ABP1_MAIZE
ID ABP1_MAIZE Reviewed; 201 AA.
AC P13689; Q41193;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Auxin-binding protein 1 {ECO:0000303|PubMed:2555179};
DE Short=ABP {ECO:0000303|PubMed:2555179};
DE AltName: Full=ERABP1 {ECO:0000303|PubMed:7693132};
DE Flags: Precursor;
GN Name=ABP1 {ECO:0000303|PubMed:2555179};
GN Synonyms=AUX311 {ECO:0000303|PubMed:1650260};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-67; 78-91; 110-119 AND
RP 185-194, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Coleoptile;
RX PubMed=2555179; DOI=10.1002/j.1460-2075.1989.tb08380.x;
RA Hesse T., Feldwisch J., Balshuesemann D., Bauw G., Puype M.,
RA Vandekerckhove J., Loebler M., Klaembt D., Schell J., Palme K.;
RT "Molecular cloning and structural analysis of a gene from Zea mays (L.)
RT coding for a putative receptor for the plant hormone auxin.";
RL EMBO J. 8:2453-2461(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2555180; DOI=10.1002/j.1460-2075.1989.tb08381.x;
RA Tillmann U., Viola G., Kayser B., Siemeister G., Hesse T., Palme K.,
RA Loebler M., Klaembt D.;
RT "cDNA clones of the auxin-binding protein from corn coleoptiles (Zea mays
RT L.): isolation and characterization by immunological methods.";
RL EMBO J. 8:2463-2467(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 39-69.
RC STRAIN=cv. Golden cross Bantam;
RX PubMed=2542939; DOI=10.1073/pnas.86.10.3564;
RA Inohara N., Shimomura S., Fukui T., Futai M.;
RT "Auxin-binding protein located in the endoplasmic reticulum of maize
RT shoots: molecular cloning and complete primary structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3564-3568(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. LG11; TISSUE=Shoot;
RX PubMed=1650260; DOI=10.1007/bf00015087;
RA Yu L.X., Lazarus C.M.;
RT "Structure and sequence of an auxin-binding protein gene from maize (Zea
RT mays L.).";
RL Plant Mol. Biol. 16:925-930(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-13.
RX PubMed=1668837;
RA Lazarus C.M., Napier R.M., Yu L.X., Lynas C., Venis M.A.;
RT "Auxin-binding protein -- antibodies and genes.";
RL Symp. Soc. Exp. Biol. 45:129-148(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=7693132; DOI=10.1046/j.1365-313x.1993.04030423.x;
RA Schwob E., Choi S.-Y., Simmons C., Migliaccio F., Ilag L., Hesse T.,
RA Palme K., Soell D.;
RT "Molecular analysis of three maize 22 kDa auxin-binding protein genes
RT -- transient promoter expression and regulatory regions.";
RL Plant J. 4:423-432(1993).
RN [7]
RP REVIEW.
RX PubMed=1650041; DOI=10.1016/0968-0004(91)90028-t;
RA Napier R.M., Venis M.A.;
RT "From auxin-binding protein to plant hormone receptor?";
RL Trends Biochem. Sci. 16:72-75(1991).
RN [8]
RP PRELIMINARY DISULFIDE BOND.
RX PubMed=11749971; DOI=10.1016/s0014-5793(01)03196-9;
RA Feckler C., Muster G., Feser W., Romer A., Palme K.;
RT "Mass spectrometric analysis reveals a cysteine bridge between residues 2
RT and 61 of the auxin-binding protein 1 from Zea mays L.";
RL FEBS Lett. 509:446-450(2001).
