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   24-JAN-2024, entry version 142.
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.P13689; -.
DR   GlyCosmos; P13689; 1 site, No reported glycans.
DR   iPTMnet; P13689; -.
DR   PaxDb; 4577-GRMZM2G116204_P01; -.
DR   MaizeGDB; 25342; -.
DR   eggNOG; ENOG502RXJU; Eukaryota.
DR   InParanoid; P13689; -.
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   CDD; cd02220; cupin_ABP1; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000526; Auxin-bd.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR37236; AUXIN-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR37236:SF1; AUXIN-BINDING PROTEIN 1; 1.
DR   Pfam; PF02041; Auxin_BP; 1.
DR   PRINTS; PR00655; AUXINBINDNGP.
DR   SUPFAM; SSF51182; RmlC-like cupins; 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
//