PIN2_ARATH
ID PIN2_ARATH Reviewed; 647 AA.
AC Q9LU77; O82810; Q9SYT2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Auxin efflux carrier component 2 {ECO:0000303|PubMed:9843496};
DE Short=AtPIN2 {ECO:0000303|PubMed:9843496};
DE AltName: Full=Auxin efflux carrier AGR {ECO:0000303|PubMed:9871369};
DE AltName: Full=Ethylene-insensitive root 1 {ECO:0000303|PubMed:9679062};
DE Short=AtEIR1 {ECO:0000303|PubMed:9679062};
DE AltName: Full=Polar-auxin-transport efflux component AGR1 {ECO:0000303|PubMed:9844024};
DE AltName: Full=Protein AGRAVITROPIC 1 {ECO:0000303|PubMed:9844024};
DE Short=AtAGR1 {ECO:0000303|PubMed:9844024};
DE AltName: Full=Protein WAVY 6 {ECO:0000303|PubMed:9843496};
GN Name=PIN2 {ECO:0000303|PubMed:9843496};
GN Synonyms=AGR {ECO:0000303|PubMed:9871369},
GN AGR1 {ECO:0000303|PubMed:9844024}, EIR1 {ECO:0000303|PubMed:9679062},
GN WAV6 {ECO:0000303|PubMed:9843496};
GN OrderedLocusNames=At5g57090 {ECO:0000312|Araport:AT5G57090};
GN ORFNames=MUL3.3 {ECO:0000312|EMBL:BAA97359.1};
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 [MRNA], CHARACTERIZATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9679062; DOI=10.1101/gad.12.14.2175;
RA Luschnig C., Gaxiola R.A., Grisafi P., Fink G.R.;
RT "EIR1, a root-specific protein involved in auxin transport, is required for
RT gravitropism in Arabidopsis thaliana.";
RL Genes Dev. 12:2175-2187(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9844024; DOI=10.1073/pnas.95.25.15112;
RA Chen R., Hilson P., Sedbrook J., Rosen E., Caspar T., Masson P.H.;
RT "The Arabidopsis thaliana AGRAVITROPIC 1 gene encodes a component of the
RT polar-auxin-transport efflux carrier.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15112-15117(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Root;
RX PubMed=9871369; DOI=10.1093/oxfordjournals.pcp.a029310;
RA Utsuno K., Shikanai T., Yamada Y., Hashimoto T.;
RT "Agr, an Agravitropic locus of Arabidopsis thaliana, encodes a novel
RT membrane-protein family member.";
RL Plant Cell Physiol. 39:1111-1118(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, AND NULL MUTANT
RP ATPIN2.
RX PubMed=9843496; DOI=10.1093/emboj/17.23.6903;
RA Mueller A., Guan C., Gaelweiler L., Taenzler P., Huijser P., Marchant A.,
RA Parry G., Bennett M., Wisman E., Palme K.;
RT "AtPIN2 defines a locus of Arabidopsis for root gravitropism control.";
RL EMBO J. 17:6903-6911(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP INTERACTION WITH FYPP1 AND FYPP3.
RX PubMed=22715043; DOI=10.1105/tpc.112.098905;
RA Dai M., Zhang C., Kania U., Chen F., Xue Q., McCray T., Li G., Qin G.,
RA Wakeley M., Terzaghi W., Wan J., Zhao Y., Xu J., Friml J., Deng X.W.,
RA Wang H.;
RT "A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation
RT and auxin efflux in Arabidopsis.";
RL Plant Cell 24:2497-2514(2012).
RN [11]
RP INDUCTION.
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).
CC -!- FUNCTION: Acts as a component of the auxin efflux carrier. Seems to be
CC involved in the root-specific auxin transport, and mediates the root
CC gravitropism. Its particular localization suggest a role in the
CC translocation of auxin towards the elongation zone.
CC {ECO:0000269|PubMed:20439545}.
CC -!- SUBUNIT: Interacts with FYPP1 AND FYPP3. {ECO:0000269|PubMed:22715043}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20439545};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Root-specific. Localized to the cortex, epidermis
CC and lateral root cap, predominantly at the upper side of cells.
CC -!- INDUCTION: Down-regulated by endoplasmic reticulum stress treatment.
