PIN7_ARATH
ID PIN7_ARATH Reviewed; 619 AA.
AC Q940Y5; O49308; Q9SQH5;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Auxin efflux carrier component 7 {ECO:0000303|PubMed:14614497};
DE Short=AtPIN7 {ECO:0000303|PubMed:14614497};
GN Name=PIN7 {ECO:0000303|PubMed:14614497}; Synonyms=AEH1;
GN OrderedLocusNames=At1g23080; ORFNames=T26J12.14;
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 1).
RA Friml J., Wisniewska J., Palme K.;
RT "PIN gene family in Arabidopsis thaliana.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 IDENTIFICATION BY 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
CC (PubMed:14614497, PubMed:20439545). Mediates the initial auxin gradient
CC which contributes to the establishment of the apical-basal axis in
CC early embryogenesis (PubMed:14614497). {ECO:0000269|PubMed:14614497,
CC ECO:0000269|PubMed:20439545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20439545};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q940Y5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q940Y5-2; Sequence=VSP_009420, VSP_009421, VSP_009422;
CC -!- DEVELOPMENTAL STAGE: Expressed during early embryogenesis. Detected
CC apically in the basal cell lineage resulting from the first zygotic
CC division. At the 32-cell stage, localization shifts to the basal side
CC of the cells in the developing embryo. {ECO:0000269|PubMed:14614497}.
CC -!- INDUCTION: Down-regulated by endoplasmic reticulum stress treatment.
CC {ECO:0000269|PubMed:24180465}.
CC -!- DISRUPTION PHENOTYPE: Plants display altered embryo with defects in
CC stereotypical pattern of early embryogenesis.
CC {ECO:0000269|PubMed:14614497}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice site
CC and to an intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF087820; AAD52697.1; -; mRNA.
DR EMBL; AC002311; AAC00611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30332.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30333.1; -; Genomic_DNA.
DR EMBL; AY052356; AAK96547.1; -; mRNA.
DR PIR; A86365; A86365.
DR RefSeq; NP_564189.1; NM_102156.1. [Q940Y5-2]
DR RefSeq; NP_849700.1; NM_179369.2. [Q940Y5-1]
DR AlphaFoldDB; Q940Y5; -.
DR BioGRID; 24155; 20.
DR IntAct; Q940Y5; 19.
DR STRING; 3702.AT1G23080.1; -.
DR TCDB; 2.A.69.1.3; the auxin efflux carrier (aec) family.
DR iPTMnet; Q940Y5; -.
DR PaxDb; Q940Y5; -.
DR PRIDE; Q940Y5; -.
DR ProteomicsDB; 236737; -. [Q940Y5-1]
DR EnsemblPlants; AT1G23080.1; AT1G23080.1; AT1G23080. [Q940Y5-1]
DR EnsemblPlants; AT1G23080.2; AT1G23080.2; AT1G23080. [Q940Y5-2]
DR GeneID; 838916; -.
DR Gramene; AT1G23080.1; AT1G23080.1; AT1G23080. [Q940Y5-1]
DR Gramene; AT1G23080.2; AT1G23080.2; AT1G23080. [Q940Y5-2]
DR KEGG; ath:AT1G23080; -.
DR Araport; AT1G23080; -.
DR TAIR; locus:2201225; AT1G23080.
DR eggNOG; ENOG502QRM7; Eukaryota.
DR InParanoid; Q940Y5; -.
DR OrthoDB; 337723at2759; -.
DR PhylomeDB; Q940Y5; -.
DR PRO; PR:Q940Y5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940Y5; baseline and differential.
DR Genevisible; Q940Y5; 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:0005634; C:nucleus; HDA: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; 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:0009942; P:longitudinal axis specification; 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 Alternative splicing; Auxin signaling pathway; Cell membrane; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..619
FT /note="Auxin efflux carrier component 7"
FT /id="PRO_0000123786"
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 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 306..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C6B8"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S7Z8"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 397..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009420"
FT VAR_SEQ 521..531
FT /note="LFMALQPKLIA -> ESSFYSVSFFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009421"
FT VAR_SEQ 532..619
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009422"
SQ SEQUENCE 619 AA; 67588 MW; C155860B1B4DF9DA CRC64;
MITWHDLYTV LTAVIPLYVA MILAYGSVRW WKIFSPDQCS GINRFVAIFA VPLLSFHFIS
SNNPYAMNLR FIAADTLQKL IMLTLLIIWA NFTRSGSLEW SITIFSLSTL PNTLVMGIPL
LIAMYGEYSG SLMVQIVVLQ CIIWYTLLLF LFEYRGAKIL IMEQFPETGA SIVSFKVESD
VVSLDGHDFL ETDAQIGDDG KLHVTVRKSN ASRRSFYGGG GTNMTPRPSN LTGAEIYSLN
TTPRGSNFNH SDFYSMMGFP GGRLSNFGPA DMYSVQSSRG PTPRPSNFEE SCAMASSPRF
GYYPGGAPGS YPAPNPEFST GNKTGSKAPK ENHHHVGKSN SNDAKELHMF VWGSNGSPVS
DRAGLQVDNG ANEQVGKSDQ GGAKEIRMLI SDHTQNGENK AGPMNGDYGG EEESERVKEV
PNGLHKLRCN STAELNPKEA IETGETVPVK HMPPASVMTR LILIMVWRKL IRNPNTYSSL
IGLIWALVAF RWDVAMPKII QQSISILSDA GLGMAMFSLG LFMALQPKLI ACGNSTATFA
MAVRFFTGPA VMAVAAMAIG LRGDLLRVAI VQAALPQGIV PFVFAKEYNV HPAILSTGVI
FGMLIALPIT LVYYILLGL