RN [9] {ECO:0007744|PDB:1LR5, ECO:0007744|PDB:1LRH}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-201 IN COMPLEX WITH THE
RP SYNTHETIC AUXIN 1-NAPHTHALENEACETATE AND ZINC ION, GLYCOSYLATION AT
RP ASN-133, MUTAGENESIS OF 199-ASP-GLU-200, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=12065401; DOI=10.1093/emboj/cdf291;
RA Woo E.J., Marshall J., Bauly J., Chen J.G., Venis M., Napier R.M.,
RA Pickersgill R.W.;
RT "Crystal structure of auxin-binding protein 1 in complex with auxin.";
RL EMBO J. 21:2877-2885(2002).
CC -!- FUNCTION: Receptor for the plant hormone auxin.
CC {ECO:0000303|PubMed:2555179}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12065401}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:2555179}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, coleoptiles, leaves, stems,
CC tassels and ears. {ECO:0000269|PubMed:7693132}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12065401,
CC ECO:0000269|PubMed:2555179}.
CC -!- CAUTION: Was originally thought to have a disulfide bond between Cys-40
CC and Cys-99. {ECO:0000305|PubMed:11749971}.
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DR EMBL; X16309; CAA34376.1; -; mRNA.
DR EMBL; J04550; AAA33436.1; -; mRNA.
DR EMBL; X56737; CAA40061.1; -; Genomic_DNA.
DR EMBL; X16308; CAA34375.1; -; mRNA.
DR EMBL; S53630; AAB25115.1; -; mRNA.
DR EMBL; L08425; AAA33430.1; -; Genomic_DNA.
DR PIR; S16262; S16262.
DR PDB; 1LR5; X-ray; 1.90 A; A/B/C/D=39-201.
DR PDB; 1LRH; X-ray; 1.90 A; A/B/C/D=39-201.
DR PDBsum; 1LR5; -.
DR PDBsum; 1LRH; -.
DR AlphaFoldDB; P13689; -.
DR SMR; P13689; -.
DR ELM; P13689; -.
DR STRING; 4577.GRMZM2G116204_P01; -.
DR iPTMnet; P13689; -.
DR PaxDb; P13689; -.
DR MaizeGDB; 25342; -.
DR eggNOG; ENOG502RXJU; Eukaryota.
DR EvolutionaryTrace; P13689; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P13689; baseline and differential.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0010011; F:auxin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IBA:GO_Central.
DR GO; GO:0045793; P:positive regulation of cell size; IBA:GO_Central.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IBA:GO_Central.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR000526; Auxin-bd.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR37236; PTHR37236; 1.
DR Pfam; PF02041; Auxin_BP; 1.
DR PRINTS; PR00655; AUXINBINDNGP.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW Receptor; Reference proteome; Signal; Zinc.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:2542939,
FT ECO:0000269|PubMed:2555179"
FT CHAIN 39..201
FT /note="Auxin-binding protein 1"
FT /id="PRO_0000020614"
FT MOTIF 198..201
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12065401"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12065401"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12065401"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12065401"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12065401"
FT DISULFID 40..193
FT /evidence="ECO:0000269|PubMed:12065401"
FT VARIANT 13
FT /note="A -> G"
FT /evidence="ECO:0000269|PubMed:1668837"
FT VARIANT 141
FT /note="N -> S"
FT MUTAGEN 199..200
FT /note="DE->EQ: Prevents ER retention."
FT /evidence="ECO:0000269|PubMed:12065401"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1LR5"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1LR5"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1LR5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1LR5"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1LR5"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1LR5"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:1LR5"
SQ SEQUENCE 201 AA; 21977 MW; 1AF11DFEC247D9D0 CRC64;
MAPDLSELAA AAAARGAYLA GVGVAVLLAA SFLPVAESSC VRDNSLVRDI SQMPQSSYGI
EGLSHITVAG ALNHGMKEVE VWLQTISPGQ RTPIHRHSCE EVFTVLKGKG TLLMGSSSLK
YPGQPQEIPF FQNTTFSIPV NDPHQVWNSD EHEDLQVLVI ISRPPAKIFL YDDWSMPHTA
AVLKFPFVWD EDCFEAAKDE L
