BOR1_ARATH
ID BOR1_ARATH Reviewed; 704 AA.
AC Q8VYR7; Q9SHX0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Boron transporter 1 {ECO:0000303|PubMed:12447444};
GN Name=BOR1 {ECO:0000303|PubMed:12447444};
GN OrderedLocusNames=At2g47160 {ECO:0000312|Araport:AT2G47160};
GN ORFNames=T3D7.3 {ECO:0000312|EMBL:AAD26598.1};
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], FUNCTION, MUTAGENESIS OF SER-74 AND GLY-86,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12447444; DOI=10.1038/nature01139;
RA Takano J., Noguchi K., Yasumori M., Kobayashi M., Gajdos Z., Miwa K.,
RA Hayashi H., Yoneyama T., Fujiwara T.;
RT "Arabidopsis boron transporter for xylem loading.";
RL Nature 420:337-340(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].
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.
RX PubMed=9390427; DOI=10.1104/pp.115.3.901;
RA Noguchi K., Yasumori M., Imai T., Naito S., Matsunaga T., Oda H.,
RA Hayashi H., Chino M., Fujiwara T.;
RT "bor1-1, an Arabidopsis thaliana mutant that requires a high level of
RT boron.";
RL Plant Physiol. 115:901-906(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16103374; DOI=10.1073/pnas.0502060102;
RA Takano J., Miwa K., Yuan L., von Wiren N., Fujiwara T.;
RT "Endocytosis and degradation of BOR1, a boron transporter of Arabidopsis
RT thaliana, regulated by boron availability.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12276-12281(2005).
RN [7]
RP FUNCTION.
RX PubMed=16805739; DOI=10.1111/j.1365-313x.2006.02763.x;
RA Miwa K., Takano J., Fujiwara T.;
RT "Improvement of seed yields under boron-limiting conditions through
RT overexpression of BOR1, a boron transporter for xylem loading, in
RT Arabidopsis thaliana.";
RL Plant J. 46:1084-1091(2006).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-373;
RP TYR-398 AND TYR-405.
RX PubMed=20194745; DOI=10.1073/pnas.0910744107;
RA Takano J., Tanaka M., Toyoda A., Miwa K., Kasai K., Fuji K., Onouchi H.,
RA Naito S., Fujiwara T.;
RT "Polar localization and degradation of Arabidopsis boron transporters
RT through distinct trafficking pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5220-5225(2010).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27449211; DOI=10.1093/pcp/pcw121;
RA Yoshinari A., Fujimoto M., Ueda T., Inada N., Naito S., Takano J.;
RT "DRP1-dependent endocytosis is essential for polar Localization and boron-
RT induced degradation of the borate transporter BOR1 in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 57:1985-2000(2016).
CC -!- FUNCTION: Efflux-type boron (B) transporter for xylem loading,
CC responsive of boron translocation from roots to shoots under boron
CC limitation (PubMed:16805739, PubMed:9390427, PubMed:12447444,
CC PubMed:27449211). Boron is essential for maintaining the integrity of
CC plants cell walls (PubMed:16805739, PubMed:9390427).
CC {ECO:0000269|PubMed:12447444, ECO:0000269|PubMed:16805739,
CC ECO:0000269|PubMed:27449211, ECO:0000269|PubMed:9390427}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12447444,
CC ECO:0000269|PubMed:27449211}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:12447444,
CC ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:27449211}; Multi-pass
CC membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:12447444, ECO:0000269|PubMed:16103374,
CC ECO:0000269|PubMed:27449211}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Transferred from the plasma membrane via the
CC endosomes to the vacuole under high-concentration of boron in a DRP1A-
CC dependent manner (PubMed:16103374, PubMed:27449211, PubMed:20194745).
CC Localized to the polar inner/stele-side domain of the plasma membrane
CC under low-boron conditions, this polar localization is established
CC after cell division (PubMed:27449211). Co-localizes with DRP1A in the
CC cell plate and the plasma membrane (PubMed:27449211). Under boron
CC excess, BOR1 is transferred from the plasma membrane via the endosomes
CC to the vacuole for degradation in a DRP1A-dependent manner
CC (PubMed:16103374, PubMed:27449211, PubMed:20194745).
CC {ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:20194745,
CC ECO:0000269|PubMed:27449211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8VYR7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in proximal side of various root cells,
CC notably in the columella, lateral root cap, epidermis and endodermis in
CC tip and elongation zones of the root (PubMed:27449211). Also detected
CC in the epidermis, cortex, endodermis, and stele cells of the root hair
CC zone (PubMed:27449211). Observed in cotyledons and hypocotyls
CC (PubMed:27449211). {ECO:0000269|PubMed:12447444,
CC ECO:0000269|PubMed:20194745, ECO:0000269|PubMed:27449211}.
CC -!- DEVELOPMENTAL STAGE: First observed in seedlings and in the primary
CC root tip and mature portion of the root (PubMed:27449211). Expressed in
CC the basal region of the hypocotyl, localized with inner/stele-side
CC polarity in the endodermal cells (PubMed:27449211). In the tip of
CC cotyledons, accumulates mostly in epidermal cells of the top side, with
CC a polar localization toward the inner side of the cotyledon
CC (PubMed:27449211). High levels in the transition and differentiation
CC zones of roots, localized with stele-side polarity in the epidermal and
CC endodermal cells (PubMed:27449211). In the root meristem zone, present
CC in epiderm, endoderm, columella, parts of the lateral cap, quiescent
CC center (QC), vascular initial and protovascular cells
CC (PubMed:27449211). In the QC, vascular initial and protovascular cells,
CC exhibits an apical polar localization (PubMed:27449211).