CC {ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function mutations impair the root
CC gravitropic response, lead to an increased sensitivity to ethylene and
CC auxin transport inhibitors, and give rise to an auxin accumulation in
CC root tips. {ECO:0000269|PubMed:9679062, ECO:0000269|PubMed:9844024}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97359.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF056026; AAC39513.1; -; mRNA.
DR EMBL; AF087459; AAC84042.1; -; Genomic_DNA.
DR EMBL; AF093241; AAC61781.1; -; mRNA.
DR EMBL; AF086906; AAD11780.1; -; mRNA.
DR EMBL; AF086907; AAD16060.1; -; Genomic_DNA.
DR EMBL; AB023042; BAA97359.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96845.1; -; Genomic_DNA.
DR EMBL; AY078965; AAL84962.1; -; mRNA.
DR EMBL; BT001152; AAN64543.1; -; mRNA.
DR PIR; T51808; T51808.
DR RefSeq; NP_568848.1; NM_125091.4.
DR AlphaFoldDB; Q9LU77; -.
DR BioGRID; 21057; 10.
DR IntAct; Q9LU77; 8.
DR STRING; 3702.AT5G57090.1; -.
DR TCDB; 2.A.69.1.2; the auxin efflux carrier (aec) family.
DR iPTMnet; Q9LU77; -.
DR PaxDb; Q9LU77; -.
DR PRIDE; Q9LU77; -.
DR ProteomicsDB; 236758; -.
DR EnsemblPlants; AT5G57090.1; AT5G57090.1; AT5G57090.
DR GeneID; 835813; -.
DR Gramene; AT5G57090.1; AT5G57090.1; AT5G57090.
DR KEGG; ath:AT5G57090; -.
DR Araport; AT5G57090; -.
DR TAIR; locus:2175559; AT5G57090.
DR eggNOG; ENOG502QV64; Eukaryota.
DR HOGENOM; CLU_019285_1_1_1; -.
DR InParanoid; Q9LU77; -.
DR OMA; NFDEEMM; -.
DR OrthoDB; 337723at2759; -.
DR PhylomeDB; Q9LU77; -.
DR PRO; PR:Q9LU77; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU77; baseline and differential.
DR Genevisible; Q9LU77; AT.
DR GO; GO:0009925; C:basal plasma membrane; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000323; C:lytic vacuole; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0010329; F:auxin efflux 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; IBA:GO_Central.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR InterPro; IPR014024; Auxin_eff_plant.
DR InterPro; IPR004776; Mem_trans.
DR Pfam; PF03547; Mem_trans; 1.
DR TIGRFAMs; TIGR00946; 2a69; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..647
FT /note="Auxin efflux carrier component 2"
FT /id="PRO_0000123781"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 339..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S7Z8"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 541
FT /note="G -> E (in Ref. 4; AAD16060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 69331 MW; D0FAFF72031FFB33 CRC64;
MITGKDMYDV LAAMVPLYVA MILAYGSVRW WGIFTPDQCS GINRFVAVFA VPLLSFHFIS
SNDPYAMNYH FLAADSLQKV VILAALFLWQ AFSRRGSLEW MITLFSLSTL PNTLVMGIPL
LRAMYGDFSG NLMVQIVVLQ SIIWYTLMLF LFEFRGAKLL ISEQFPETAG SITSFRVDSD
VISLNGREPL QTDAEIGDDG KLHVVVRRSS AASSMISSFN KSHGGGLNSS MITPRASNLT
GVEIYSVQSS REPTPRASSF NQTDFYAMFN ASKAPSPRHG YTNSYGGAGA GPGGDVYSLQ
SSKGVTPRTS NFDEEVMKTA KKAGRGGRSM SGELYNNNSV PSYPPPNPMF TGSTSGASGV
KKKESGGGGS GGGVGVGGQN KEMNMFVWSS SASPVSEANA KNAMTRGSST DVSTDPKVSI
PPHDNLATKA MQNLIENMSP GRKGHVEMDQ DGNNGGKSPY MGKKGSDVED GGPGPRKQQM
PPASVMTRLI LIMVWRKLIR NPNTYSSLFG LAWSLVSFKW NIKMPTIMSG SISILSDAGL
GMAMFSLGLF MALQPKIIAC GKSVAGFAMA VRFLTGPAVI AATSIAIGIR GDLLHIAIVQ
AALPQGIVPF VFAKEYNVHP DILSTAVIFG MLVALPVTVL YYVLLGL
