P13689 (ABP1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Auxin-binding protein 1
Short name=ABP

Alternative name(s):
ERABP1

Gene names

Name:	ABP1
Synonyms:	AUX311

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is probably a receptor for the plant hormone auxin.
Subunit structure	Homodimer.
Subcellular location	Endoplasmic reticulum lumen.
Caution	Was originally (Ref.8) thought to have a disulfide bond between Cys-40 and Cys-99.

Ontologies

Keywords
Biological process	Auxin signaling pathway
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	auxin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from electronic annotation. Source: EnsemblPlants/Gramene positive regulation of DNA endoreduplication Inferred from electronic annotation. Source: EnsemblPlants/Gramene positive regulation of cell division Inferred from electronic annotation. Source: EnsemblPlants/Gramene positive regulation of cell size Inferred from electronic annotation. Source: EnsemblPlants/Gramene unidimensional cell growth Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	auxin binding Inferred from direct assay Ref.9. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 38

38

Chain

39 – 201

163

Auxin-binding protein 1

PRO_0000020614

Regions

Motif

198 – 201

4

Prevents secretion from ER

Sites

Metal binding

95

1

Zinc

Metal binding

97

1

Zinc

Metal binding

101

1

Zinc

Metal binding

144

1

Zinc

Binding site

95

1

Auxin

Binding site

101

1

Auxin

Amino acid modifications

Glycosylation

133

1

N-linked (GlcNAc...)

Disulfide bond

40 ↔ 193

Ref.8 Ref.9

Natural variations

Natural variant

13

1

A → G. Ref.5

Natural variant

141

1

N → S.

Experimental info

Mutagenesis

199 – 200

2

DE → EQ: Prevents ER retention. Ref.9

Secondary structure

1

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201

Helix Strand Turn

Details...

Beta strand

46 – 49

4

Helix

50 – 52

3

Beta strand

63 – 69

7

Helix

71 – 74

4

Beta strand

77 – 86

10

Beta strand

94 – 99

6

Beta strand

101 – 107

7

Beta strand

110 – 114

5

Beta strand

117 – 121

5

Beta strand

126 – 130

5

Beta strand

134 – 138

5

Beta strand

144 – 147

4

Beta strand

151 – 153

3

Beta strand

155 – 165

11

Beta strand

168 – 173

6

Helix

178 – 180

3

Beta strand

182 – 186

5

Turn

188 – 190

3

Helix

191 – 196

6

Sequences

	Sequence		Length	Mass (Da)
	P13689 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 1AF11DFEC247D9D0	FASTA	201	21,977
	10 20 30 40 50 60 MAPDLSELAA AAAARGAYLA GVGVAVLLAA SFLPVAESSC VRDNSLVRDI SQMPQSSYGI 70 80 90 100 110 120 EGLSHITVAG ALNHGMKEVE VWLQTISPGQ RTPIHRHSCE EVFTVLKGKG TLLMGSSSLK 130 140 150 160 170 180 YPGQPQEIPF FQNTTFSIPV NDPHQVWNSD EHEDLQVLVI ISRPPAKIFL YDDWSMPHTA 190 200 AVLKFPFVWD EDCFEAAKDE L

References

[1]	"Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin." Hesse T., Feldwisch J., Balshuesemann D., Bauw G., Puype M., Vandekerckhove J., Loebler M., Klaembt D., Schell J., Palme K. EMBO J. 8:2453-2461(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Coleoptile.
[2]	"cDNA clones of the auxin-binding protein from corn coleoptiles (Zea mays L.): isolation and characterization by immunological methods." Tillmann U., Viola G., Kayser B., Siemeister G., Hesse T., Palme K., Loebler M., Klaembt D. EMBO J. 8:2463-2467(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Auxin-binding protein located in the endoplasmic reticulum of maize shoots: molecular cloning and complete primary structure." Inohara N., Shimomura S., Fukui T., Futai M. Proc. Natl. Acad. Sci. U.S.A. 86:3564-3568(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and sequence of an auxin-binding protein gene from maize (Zea mays L.)." Yu L.X., Lazarus C.M. Plant Mol. Biol. 16:925-930(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. LG11. Tissue: Shoot.
[5]	"Auxin-binding protein -- antibodies and genes." Lazarus C.M., Napier R.M., Yu L.X., Lynas C., Venis M.A. Symp. Soc. Exp. Biol. 45:129-148(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, VARIANT GLY-13.
[6]	"Molecular analysis of three maize 22 kDa auxin-binding protein genes -- transient promoter expression and regulatory regions." Schwob E., Choi S.-Y., Simmons C., Migliaccio F., Ilag L., Hesse T., Palme K., Soell D. Plant J. 4:423-432(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Wisconsin 22.
[7]	"From auxin-binding protein to plant hormone receptor?" Napier R.M., Venis M.A. Trends Biochem. Sci. 16:72-75(1991) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[8]	"Mass spectrometric analysis reveals a cysteine bridge between residues 2 and 61 of the auxin-binding protein 1 from Zea mays L." Feckler C., Muster G., Feser W., Romer A., Palme K. FEBS Lett. 509:446-450(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY DISULFIDE BOND.
[9]	"Crystal structure of auxin-binding protein 1 in complex with auxin." Woo E.J., Marshall J., Bauly J., Chen J.G., Venis M., Napier R.M., Pickersgill R.W. EMBO J. 21:2877-2885(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH AUXIN AND ZINC ION, GLYCOSYLATION, MUTAGENESIS OF 199-ASP-GLU-200, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16309 mRNA. Translation: CAA34376.1.
J04550 mRNA. Translation: AAA33436.1.
X56737 Genomic DNA. Translation: CAA40061.1.
X16308 mRNA. Translation: CAA34375.1.
S53630 mRNA. Translation: AAB25115.1.
L08425 Genomic DNA. Translation: AAA33430.1.

PIR

S16262.

RefSeq

NP_001105312.1. NM_001111842.1.

UniGene

Zm.152.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LR5	X-ray	1.90	A/B/C/D	39-198	[»]
1LRH	X-ray	1.90	A/B/C/D	39-198	[»]

ProteinModelPortal

P13689.

SMR

P13689. Positions 39-198.

ModBase

Search...

Proteomic databases

PRIDE

P13689.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

542232.

KEGG

zma:542232.

Organism-specific databases

Gramene

P13689.

MaizeGDB

25342.

Family and domain databases

Gene3D

2.60.120.10. 1 hit.

InterPro

IPR000526. Auxin-bd.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]

Pfam

PF02041. Auxin_BP. 1 hit.
[Graphical view]

PRINTS

PR00655. AUXINBINDNGP.

SUPFAM

SSF51182. RmlC_like_cupin. 1 hit.

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P13689.

Entry information

Entry name

ABP1_MAIZE

Accession

Primary (citable) accession number: P13689
Secondary accession number(s): Q41193

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program