CC {ECO:0000269|PubMed:27449211}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31.3) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD26598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073713; BAC20173.1; -; mRNA.
DR EMBL; AC007236; AAD26598.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004411; AAD26598.1; JOINED; Genomic_DNA.
DR EMBL; CP002685; AEC10808.1; -; Genomic_DNA.
DR EMBL; AY070067; AAL49824.1; -; mRNA.
DR EMBL; AY096436; AAM20076.1; -; mRNA.
DR EMBL; BT000732; AAN31874.1; -; mRNA.
DR PIR; G84911; G84911.
DR RefSeq; NP_850469.1; NM_180138.3. [Q8VYR7-1]
DR PDB; 5L25; X-ray; 4.11 A; A=1-645.
DR PDBsum; 5L25; -.
DR AlphaFoldDB; Q8VYR7; -.
DR SMR; Q8VYR7; -.
DR BioGRID; 4664; 1.
DR STRING; 3702.AT2G47160.2; -.
DR TCDB; 2.A.31.3.1; the anion exchanger (ae) family.
DR iPTMnet; Q8VYR7; -.
DR PaxDb; Q8VYR7; -.
DR ProteomicsDB; 240436; -. [Q8VYR7-1]
DR EnsemblPlants; AT2G47160.1; AT2G47160.1; AT2G47160. [Q8VYR7-1]
DR GeneID; 819329; -.
DR Gramene; AT2G47160.1; AT2G47160.1; AT2G47160. [Q8VYR7-1]
DR KEGG; ath:AT2G47160; -.
DR Araport; AT2G47160; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q8VYR7; -.
DR PhylomeDB; Q8VYR7; -.
DR PRO; PR:Q8VYR7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYR7; baseline and differential.
DR Genevisible; Q8VYR7; AT.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046715; F:active borate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0035445; P:borate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0080029; P:cellular response to boron-containing substance levels; IDA:UniProtKB.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0010036; P:response to boron-containing substance; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF00955; HCO3_cotransp; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Anion exchange; Cell membrane;
KW Endosome; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..704
FT /note="Boron transporter 1"
FT /id="PRO_0000079237"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 641..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 74
FT /note="S->P: In bor1-2; reduced boron uptake."
FT /evidence="ECO:0000269|PubMed:12447444"
FT MUTAGEN 86
FT /note="G->E: In bor1-1; reduced boron uptake."
FT /evidence="ECO:0000269|PubMed:12447444"
FT MUTAGEN 373
FT /note="Y->A: Does not affect polar localization and
FT vacuolar targeting."
FT /evidence="ECO:0000269|PubMed:20194745"
FT MUTAGEN 398
FT /note="Y->A: Affects polar localization and vacuolar
FT targeting; when associated with A-405."
FT /evidence="ECO:0000269|PubMed:20194745"
FT MUTAGEN 405
FT /note="Y->A: Affects polar localization and vacuolar
FT targeting; when associated with A-398."
FT /evidence="ECO:0000269|PubMed:20194745"
SQ SEQUENCE 704 AA; 78605 MW; 5FEF25C64CAADA38 CRC64;
MEETFVPFEG IKNDLKGRLM CYKQDWTGGF KAGFRILAPT TYIFFASAIP VISFGEQLER
STDGVLTAVQ TLASTAICGM IHSIIGGQPL LILGVAEPTV IMYTFMFNFA KARPELGRDL
FLAWSGWVCV WTALMLFVLA ICGACSIINR FTRVAGELFG LLIAMLFMQQ AIKGLVDEFR
IPERENQKLK EFLPSWRFAN GMFALVLSFG LLLTGLRSRK ARSWRYGTGW LRSLIADYGV
PLMVLVWTGV SYIPAGDVPK GIPRRLFSPN PWSPGAYGNW TVVKEMLDVP IVYIIGAFIP
ASMIAVLYYF DHSVASQLAQ QKEFNLRKPS SYHYDLLLLG FLTLMCGLLG VPPSNGVIPQ
SPMHTKSLAT LKYQLLRNRL VATARRSIKT NASLGQLYDN MQEAYHHMQT PLVYQQPQGL
KELKESTIQA TTFTGNLNAP VDETLFDIEK EIDDLLPVEV KEQRVSNLLQ STMVGGCVAA
MPILKMIPTS VLWGYFAFMA IESLPGNQFW ERILLLFTAP SRRFKVLEDY HATFVETVPF
KTIAMFTLFQ TTYLLICFGL TWIPIAGVMF PLMIMFLIPV RQYLLPRFFK GAHLQDLDAA
EYEEAPALPF NLAAETEIGS TTSYPGDLEI LDEVMTRSRG EFRHTSSPKV TSSSSTPVNN
RSLSQVFSPR VSGIRLGQMS PRVVGNSPKP ASCGRSPLNQ SSSN
