PINI_ARATH
ID PINI_ARATH Reviewed; 622 AA.
AC Q9C6B8; Q9ZSY5; Q9ZSY6;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Auxin efflux carrier component 1 {ECO:0000303|PubMed:9856939};
DE AltName: Full=Protein PIN-FORMED {ECO:0000303|PubMed:9856939};
DE Short=AtPIN1 {ECO:0000303|PubMed:9856939};
GN Name=PIN1 {ECO:0000303|PubMed:9856939};
GN OrderedLocusNames=At1g73590 {ECO:0000312|Araport:AT1G73590};
GN ORFNames=F6D5.2 {ECO:0000312|EMBL:AAG51807.1};
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 [GENOMIC DNA / MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9856939; DOI=10.1126/science.282.5397.2226;
RA Gaelweiler L., Guan C., Mueller A., Wisman E., Mendgen K., Yephremov A.,
RA Palme K.;
RT "Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular
RT tissue.";
RL Science 282:2226-2230(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 POLAR LOCALIZATION.
RX PubMed=10514379; DOI=10.1126/science.286.5438.316;
RA Steinmann T., Geldner N., Grebe M., Mangold S., Jackson C.L., Paris S.,
RA Gaelweiler L., Palme K., Juergens G.;
RT "Coordinated polar localization of auxin efflux carrier PIN1 by GNOM ARF
RT GEF.";
RL Science 286:316-318(1999).
RN [6]
RP PIN1 CYCLING.
RX PubMed=11574889; DOI=10.1038/35096571;
RA Geldner N., Friml J., Stierhof Y.-D., Juergens G., Palme K.;
RT "Auxin transport inhibitors block PIN1 cycling and vesicle trafficking.";
RL Nature 413:425-428(2001).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=14651850; DOI=10.1016/s0092-8674(03)00924-3;
RA Benkova E., Michniewicz M., Sauer M., Teichmann T., Seifertova D.,
RA Juergens G., Friml J.;
RT "Local, efflux-dependent auxin gradients as a common module for plant organ
RT formation.";
RL Cell 115:591-602(2003).
RN [9]
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 [10]
RP FUNCTION, PHOSPHORYLATION AT SER-231; SER-252 AND SER-290, AND MUTAGENESIS
RP OF SER-231; SER-252 AND SER-290.
RX PubMed=20407025; DOI=10.1105/tpc.109.072678;
RA Huang F., Zago M.K., Abas L., van Marion A., Galvan-Ampudia C.S.,
RA Offringa R.;
RT "Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity
RT and auxin transport.";
RL Plant Cell 22:1129-1142(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION AT SER-337 AND THR-340.
RX PubMed=20080776; DOI=10.1073/pnas.0909460107;
RA Zhang J., Nodzynski T., Pencik A., Rolcik J., Friml J.;
RT "PIN phosphorylation is sufficient to mediate PIN polarity and direct auxin
RT transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:918-922(2010).
RN [13]
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 [14]
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 [15]
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 [16]
RP INTERACTION WITH TOPP4.
RX PubMed=25560878; DOI=10.1104/pp.114.249904;
RA Guo X., Qin Q., Yan J., Niu Y., Huang B., Guan L., Li Y., Ren D., Li J.,
RA Hou S.;
RT "TYPE-ONE PROTEIN PHOSPHATASE4 regulates pavement cell interdigitation by
RT modulating PIN-FORMED1 polarity and trafficking in Arabidopsis.";
RL Plant Physiol. 167:1058-1075(2015).
CC -!- FUNCTION: Acts as a component of the auxin efflux carrier. Seems to be
CC involved in the basipetal auxin transport. Mediates the formation of
CC auxin gradient which is required to ensure correct organogenesis.
CC Coordinated polar localization of PIN1 is directly regulated by the
CC vesicle trafficking process and apical-basal PIN1 polarity also depends
CC on the phosphorylation of conserved serine residues by PID kinase. The
CC ARF-GEF protein GNOM is required for the correct recycling of PIN1
CC between the plasma membrane and endosomal compartments.
CC {ECO:0000269|PubMed:14651850, ECO:0000269|PubMed:20407025,
CC ECO:0000269|PubMed:20439545}.
CC -!- SUBUNIT: Interacts with TOPP4 (PubMed:11574889). Interacts with FYPP1
CC AND FYPP3 (PubMed:22715043). {ECO:0000269|PubMed:11574889,
CC ECO:0000269|PubMed:22715043}.
CC -!- INTERACTION:
CC Q9C6B8; Q9LJX0: ABCB19; NbExp=7; IntAct=EBI-1541799, EBI-371791;
CC Q9C6B8; O64682: PID; NbExp=2; IntAct=EBI-1541799, EBI-1393382;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20439545};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at the basal side of elongated
CC parenchymatous xylem cells.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis. Already detected
CC in the 8-cell stage at the inner cell boundaries. Later, polarity is
CC gradually established at the basal side of provascular cells then in
CC epidermis cells. {ECO:0000269|PubMed:14614497}.
