PIN5_ARATH
ID PIN5_ARATH Reviewed; 351 AA.
AC Q9FFD0;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Auxin efflux carrier component 5 {ECO:0000303|PubMed:15817418};
DE Short=AtPIN5 {ECO:0000303|PubMed:15817418};
GN Name=PIN5 {ECO:0000303|PubMed:15817418}; Synonyms=AEH2, PIN8;
GN OrderedLocusNames=At5g16530 {ECO:0000312|Araport:AT5G16530};
GN ORFNames=MQK4.28 {ECO:0000312|EMBL:BAB09622.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15817418; DOI=10.1016/j.tplants.2005.02.009;
RA Paponov I.A., Teale W.D., Trebar M., Blilou I., Palme K.;
RT "The PIN auxin efflux facilitators: evolutionary and functional
RT perspectives.";
RL Trends Plant Sci. 10:170-177(2005).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19506555; DOI=10.1038/nature08066;
RA Mravec J., Skupa P., Bailly A., Hoyerova K., Krecek P., Bielach A.,
RA Petrasek J., Zhang J., Gaykova V., Stierhof Y.D., Dobrev P.I.,
RA Schwarzerova K., Rolcik J., Seifertova D., Luschnig C., Benkova E.,
RA Zazimalova E., Geisler M., Friml J.;
RT "Subcellular homeostasis of phytohormone auxin is mediated by the ER-
RT localized PIN5 transporter.";
RL Nature 459:1136-1140(2009).
RN [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20439545; DOI=10.1104/pp.110.156505;
RA Ganguly A., Lee S.H., Cho M., Lee O.R., Yoo H., Cho H.T.;
RT "Differential auxin-transporting activities of PIN-FORMED proteins in
RT Arabidopsis root hair cells.";
RL Plant Physiol. 153:1046-1061(2010).
RN [6]
RP FUNCTION.
RX PubMed=22760640; DOI=10.1038/ncomms1941;
RA Ding Z., Wang B., Moreno I., Duplakova N., Simon S., Carraro N.,
RA Reemmer J., Pencik A., Chen X., Tejos R., Skupa P., Pollmann S., Mravec J.,
RA Petrasek J., Zazimalova E., Honys D., Rolcik J., Murphy A., Orellana A.,
RA Geisler M., Friml J.;
RT "ER-localized auxin transporter PIN8 regulates auxin homeostasis and male
RT gametophyte development in Arabidopsis.";
RL Nat. Commun. 3:941-941(2012).
RN [7]
RP FUNCTION.
RX PubMed=22990451; DOI=10.4161/psb.21953;
RA Dal Bosco C., Dovzhenko A., Palme K.;
RT "Intracellular auxin transport in pollen: PIN8, PIN5 and PILS5.";
RL Plant Signal. Behav. 7:1504-1505(2012).
RN [8]
RP FUNCTION.
RX PubMed=23437008; DOI=10.1371/journal.pgen.1003294;
RA Sawchuk M.G., Edgar A., Scarpella E.;
RT "Patterning of leaf vein networks by convergent auxin transport pathways.";
RL PLoS Genet. 9:E1003294-E1003294(2013).
RN [9]
RP FUNCTION.
RX PubMed=24304505; DOI=10.4161/psb.27205;
RA Sawchuk M.G., Scarpella E.;
RT "Control of vein patterning by intracellular auxin transport.";
RL Plant Signal. Behav. 8:E27205-E27205(2013).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24692422; DOI=10.1105/tpc.113.118422;
RA Ganguly A., Park M., Kesawat M.S., Cho H.T.;
RT "Functional analysis of the hydrophilic loop in intracellular trafficking
RT of Arabidopsis PIN-FORMED proteins.";
RL Plant Cell 26:1570-1585(2014).
RN [11]
RP INDUCTION, AND FUNCTION.
RX PubMed=24180465; DOI=10.1111/tpj.12373;
RA Chen Y., Aung K., Rolcik J., Walicki K., Friml J., Brandizzi F.;
RT "Inter-regulation of the unfolded protein response and auxin signaling.";
RL Plant J. 77:97-107(2014).
RN [12]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=26560462; DOI=10.1186/s12915-015-0208-3;
RA Verna C., Sawchuk M.G., Linh N.M., Scarpella E.;
RT "Control of vein network topology by auxin transport.";
RL BMC Biol. 13:94-94(2015).
CC -!- FUNCTION: Auxin transporter regulating intracellular auxin homeostasis
CC and metabolism (PubMed:19506555, PubMed:20439545). Mediates the auxin
CC transport from the cytosol into the lumen of the endoplasmic reticulum
CC (PubMed:19506555). May also act as an auxin efflux carrier when located
CC to the cell membrane (PubMed:24692422). PIN5 and PIN8 may have an
CC antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451).
