PILS5_ARATH
ID PILS5_ARATH Reviewed; 396 AA.
AC Q9SHL8; B9DG37; Q8LGC5;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein PIN-LIKES 5 {ECO:0000303|PubMed:22504182};
DE AltName: Full=Auxin efflux carrier-like protein 5 {ECO:0000303|PubMed:22504182};
GN Name=PILS5 {ECO:0000303|PubMed:22504182};
GN OrderedLocusNames=At2g17500 {ECO:0000312|Araport:AT2G17500};
GN ORFNames=MJB20.6 {ECO:0000312|EMBL:AAD32907.1};
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-210.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, GENE FAMILY,
RP NOMENCLATURE, DISRUPTION PHENOTYPE, AND 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 [7]
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:0000269|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, cauline leaves and flowers.
CC {ECO:0000269|PubMed:22504182}.
CC -!- INDUCTION: Up-regulated by auxin application.
CC {ECO:0000269|PubMed:22504182}.
CC -!- DISRUPTION PHENOTYPE: Increased root growth and lateral root
CC initiation. {ECO:0000269|PubMed:22504182}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.2) family.
CC {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; AC007584; AAD32907.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06634.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06635.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06636.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06637.1; -; Genomic_DNA.
DR EMBL; AK226321; BAE98473.1; -; mRNA.
DR EMBL; AY084347; AAM60930.1; -; mRNA.
DR EMBL; AK317010; BAH19704.1; -; mRNA.
DR PIR; H84552; H84552.
DR RefSeq; NP_001031363.1; NM_001036286.3.
DR RefSeq; NP_565417.1; NM_127304.3.
DR RefSeq; NP_849964.1; NM_179633.4.
DR RefSeq; NP_973479.1; NM_201750.2.
DR AlphaFoldDB; Q9SHL8; -.
DR STRING; 3702.AT2G17500.2; -.
DR PaxDb; Q9SHL8; -.
DR PRIDE; Q9SHL8; -.
DR ProteomicsDB; 235017; -.
DR EnsemblPlants; AT2G17500.1; AT2G17500.1; AT2G17500.
DR EnsemblPlants; AT2G17500.2; AT2G17500.2; AT2G17500.
DR EnsemblPlants; AT2G17500.3; AT2G17500.3; AT2G17500.
DR EnsemblPlants; AT2G17500.4; AT2G17500.4; AT2G17500.
DR GeneID; 816256; -.
DR Gramene; AT2G17500.1; AT2G17500.1; AT2G17500.
DR Gramene; AT2G17500.2; AT2G17500.2; AT2G17500.
DR Gramene; AT2G17500.3; AT2G17500.3; AT2G17500.
DR Gramene; AT2G17500.4; AT2G17500.4; AT2G17500.
DR KEGG; ath:AT2G17500; -.
DR Araport; AT2G17500; -.
DR TAIR; locus:2053908; AT2G17500.
DR eggNOG; KOG2722; Eukaryota.
DR HOGENOM; CLU_044945_0_0_1; -.
DR InParanoid; Q9SHL8; -.
DR OMA; IFGAVRW; -.
DR OrthoDB; 1055578at2759; -.
DR PhylomeDB; Q9SHL8; -.
DR PRO; PR:Q9SHL8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHL8; 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:0010329; F:auxin efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0010252; P:auxin homeostasis; IDA:UniProtKB.
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:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:0040009; P:regulation of growth rate; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR InterPro; IPR004776; Mem_trans.
DR InterPro; IPR045033; PILS1/3/4/5/7.
DR PANTHER; PTHR31651; PTHR31651; 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..396
FT /note="Protein PIN-LIKES 5"
FT /id="PRO_0000436500"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..73
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..144
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..273
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..337
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23091477"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..396
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:23091477"
FT CONFLICT 216
FT /note="K -> E (in Ref. 4; AAM60930)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="V -> A (in Ref. 4; AAM60930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43394 MW; 81A78C8A017CF67D CRC64;
MGFWSLLEVA SMPVIQVLFM SLVGAFMASD RCKLFPVEAR NSMNKVVFVL FAPALMFANL
AQTVTLEDII SWWFMPVNMG LTFLIGGLLG WLVVKILKPP PYLEGLIVAT CSAGNMGNLP
IILVPAICDE DKSPFGNRSV CRTVGLSYAS FSMALGGFYI WTYTFRLIKG SAMKVQAIEE
SEKIAIKSSN SDLEADHKTH LLGAPEDKEN KVVKEKTGFW RKGVDFLHEI LEELLAPPTL
GAIIGFIFGA VRWLRNLIIG DDAPLRIVQS TAKLLGDGTI PCMTIILGGN LIQGLRSSAV
KPMVVLGIVC VRYIAMPIIG IGIVLTAANL GFLPADPLFQ YVLMLQFTLP PAMNIGTMTQ
LYNVAQDECS VLMLWTYLVA ILALTVWSTI FLHLLV