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P13689

- ABP1_MAIZE

UniProt

P13689 - ABP1_MAIZE

Protein

Auxin-binding protein 1

Gene

ABP1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    This is probably a receptor for the plant hormone auxin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi95 – 951Zinc
    Binding sitei95 – 951Auxin1 Publication
    Metal bindingi97 – 971Zinc
    Metal bindingi101 – 1011Zinc
    Binding sitei101 – 1011Auxin1 Publication
    Metal bindingi144 – 1441Zinc

    GO - Molecular functioni

    1. auxin binding Source: UniProtKB
    2. receptor activity Source: InterPro
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Auxin signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Auxin-binding protein 1
    Short name:
    ABP
    Alternative name(s):
    ERABP1
    Gene namesi
    Name:ABP1
    Synonyms:AUX311
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiP13689.
    MaizeGDBi25342.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 2002DE → EQ: Prevents ER retention. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Add
    BLAST
    Chaini39 – 201163Auxin-binding protein 1PRO_0000020614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 1931 Publication
    Glycosylationi133 – 1331N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP13689.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 494
    Helixi50 – 523
    Beta strandi63 – 697
    Helixi71 – 744
    Beta strandi77 – 8610
    Beta strandi94 – 996
    Beta strandi101 – 1077
    Beta strandi110 – 1145
    Beta strandi117 – 1215
    Beta strandi126 – 1305
    Beta strandi134 – 1385
    Beta strandi144 – 1474
    Beta strandi151 – 1533
    Beta strandi155 – 16511
    Beta strandi168 – 1736
    Helixi178 – 1803
    Beta strandi182 – 1865
    Turni188 – 1903
    Helixi191 – 1966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LR5X-ray1.90A/B/C/D39-201[»]
    1LRHX-ray1.90A/B/C/D39-201[»]
    ProteinModelPortaliP13689.
    SMRiP13689. Positions 39-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13689.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi198 – 2014Prevents secretion from ER

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR000526. Auxin-bd.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PfamiPF02041. Auxin_BP. 1 hit.
    [Graphical view]
    PRINTSiPR00655. AUXINBINDNGP.
    SUPFAMiSSF51182. SSF51182. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13689-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPDLSELAA AAAARGAYLA GVGVAVLLAA SFLPVAESSC VRDNSLVRDI    50
    SQMPQSSYGI EGLSHITVAG ALNHGMKEVE VWLQTISPGQ RTPIHRHSCE 100
    EVFTVLKGKG TLLMGSSSLK YPGQPQEIPF FQNTTFSIPV NDPHQVWNSD 150
    EHEDLQVLVI ISRPPAKIFL YDDWSMPHTA AVLKFPFVWD EDCFEAAKDE 200
    L 201
    Length:201
    Mass (Da):21,977
    Last modified:January 1, 1990 - v1
    Checksum:i1AF11DFEC247D9D0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131A → G.1 Publication
    Natural varianti141 – 1411N → S.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS16262.
    RefSeqiNP_001105312.1. NM_001111842.1.
    UniGeneiZm.152.

    Genome annotation databases

    GeneIDi542232.
    KEGGizma:542232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S16262.
    RefSeqi NP_001105312.1. NM_001111842.1.
    UniGenei Zm.152.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LR5 X-ray 1.90 A/B/C/D 39-201 [» ]
    1LRH X-ray 1.90 A/B/C/D 39-201 [» ]
    ProteinModelPortali P13689.
    SMRi P13689. Positions 39-198.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P13689.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 542232.
    KEGGi zma:542232.

    Organism-specific databases

    Gramenei P13689.
    MaizeGDBi 25342.

    Miscellaneous databases

    EvolutionaryTracei P13689.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR000526. Auxin-bd.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    Pfami PF02041. Auxin_BP. 1 hit.
    [Graphical view ]
    PRINTSi PR00655. AUXINBINDNGP.
    SUPFAMi SSF51182. SSF51182. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiABP1_MAIZE
    AccessioniPrimary (citable) accession number: P13689
    Secondary accession number(s): Q41193
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to have a disulfide bond between Cys-40 and Cys-99.1 Publication

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3