PILS6_ARATH
ID PILS6_ARATH Reviewed; 431 AA.
AC Q9LZN2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein PIN-LIKES 6 {ECO:0000303|PubMed:22504182};
DE AltName: Full=Auxin efflux carrier-like protein 6 {ECO:0000303|PubMed:22504182};
GN Name=PILS6 {ECO:0000303|PubMed:22504182};
GN OrderedLocusNames=At5g01990 {ECO:0000312|Araport:AT5G01990};
GN ORFNames=T7H20_40 {ECO:0000312|EMBL:CAB82972.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 TISSUE SPECIFICITY, INDUCTION BY AUXIN, GENE FAMILY, NOMENCLATURE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22504182; DOI=10.1038/nature11001;
RA Barbez E., Kubes M., Rolcik J., Beziat C., Pencik A., Wang B.,
RA Rosquete M.R., Zhu J., Dobrev P.I., Lee Y., Zazimalova E., Petrasek J.,
RA Geisler M., Friml J., Kleine-Vehn J.;
RT "A novel putative auxin carrier family regulates intracellular auxin
RT homeostasis in plants.";
RL Nature 485:119-122(2012).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23091477; DOI=10.3389/fpls.2012.00227;
RA Feraru E., Vosolsobe S., Feraru M.I., Petrasek J., Kleine-Vehn J.;
RT "Evolution and structural diversification of PILS putative auxin carriers
RT in plants.";
RL Front. Plant Sci. 3:227-227(2012).
CC -!- FUNCTION: Involved in cellular auxin homeostasis by regulating auxin
CC metabolism. Regulates intracellular auxin accumulation at the
CC endoplasmic reticulum and thus auxin availability for nuclear auxin
CC signaling. {ECO:0000305|PubMed:22504182}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22504182}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, rosette and cauline leaves,
CC stems and flowers. {ECO:0000269|PubMed:22504182}.
CC -!- INDUCTION: Up-regulated by auxin application.
CC {ECO:0000269|PubMed:22504182}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.2) family.
CC {ECO:0000305}.
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DR EMBL; AL162508; CAB82972.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90417.1; -; Genomic_DNA.
DR PIR; T48220; T48220.
DR RefSeq; NP_195819.1; NM_120277.3.
DR AlphaFoldDB; Q9LZN2; -.
DR STRING; 3702.AT5G01990.1; -.
DR PaxDb; Q9LZN2; -.
DR PRIDE; Q9LZN2; -.
DR ProteomicsDB; 235001; -.
DR EnsemblPlants; AT5G01990.1; AT5G01990.1; AT5G01990.
DR GeneID; 830729; -.
DR Gramene; AT5G01990.1; AT5G01990.1; AT5G01990.
DR KEGG; ath:AT5G01990; -.
DR Araport; AT5G01990; -.
DR TAIR; locus:2185123; AT5G01990.
DR eggNOG; KOG2722; Eukaryota.
DR HOGENOM; CLU_044945_0_0_1; -.
DR InParanoid; Q9LZN2; -.
DR OMA; VLWFTMM; -.
DR OrthoDB; 1055578at2759; -.
DR PhylomeDB; Q9LZN2; -.
DR PRO; PR:Q9LZN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZN2; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0080162; P:endoplasmic reticulum to cytosol auxin transport; IEA:InterPro.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR InterPro; IPR004776; Mem_trans.
DR InterPro; IPR039305; PILS2/6.
DR PANTHER; PTHR31419; PTHR31419; 1.
DR Pfam; PF03547; Mem_trans; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..431
FT /note="Protein PIN-LIKES 6"
FT /id="PRO_0000436501"
FT TOPO_DOM 1..29
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..93
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..169
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..306
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..376
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..431
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
SQ SEQUENCE 431 AA; 46465 MW; 17129A921784CB74 CRC64;
MIARILAALA DSMEMPVAAG GGSVLGTIKI AVMPIAKVFT MCFLGLLMAS KYVNILPPSG
RKLLNGLVFS LLLPCLIFSQ LGQAVTLQKM LQWWFIPVNV VLGTISGSII GFIVASIVRP
PYPYFKFTII QIGVGNIGNV PLVLLAALCR DTSNPFGDSE KCSIDGTAYI SFGQWVGAII
LYTYVYQMFA PPPEGFDAEE ENLALKTLPV DAAPEQVPLL TQNFPKDFSP TQDLLPVQST
EPRGRGVSRK GKIAQIFVFL YEKLKLKQIV QPAIVASILA MILGAIPFTK KLIFTNGAPL
FFFTDSCMIL GDAMIPCILL ALGGNLINGP GSSKLGFKTT AAIIIGRLVL VPPVGLGIVT
VADKLGFLPA DDKMFRFVLL LQHTMPTSVL SGAVANLRGC GRESAAVLFW VHIFAIFSMA
GWMVLYINIL F
