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Reviewed, UniProtKB/Swiss-Prot Q9SL42 (PIN1_ARATH)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase 1
    EC=5.2.1.8
Alternative name(s):
    Rotamase Pin1
    PPIase Pin1
    PIN1At
Gene names
Name: PIN1
Ordered Locus Names: At2g18040
ORF Names: T27K22.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

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.

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell cycle

Traceable author statement. Source: TAIR

   Cellular componentplasma membrane

Inferred from direct assay. Source: TAIR

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from genetic interaction. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 119119Peptidyl-prolyl cis-trans isomerase 1
PRO_0000193440

Regions

Domain4 – 119116PpiC

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SL42-1 [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: 10744752] [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: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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].
[5]"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: 8580968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-119.
Strain: cv. Columbia.
Tissue: Dry seed.
[6]"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: 10959635] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-18 AND 36-119.
[7]"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: 12079389] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006201 Genomic DNA. Translation: AAD20122.1.
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.
IPIIPI00529445.
PIRE84559.
RefSeqNP_179395.1.
UniGeneAt.20592

3D structure databases

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

Protein-protein interaction databases

STRINGQ9SL42.

Proteomic databases

PRIDEQ9SL42.

Genome annotation databases

GeneID816316.
GenomeReviewsGene locus AT2G18040 in contig CT485783_GR.
KEGGath:AT2G18040.
NMPDRfig|3702.1.peg.8800.

Organism-specific databases

TAIRAt2g18040.

Phylogenomic databases

HOGENOMHBG526275.
InParanoidQ9SL42.
OMAEMQPSFE.
PhylomeDBQ9SL42.

Enzyme and pathway databases

BRENDA5.2.1.8. 302.

Gene expression databases

ArrayExpressQ9SL42.
GenevestigatorQ9SL42.
GermOnlineAT2G18040. Arabidopsis thaliana.

Family and domain databases

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

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: February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents