORFNames=T1D16.12 {ECO:0000312|EMBL:AAC14534.1};
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 [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 GENE FAMILY, AND NOMENCLATURE.
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; AC004484; AAC14534.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07812.1; -; Genomic_DNA.
DR EMBL; AY072431; AAL62423.1; -; mRNA.
DR EMBL; BT000271; AAN15590.1; -; mRNA.
DR PIR; A84658; A84658.
DR RefSeq; NP_180192.1; NM_128181.4.
DR AlphaFoldDB; O64847; -.
DR STRING; 3702.AT2G26240.1; -.
DR PaxDb; O64847; -.
DR EnsemblPlants; AT2G26240.1; AT2G26240.1; AT2G26240.
DR GeneID; 817164; -.
DR Gramene; AT2G26240.1; AT2G26240.1; AT2G26240.
DR KEGG; ath:AT2G26240; -.
DR Araport; AT2G26240; -.
DR TAIR; locus:2057721; AT2G26240.
DR eggNOG; KOG4267; Eukaryota.
DR HOGENOM; CLU_096652_5_2_1; -.
DR InParanoid; O64847; -.
DR OMA; ANSHKIM; -.
DR OrthoDB; 1642026at2759; -.
DR PhylomeDB; O64847; -.
DR PRO; PR:O64847; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64847; baseline and differential.
DR Genevisible; O64847; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA: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 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..108
FT /note="Protein FATTY ACID EXPORT 7"
FT /id="PRO_0000221177"
FT TRANSMEM 32..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 108 AA; 11108 MW; 7288CD81200763C0 CRC64;
MDSSLSQKFT LAYASLLGVG GLMGYLKRGS KISLVAGGGS AALFYYVYTE LPGNPVLASS
IGIVGSAALT GMMGSRYLRT RKVVPAGLVS VVSLVMTGAY LHGLIRSS