CC -!- INDUCTION: Down-regulated by endoplasmic reticulum stress treatment.
CC {ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit developed naked, pin-shaped
CC inflorescences and abnormalities in the number, size, shape, and
CC position of lateral organs. {ECO:0000269|PubMed:9856939}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD04377.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF089084; AAD04376.1; -; mRNA.
DR EMBL; AF089085; AAD04377.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079676; AAG51807.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35479.1; -; Genomic_DNA.
DR EMBL; AF372950; AAK50090.1; -; mRNA.
DR EMBL; AY093960; AAM16221.1; -; mRNA.
DR PIR; G96762; G96762.
DR RefSeq; NP_177500.1; NM_106017.4.
DR AlphaFoldDB; Q9C6B8; -.
DR BioGRID; 28912; 12.
DR DIP; DIP-40041N; -.
DR IntAct; Q9C6B8; 6.
DR STRING; 3702.AT1G73590.1; -.
DR TCDB; 2.A.69.1.1; the auxin efflux carrier (aec) family.
DR iPTMnet; Q9C6B8; -.
DR PaxDb; Q9C6B8; -.
DR PRIDE; Q9C6B8; -.
DR ProteomicsDB; 234756; -.
DR EnsemblPlants; AT1G73590.1; AT1G73590.1; AT1G73590.
DR GeneID; 843693; -.
DR Gramene; AT1G73590.1; AT1G73590.1; AT1G73590.
DR KEGG; ath:AT1G73590; -.
DR Araport; AT1G73590; -.
DR TAIR; locus:2035037; AT1G73590.
DR eggNOG; ENOG502QRM7; Eukaryota.
DR HOGENOM; CLU_019285_1_1_1; -.
DR InParanoid; Q9C6B8; -.
DR OMA; YSMMASG; -.
DR OrthoDB; 337723at2759; -.
DR PhylomeDB; Q9C6B8; -.
DR PRO; PR:Q9C6B8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6B8; baseline and differential.
DR Genevisible; Q9C6B8; AT.
DR GO; GO:0045177; C:apical part of cell; IDA:TAIR.
DR GO; GO:0009925; C:basal plasma membrane; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA: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:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IMP: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:0048825; P:cotyledon development; IGI:UniProtKB.
DR GO; GO:0048826; P:cotyledon morphogenesis; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0010229; P:inflorescence development; IMP:TAIR.
DR GO; GO:0010338; P:leaf formation; IGI:TAIR.
DR GO; GO:0010358; P:leaf shaping; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; TAS:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP: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..622
FT /note="Auxin efflux carrier component 1"
FT /id="PRO_0000123780"
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 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 213..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20407025"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20407025"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20407025"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20080776"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20080776"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S7Z8"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 231
FT /note="S->A: Apical-to-basal shift in polar targeting and
FT increased auxin accumulation in the root tips; when
FT associated with A-252 and A-290."
FT /evidence="ECO:0000269|PubMed:20407025"
FT MUTAGEN 252
FT /note="S->A: Apical-to-basal shift in polar targeting and
FT increased auxin accumulation in the root tips; when
FT associated with A-231 and A-290."
FT /evidence="ECO:0000269|PubMed:20407025"
FT MUTAGEN 290
FT /note="S->A: Apical-to-basal shift in polar targeting and
FT increased auxin accumulation in the root tips; when
FT associated with A-231 and A-252."
FT /evidence="ECO:0000269|PubMed:20407025"
FT CONFLICT 146
FT /note="T -> I (in Ref. 1; AAD04376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 67019 MW; 333E90DB12F62C83 CRC64;
MITAADFYHV MTAMVPLYVA MILAYGSVKW WKIFTPDQCS GINRFVALFA VPLLSFHFIA
ANNPYAMNLR FLAADSLQKV IVLSLLFLWC KLSRNGSLDW TITLFSLSTL PNTLVMGIPL
LKGMYGNFSG DLMVQIVVLQ CIIWYTLMLF LFEYRGAKLL ISEQFPDTAG SIVSIHVDSD
IMSLDGRQPL ETEAEIKEDG KLHVTVRRSN ASRSDIYSRR SQGLSATPRP SNLTNAEIYS
LQSSRNPTPR GSSFNHTDFY SMMASGGGRN SNFGPGEAVF GSKGPTPRPS NYEEDGGPAK
PTAAGTAAGA GRFHYQSGGS GGGGGAHYPA PNPGMFSPNT GGGGGTAAKG NAPVVGGKRQ
DGNGRDLHMF VWSSSASPVS DVFGGGGGNH HADYSTATND HQKDVKISVP QGNSNDNQYV
EREEFSFGNK DDDSKVLATD GGNNISNKTT QAKVMPPTSV MTRLILIMVW RKLIRNPNSY
SSLFGITWSL ISFKWNIEMP ALIAKSISIL SDAGLGMAMF SLGLFMALNP RIIACGNRRA
AFAAAMRFVV GPAVMLVASY AVGLRGVLLH VAIIQAALPQ GIVPFVFAKE YNVHPDILST
AVIFGMLIAL PITLLYYILL GL
