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Q9SL42

- PIN1_ARATH

UniProt

Q9SL42 - PIN1_ARATH

Protein

Peptidyl-prolyl cis-trans isomerase Pin1

Gene

PIN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.1 Publication

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: TAIR
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. protein peptidyl-prolyl isomerization Source: GOC
    3. regulation of cell cycle Source: TAIR

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciARA:AT2G18040-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase Pin1 (EC:5.2.1.8)
    Short name:
    PPIase Pin1
    Alternative name(s):
    PIN1At
    Rotamase Pin1
    Gene namesi
    Name:PIN1
    Ordered Locus Names:At2g18040
    ORF Names:T27K22.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G18040.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. endoplasmic reticulum Source: TAIR
    3. plasma membrane Source: TAIR
    4. plasmodesma Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 119119Peptidyl-prolyl cis-trans isomerase Pin1PRO_0000193440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9SL42.
    PRIDEiQ9SL42.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems and flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9SL42.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGL24O827944EBI-2618990,EBI-592083
    SOC1O646453EBI-2618990,EBI-592041

    Protein-protein interaction databases

    IntActiQ9SL42. 2 interactions.

    Structurei

    Secondary structure

    1
    119
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Beta strandi20 – 245
    Helixi38 – 5316
    Helixi60 – 656
    Helixi69 – 735
    Beta strandi76 – 805
    Beta strandi82 – 865
    Helixi89 – 968
    Beta strandi99 – 1013
    Beta strandi106 – 1083
    Beta strandi111 – 1133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J6YNMR-A1-119[»]
    ProteinModelPortaliQ9SL42.
    SMRiQ9SL42. Positions 1-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9SL42.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 119116PpiCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PpiC/parvulin rotamase family.Curated
    Contains 1 PpiC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0760.
    HOGENOMiHOG000275331.
    InParanoidiQ9SL42.
    KOiK09578.
    OMAiETVRASH.
    PhylomeDBiQ9SL42.

    Family and domain databases

    InterProiIPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    [Graphical view]
    PfamiPF00639. Rotamase. 1 hit.
    [Graphical view]
    PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9SL42-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE    50
    DIVSGKANFE EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG 100
    DISDIVDTDS GVHIIKRTA 119
    Length:119
    Mass (Da):13,015
    Last modified:May 1, 2000 - v1
    Checksum:iE926CB566E76A0A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006201 Genomic DNA. Translation: AAD20122.1.
    CP002685 Genomic DNA. Translation: AEC06719.1.
    AF360318 mRNA. Translation: AAK26028.1.
    AY057514 mRNA. Translation: AAL09755.1.
    AY056314 mRNA. Translation: AAL07163.1.
    AY085059 mRNA. Translation: AAM61615.1.
    F13919 mRNA. Translation: CAA23077.1.
    PIRiE84559.
    RefSeqiNP_179395.1. NM_127360.3.
    UniGeneiAt.20592.

    Genome annotation databases

    EnsemblPlantsiAT2G18040.1; AT2G18040.1; AT2G18040.
    GeneIDi816316.
    KEGGiath:AT2G18040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006201 Genomic DNA. Translation: AAD20122.1 .
    CP002685 Genomic DNA. Translation: AEC06719.1 .
    AF360318 mRNA. Translation: AAK26028.1 .
    AY057514 mRNA. Translation: AAL09755.1 .
    AY056314 mRNA. Translation: AAL07163.1 .
    AY085059 mRNA. Translation: AAM61615.1 .
    F13919 mRNA. Translation: CAA23077.1 .
    PIRi E84559.
    RefSeqi NP_179395.1. NM_127360.3.
    UniGenei At.20592.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J6Y NMR - A 1-119 [» ]
    ProteinModelPortali Q9SL42.
    SMRi Q9SL42. Positions 1-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9SL42. 2 interactions.

    Proteomic databases

    PaxDbi Q9SL42.
    PRIDEi Q9SL42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G18040.1 ; AT2G18040.1 ; AT2G18040 .
    GeneIDi 816316.
    KEGGi ath:AT2G18040.

    Organism-specific databases

    TAIRi AT2G18040.

    Phylogenomic databases

    eggNOGi COG0760.
    HOGENOMi HOG000275331.
    InParanoidi Q9SL42.
    KOi K09578.
    OMAi ETVRASH.
    PhylomeDBi Q9SL42.

    Enzyme and pathway databases

    BioCyci ARA:AT2G18040-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9SL42.
    PROi Q9SL42.

    Gene expression databases

    Genevestigatori Q9SL42.

    Family and domain databases

    InterProi IPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    [Graphical view ]
    Pfami PF00639. Rotamase. 1 hit.
    [Graphical view ]
    PROSITEi PS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase."
      Landrieu I., de Veylder L., Fruchart J.-S., Odaert B., Casteels P., Portetelle D., Van Montagu M., Inze D., Lippens G.
      J. Biol. Chem. 275:10577-10581(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-119.
      Strain: cv. Columbia.
      Tissue: Dry seed.
    7. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
      Aryal U.K., Krochko J.E., Ross A.R.
      J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein."
      Landrieu I., Wieruszeski J.-M., Odaert B., Inze D., Grzesiek S., Lippen G.
      J. Biomol. NMR 17:271-272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-18 AND 36-119.
    9. "Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana."
      Landrieu I., Wieruszeski J.-M., Wintjens R., Inze D., Lippens G.
      J. Mol. Biol. 320:321-332(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiPIN1_ARATH
    AccessioniPrimary (citable) accession number: Q9SL42
    Secondary accession number(s): Q42334
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Like all plant Pin1-type PPIases, do not contain the N-terminal WW domain found in other eukaryotic parvulins, but contains a four-amino acid insertion next to the phospho-specific recognition site of the active site. These extra amino acids may be important for mediating the substrate interaction of plant enzymes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3