CC Involved in unfolded protein response (UPR) activation
CC (PubMed:24180465). Involved in the control of vein patterning
CC (PubMed:24304505). Promotes vein formation (PubMed:26560462). PIN5,
CC PIN6, and PIN8 control vein network geometry, but they are expressed in
CC mutually exclusive domains of leaf vascular cells (PubMed:26560462).
CC {ECO:0000269|PubMed:19506555, ECO:0000269|PubMed:20439545,
CC ECO:0000269|PubMed:22760640, ECO:0000269|PubMed:24180465,
CC ECO:0000269|PubMed:24304505, ECO:0000269|PubMed:26560462,
CC ECO:0000305|PubMed:22990451, ECO:0000305|PubMed:24692422}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19506555, ECO:0000269|PubMed:20439545,
CC ECO:0000269|PubMed:24692422}; Multi-pass membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:24692422}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Along the root developmental
CC zones, the localization gradually shifted from cell membrane
CC localization in the meristematic epidermal cells to internal
CC localization in the older elongating epidermal cells. Localizes to the
CC cell membrane in the pavement and guard cells of the cotyledon and to
CC internal compartments in the vascular tissues.
CC {ECO:0000269|PubMed:24692422}.
CC -!- TISSUE SPECIFICITY: Expressed in elongating parts of hypocotyl,
CC cotyledon vasculature and guard cells (PubMed:19506555,
CC PubMed:24692422). Detected in root pericycle and root tip and at later
CC developmental stages in leaves, stems and flowers (PubMed:19506555,
CC PubMed:24692422). Expressed in veins of mature leaves
CC (PubMed:26560462). {ECO:0000269|PubMed:19506555,
CC ECO:0000269|PubMed:24692422, ECO:0000269|PubMed:26560462}.
CC -!- INDUCTION: Down-regulated upon auxin treatment (PubMed:19506555). Down-
CC regulated by endoplasmic reticulum stress treatment (PubMed:24180465).
CC {ECO:0000269|PubMed:19506555, ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Defects in lateral root initiation and in root
CC and hypocotyl growth. Increased levels of endogenous free auxin.
CC {ECO:0000269|PubMed:19506555}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005242; BAB09622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92305.1; -; Genomic_DNA.
DR RefSeq; NP_197157.4; NM_121659.5.
DR AlphaFoldDB; Q9FFD0; -.
DR BioGRID; 16791; 42.
DR IntAct; Q9FFD0; 42.
DR STRING; 3702.AT5G16530.1; -.
DR TCDB; 2.A.69.1.6; the auxin efflux carrier (aec) family.
DR PaxDb; Q9FFD0; -.
DR PRIDE; Q9FFD0; -.
DR EnsemblPlants; AT5G16530.1; AT5G16530.1; AT5G16530.
DR GeneID; 831515; -.
DR Gramene; AT5G16530.1; AT5G16530.1; AT5G16530.
DR KEGG; ath:AT5G16530; -.
DR Araport; AT5G16530; -.
DR TAIR; locus:2171392; AT5G16530.
DR eggNOG; ENOG502QS1X; Eukaryota.
DR HOGENOM; CLU_019285_0_0_1; -.
DR InParanoid; Q9FFD0; -.
DR OMA; YYAVLEF; -.
DR OrthoDB; 1106458at2759; -.
DR PhylomeDB; Q9FFD0; -.
DR PRO; PR:Q9FFD0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFD0; baseline and differential.
DR Genevisible; Q9FFD0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0080161; F:auxin transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IBA:GO_Central.
DR GO; GO:0010252; P:auxin homeostasis; IMP:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0080162; P:endoplasmic reticulum to cytosol auxin transport; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR InterPro; IPR014024; Auxin_eff_plant.
DR InterPro; IPR004776; Mem_trans.
DR Pfam; PF03547; Mem_trans; 2.
DR TIGRFAMs; TIGR00946; 2a69; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Cell membrane; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..351
FT /note="Auxin efflux carrier component 5"
FT /id="PRO_0000123787"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 351 AA; 38573 MW; B75E1F7B06E9853B CRC64;
MINCGDVYKV IEAMVPLYVA LILGYGSVKW WHIFTRDQCD AINRLVCYFT LPLFTIEFTA
HVDPFNMNYR FIAADVLSKV IIVTVLALWA KYSNKGSYCW SITSFSLCTL TNSLVVGVPL
AKAMYGQQAV DLVVQSSVFQ AIVWLTLLLF VLEFRKAGFS SNNISDVQVD NINIESGKRE
TVVVGEKSFL EVMSLVWLKL ATNPNCYSCI LGIAWAFISN RWHLELPGIL EGSILIMSKA
GTGTAMFNMG IFMALQEKLI VCGTSLTVMG MVLKFIAGPA AMAIGSIVLG LHGDVLRVAI
IQAALPQSIT SFIFAKEYGL HADVLSTAVI FGMLVSLPVL VAYYAALEFI H
