PIN4_ARATH
ID PIN4_ARATH Reviewed; 616 AA.
AC Q8RWZ6; Q9M7Q6; Q9MAS3;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Auxin efflux carrier component 4 {ECO:0000303|PubMed:11893337};
DE Short=AtPIN4 {ECO:0000303|PubMed:11893337};
GN Name=PIN4 {ECO:0000303|PubMed:11893337};
GN OrderedLocusNames=At2g01420 {ECO:0000312|Araport:AT2G01420};
GN ORFNames=F2I9.4 {ECO:0000312|EMBL:AAC67319.2};
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] (ISOFORM 2), CHARACTERIZATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11893337; DOI=10.1016/s0092-8674(02)00656-6;
RA Friml J., Benkova E., Blilou I., Wisniewska J., Hamann T., Ljung K.,
RA Woody S., Sandberg G., Scheres B., Juergens G., Palme K.;
RT "AtPIN4 mediates sink-driven auxin gradients and root patterning in
RT Arabidopsis.";
RL Cell 108:661-673(2002).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=14614497; DOI=10.1038/nature02085;
RA Friml J., Vieten A., Sauer M., Weijers D., Schwarz H., Hamann T.,
RA Offringa R., Juergens G.;
RT "Efflux-dependent auxin gradients establish the apical-basal axis of
RT Arabidopsis.";
RL Nature 426:147-153(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-395 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=22540348; DOI=10.1111/j.1365-313x.2012.05037.x;
RA Dal Bosco C., Dovzhenko A., Liu X., Woerner N., Rensch T., Eismann M.,
RA Eimer S., Hegermann J., Paponov I.A., Ruperti B., Heberle-Bors E.,
RA Touraev A., Cohen J.D., Palme K.;
RT "The endoplasmic reticulum localized PIN8 is a pollen-specific auxin
RT carrier involved in intracellular auxin homeostasis.";
RL Plant J. 71:860-870(2012).
RN [10]
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).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. C24, cv. Columbia, cv. Cvi-0, cv. Lac-5, cv. Ler-1, cv. Mib-60,
RC cv. Sha, cv. Ty-0, and cv. Wassilewskija-2;
RX PubMed=31299202; DOI=10.1016/j.cell.2019.06.021;
RA Ogura T., Goeschl C., Filiault D., Wolhrab B., Satbhai S.B., Busch W.;
RT "Root system depth in Arabidopsis is shaped by EXOCYST70A3 via the dynamic
RT modulation of auxin transport.";
RL Cell 178:P400.E16-P412.E16(2019).
CC -!- FUNCTION: Acts as a component of the auxin efflux carrier. Plays a role
CC in generating a sink for auxin into columella cells (PubMed:20439545).
CC Maintains the endogenous auxin gradient, which is essential for correct
CC root patterning (PubMed:20439545). Involved in EXO70A3-regulated
CC gravitropic responses in columella cells and in root system
CC architecture (RSA) (PubMed:31299202). {ECO:0000269|PubMed:20439545,
CC ECO:0000269|PubMed:31299202}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20439545,
CC ECO:0000269|PubMed:31299202}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Distribution in columella cells is regulated by
CC EXO70A3. {ECO:0000269|PubMed:31299202}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWZ6-2; Sequence=VSP_009419;
CC -!- TISSUE SPECIFICITY: Expressed in the quiescent center precursors and
CC surrounding cells (PubMed:22540348). Present in columella cells of
CC primary roots (PubMed:31299202). Detected in pollen (PubMed:22540348).
CC {ECO:0000269|PubMed:22540348, ECO:0000269|PubMed:31299202}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (PubMed:14614497).
CC Detected in the embryonic and seedling root meristems
CC (PubMed:14614497). {ECO:0000269|PubMed:14614497}.
CC -!- INDUCTION: Down-regulated by endoplasmic reticulum stress treatment.
CC {ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Plants display altered patterning in the
CC developing root meristem (PubMed:11893337). Larger variation of root
CC tip angles during the dynamic root gravitropic response
CC (PubMed:31299202). Deeper root system architecture (RSA)
CC (PubMed:31299202). {ECO:0000269|PubMed:11893337,
CC ECO:0000269|PubMed:31299202}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
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DR EMBL; AF087016; AAF36769.1; -; mRNA.
