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P13689 (ABP1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Auxin-binding protein 1

Short name=ABP
Alternative name(s):
ERABP1
Gene names
Name:ABP1
Synonyms:AUX311
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processAuxin signaling pathway
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processauxin-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionauxin 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838
Chain39 – 201163Auxin-binding protein 1
PRO_0000020614

Regions

Motif198 – 2014Prevents secretion from ER

Sites

Metal binding951Zinc
Metal binding971Zinc
Metal binding1011Zinc
Metal binding1441Zinc
Binding site951Auxin
Binding site1011Auxin

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...)
Disulfide bond40 ↔ 193 Ref.8 Ref.9

Natural variations

Natural variant131A → G. Ref.5
Natural variant1411N → S.

Experimental info

Mutagenesis199 – 2002DE → EQ: Prevents ER retention. Ref.9

Secondary structure

..................................... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13689 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 1AF11DFEC247D9D0

FASTA20121,977
        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 

« Hide

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.
PIRS16262.
RefSeqNP_001105312.1. NM_001111842.1.
UniGeneZm.152.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LR5X-ray1.90A/B/C/D39-201[»]
1LRHX-ray1.90A/B/C/D39-201[»]
ProteinModelPortalP13689.
SMRP13689. Positions 39-198.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP13689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542232.
KEGGzma:542232.

Organism-specific databases

GrameneP13689.
MaizeGDB25342.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR000526. Auxin-bd.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF02041. Auxin_BP. 1 hit.
[Graphical view]
PRINTSPR00655. AUXINBINDNGP.
SUPFAMSSF51182. SSF51182. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13689.

Entry information

Entry nameABP1_MAIZE
AccessionPrimary (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: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references