FAX5_ARATH
ID FAX5_ARATH Reviewed; 119 AA.
AC Q9C6T7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein FATTY ACID EXPORT 5 {ECO:0000303|PubMed:25646734};
DE Short=At-FAX5 {ECO:0000303|PubMed:25646734};
GN Name=FAX5 {ECO:0000303|PubMed:25646734};
GN OrderedLocusNames=At1g50740 {ECO:0000312|Araport:AT1G50740};
GN ORFNames=F4M15.3 {ECO:0000312|EMBL:AAG50780.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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; AC079027; AAG50780.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32586.1; -; Genomic_DNA.
DR EMBL; AY074495; AAL69479.1; -; mRNA.
DR EMBL; AY096728; AAM20362.1; -; mRNA.
DR EMBL; AY087361; AAM64911.1; -; mRNA.
DR PIR; C96544; C96544.
DR RefSeq; NP_564579.1; NM_103956.4.
DR AlphaFoldDB; Q9C6T7; -.
DR IntAct; Q9C6T7; 9.
DR STRING; 3702.AT1G50740.1; -.
DR PaxDb; Q9C6T7; -.
DR PRIDE; Q9C6T7; -.
DR EnsemblPlants; AT1G50740.1; AT1G50740.1; AT1G50740.
DR GeneID; 841496; -.
DR Gramene; AT1G50740.1; AT1G50740.1; AT1G50740.
DR KEGG; ath:AT1G50740; -.
DR Araport; AT1G50740; -.
DR TAIR; locus:2033177; AT1G50740.
DR eggNOG; KOG4267; Eukaryota.
DR HOGENOM; CLU_096652_5_0_1; -.
DR InParanoid; Q9C6T7; -.
DR OMA; MGTRYKK; -.
DR OrthoDB; 1642026at2759; -.
DR PhylomeDB; Q9C6T7; -.
DR PRO; PR:Q9C6T7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6T7; baseline and differential.
DR Genevisible; Q9C6T7; AT.
DR GO; GO:0009706; C:chloroplast inner membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
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 5"
FT /id="PRO_0000432805"
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 85..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 119 AA; 12512 MW; E51ECBED94E99F32 CRC64;
MHDFCFTIPY GILLIVGGFI GYLKKGSIAS LAGGAGTGLL VVLAGFISLK AFEKKKTSLL
ATLLETVIAA ALTFVMGQRF LQTQKIMPAA LVAGISALMT CFYVYKIATG GNHIPPKAE
