PIN3_ARATH
ID PIN3_ARATH Reviewed; 640 AA.
AC Q9S7Z8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Auxin efflux carrier component 3 {ECO:0000303|PubMed:11845211};
DE Short=AtPIN3 {ECO:0000303|PubMed:11845211};
GN Name=PIN3 {ECO:0000303|PubMed:11845211};
GN OrderedLocusNames=At1g70940 {ECO:0000312|Araport:AT1G70940};
GN ORFNames=F15H11.14 {ECO:0000312|EMBL:AAD55507.1};
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=11845211; DOI=10.1038/415806a;
RA Friml J., Wisniewska J., Benkova E., Mendgen K., Palme K.;
RT "Lateral relocation of auxin efflux regulator PIN3 mediates tropism in
RT Arabidopsis.";
RL Nature 415:806-809(2002).
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 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-366, AND IDENTIFICATION BY
RP MASS 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 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 lateral auxin transport system and mediates tropic
CC growth. Coordinated polar localization of PIN3 is directly regulated by
CC the vesicle trafficking process. {ECO:0000269|PubMed:20439545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20439545};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed at the lateral side of
CC shoot endodermis cells as well as root pericycle and columella cells.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis. Detected in the
CC precursors of the columella root cells. {ECO:0000269|PubMed:14614497}.
CC -!- INDUCTION: Down-regulated by endoplasmic reticulum stress treatment.
CC {ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Plants display defects in hypocotyl differential
CC growth. {ECO:0000269|PubMed:11845211}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
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DR EMBL; AF087818; AAD52695.1; -; mRNA.
DR EMBL; AC008148; AAD55507.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35140.1; -; Genomic_DNA.
DR EMBL; AY136327; AAM96993.1; -; mRNA.
DR EMBL; BT002085; AAN72096.1; -; mRNA.
DR PIR; G96733; G96733.
DR RefSeq; NP_177250.1; NM_105762.3.
DR AlphaFoldDB; Q9S7Z8; -.
DR BioGRID; 28652; 8.
DR IntAct; Q9S7Z8; 2.
DR STRING; 3702.AT1G70940.1; -.
DR TCDB; 2.A.69.1.4; the auxin efflux carrier (aec) family.
DR iPTMnet; Q9S7Z8; -.
DR PaxDb; Q9S7Z8; -.
DR PRIDE; Q9S7Z8; -.
DR ProteomicsDB; 235029; -.
DR EnsemblPlants; AT1G70940.1; AT1G70940.1; AT1G70940.
DR GeneID; 843432; -.
DR Gramene; AT1G70940.1; AT1G70940.1; AT1G70940.
DR KEGG; ath:AT1G70940; -.
DR Araport; AT1G70940; -.
DR TAIR; locus:2013975; AT1G70940.
DR eggNOG; ENOG502QRM7; Eukaryota.
DR HOGENOM; CLU_019285_1_1_1; -.
DR InParanoid; Q9S7Z8; -.
DR OMA; DQSHNGE; -.
DR OrthoDB; 337723at2759; -.
DR PhylomeDB; Q9S7Z8; -.
DR PRO; PR:Q9S7Z8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7Z8; baseline and differential.
DR Genevisible; Q9S7Z8; AT.
DR GO; GO:0009986; C:cell surface; 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:0016328; C:lateral plasma membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0012506; C:vesicle membrane; IDA:TAIR.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IMP:TAIR.
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; TAS:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IDA:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
DR GO; GO:0009606; P:tropism; 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..640
FT /note="Auxin efflux carrier component 3"
FT /id="PRO_0000123782"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
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 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 310..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 640 AA; 69466 MW; 256F82C8E1ADADB0 CRC64;
MISWHDLYTV LTAVIPLYVA MILAYGSVRW WKIFSPDQCS GINRFVAIFA VPLLSFHFIS
TNNPYAMNLR FIAADTLQKI IMLSLLVLWA NFTRSGSLEW SITIFSLSTL PNTLVMGIPL
LIAMYGEYSG SLMVQIVVLQ CIIWYTLLLF LFEFRGAKML IMEQFPETAA SIVSFKVESD
VVSLDGHDFL ETDAEIGDDG KLHVTVRKSN ASRRSFCGPN MTPRPSNLTG AEIYSLSTTP
RGSNFNHSDF YNMMGFPGGR LSNFGPADMY SVQSSRGPTP RPSNFEENCA MASSPRFGYY
PGGGAGSYPA PNPEFSSTTT STANKSVNKN PKDVNTNQQT TLPTGGKSNS HDAKELHMFV
WSSNGSPVSD RAGLNVFGGA PDNDQGGRSD QGAKEIRMLV PDQSHNGETK AVAHPASGDF
GGEQQFSFAG KEEEAERPKD AENGLNKLAP NSTAALQSKT GLGGAEASQR KNMPPASVMT
RLILIMVWRK LIRNPNTYSS LIGLIWALVA FRWHVAMPKI IQQSISILSD AGLGMAMFSL
GLFMALQPKL IACGNSVATF AMAVRFLTGP AVMAVAAIAI GLRGDLLRVA IVQAALPQGI
VPFVFAKEYN VHPAILSTGV IFGMLIALPI TLVYYILLGL