DR EMBL; AC005560; AAC67319.2; -; Genomic_DNA.
DR EMBL; AC006200; AAM15143.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05448.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05449.1; -; Genomic_DNA.
DR EMBL; AY091009; AAM14031.1; -; mRNA.
DR EMBL; BT008691; AAP40497.1; -; mRNA.
DR PIR; E84424; E84424.
DR RefSeq; NP_565261.1; NM_126203.3. [Q8RWZ6-2]
DR RefSeq; NP_849923.1; NM_179592.2. [Q8RWZ6-1]
DR AlphaFoldDB; Q8RWZ6; -.
DR BioGRID; 73; 62.
DR IntAct; Q8RWZ6; 59.
DR STRING; 3702.AT2G01420.2; -.
DR iPTMnet; Q8RWZ6; -.
DR PaxDb; Q8RWZ6; -.
DR PRIDE; Q8RWZ6; -.
DR ProteomicsDB; 235030; -. [Q8RWZ6-1]
DR EnsemblPlants; AT2G01420.1; AT2G01420.1; AT2G01420. [Q8RWZ6-2]
DR EnsemblPlants; AT2G01420.2; AT2G01420.2; AT2G01420. [Q8RWZ6-1]
DR GeneID; 814670; -.
DR Gramene; AT2G01420.1; AT2G01420.1; AT2G01420. [Q8RWZ6-2]
DR Gramene; AT2G01420.2; AT2G01420.2; AT2G01420. [Q8RWZ6-1]
DR KEGG; ath:AT2G01420; -.
DR Araport; AT2G01420; -.
DR TAIR; locus:2038781; AT2G01420.
DR eggNOG; ENOG502QRM7; Eukaryota.
DR InParanoid; Q8RWZ6; -.
DR OMA; KATHMPP; -.
DR PhylomeDB; Q8RWZ6; -.
DR PRO; PR:Q8RWZ6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWZ6; baseline and differential.
DR Genevisible; Q8RWZ6; AT.
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:0005739; C:mitochondrion; HDA:TAIR.
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: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:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
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 Alternative splicing; Auxin signaling pathway; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..616
FT /note="Auxin efflux carrier component 4"
FT /id="PRO_0000123783"
FT TRANSMEM 8..28
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 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 302..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S7Z8"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 396..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11893337"
FT /id="VSP_009419"
FT MOD_RES Q8RWZ6-2:395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 616 AA; 66742 MW; 75EA7B6543E79A34 CRC64;
MITWHDLYTV LTAVVPLYVA MILAYGSVQW WKIFSPDQCS GINRFVAIFA VPLLSFHFIS
TNDPYAMNFR FVAADTLQKI IMLVLLALWA NLTKNGSLEW MITIFSLSTL PNTLVMGIPL
LIAMYGTYAG SLMVQVVVLQ CIIWYTLLLF LFEYRGAKLL IMEQFPETGA SIVSFKVESD
VVSLDGHDFL ETDAEIGNDG KLHVTVRKSN ASRRSLMMTP RPSNLTGAEI YSLSSTPRGS
NFNHSDFYSV MGFPGGRLSN FGPADLYSVQ SSRGPTPRPS NFEENNAVKY GFYNNTNSSV
PAAGSYPAPN PEFSTGTGVS TKPNKIPKEN QQQLQEKDSK ASHDAKELHM FVWSSSASPV
SDVFGGGAGD NVATEQSEQG AKEIRMVVSD QPRKSNARGG GDDIGGLDSG EGEREIEKAT
AGLNKMGSNS TAELEAAGGD GGGNNGTHMP PTSVMTRLIL IMVWRKLIRN PNTYSSLIGL
IWALVAYRWH VAMPKILQQS ISILSDAGLG MAMFSLGLFM ALQPKIIACG NSVATFAMAV
RFITGPAIMA VAGIAIGLHG DLLRIAIVQA ALPQGIVPFV FAKEYNVHPT ILSTGVIFGM
LIALPITLVY YILLGL
