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Q9SL42 (PIN1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase Pin1

Short name=PPIase Pin1
EC=5.2.1.8
Alternative name(s):
PIN1At
Rotamase Pin1
Gene names
Name:PIN1
Ordered Locus Names:At2g18040
ORF Names:T27K22.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Tissue specificity

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

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.

Sequence similarities

Belongs to the PpiC/parvulin rotamase family.

Contains 1 PpiC domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 119119Peptidyl-prolyl cis-trans isomerase Pin1
PRO_0000193440

Regions

Domain4 – 119116PpiC

Amino acid modifications

Modified residue1031Phosphoserine Ref.7

Secondary structure

....................... 119
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SL42 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E926CB566E76A0A3

FASTA11913,015
        10         20         30         40         50         60 
MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE DIVSGKANFE 

        70         80         90        100        110 
EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG DISDIVDTDS GVHIIKRTA 

« Hide

References

« Hide 'large scale' references
[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]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs."
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. expand/collapse author list , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.
Plant J. 9:101-124(1996) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRE84559.
RefSeqNP_179395.1. NM_127360.3.
UniGeneAt.20592.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J6YNMR-A1-119[»]
ProteinModelPortalQ9SL42.
SMRQ9SL42. Positions 1-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9SL42. 2 interactions.

Proteomic databases

PaxDbQ9SL42.
PRIDEQ9SL42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G18040.1; AT2G18040.1; AT2G18040.
GeneID816316.
KEGGath:AT2G18040.

Organism-specific databases

TAIRAT2G18040.

Phylogenomic databases

eggNOGCOG0760.
HOGENOMHOG000275331.
InParanoidQ9SL42.
KOK09578.
OMAETVRASH.
PhylomeDBQ9SL42.

Enzyme and pathway databases

BioCycARA:AT2G18040-MONOMER.

Gene expression databases

GenevestigatorQ9SL42.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
[Graphical view]
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9SL42.
PROQ9SL42.

Entry information

Entry namePIN1_ARATH
AccessionPrimary (citable) accession number: Q9SL42
Secondary accession number(s): Q42334
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names