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UniProtKB/Swiss-Prot entry Q9SL42


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIN1_ARATH
Primary accession number Q9SL42
Secondary accession number Q42334
Integrated into Swiss-Prot on October 31, 2003
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 58)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase 1
Synonyms EC 5.2.1.8
Rotamase Pin1
PPIase Pin1
PIN1At
Gene name
Name: PIN1
OrderedLocusNames: At2g18040
ORFNames: T27K22.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.275.14.10577; PubMed=10744752 [NCBI, ExPASy, EBI, Israel, Japan]
Landrieu I., de Veylder L., Fruchart J.-S., Odaert B., Casteels P., Portetelle D., Van Montagu M., Inze D., Lippens G.;
"The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase.";
J. Biol. Chem. 275:10577-10581(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-119.
STRAIN=cv. Columbia;
TISSUE=Dry seed;
DOI=10.1046/j.1365-313X.1996.09010101.x; PubMed=8580968 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[6]
STRUCTURE BY NMR OF 1-18 AND 36-119.
DOI=10.1023/A:1008375707703; PubMed=10959635 [NCBI, ExPASy, EBI, Israel, Japan]
Landrieu I., Wieruszeski J.-M., Odaert B., Inze D., Grzesiek S., Lippen G.;
"Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein.";
J. Biomol. NMR 17:271-272(2000).
[7]
STRUCTURE BY NMR.
DOI=10.1016/S0022-2836(02)00429-1; PubMed=12079389 [NCBI, ExPASy, EBI, Israel, Japan]
Landrieu I., Wieruszeski J.-M., Wintjens R., Inze D., Lippens G.;
"Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.";
J. Mol. Biol. 320:321-332(2002).
Comments
  • FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.
  • CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
  • TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
  • 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.
  • SIMILARITY: Belongs to the ppiC/parvulin rotamase family.
  • SIMILARITY: Contains 1 PpiC domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC006201; AAD20122.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360318; AAK26028.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY057514; AAL09755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056314; AAL07163.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085059; AAM61615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
F13919; CAA23077.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00529445; -.
PIR E84559; E84559.
RefSeq NP_179395.1; -.
UniGene At.20592
3D structure databases
PDB
1J6Y; NMR; -; A=1-119.[ExPASy / RCSB / EBI]
PDBsum 1J6Y; -.
ModBase Q9SL42.
Enzyme and pathway databases
BRENDA 5.2.1.8; 302.
Organism-specific databases
TAIR At2g18040; -.
Gene expression databases
ArrayExpress Q9SL42; -.
GermOnline AT2G18040; Arabidopsis thaliana.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from TAIR).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from genetic interaction from TAIR).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
GO:0051726; Biological process: regulation of cell cycle (traceable author statement from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR000297; PPIase_PpiC.
Graphical view of domain structure.
Pfam PF00639; Rotamase; 1.
Pfam graphical view of domain structure.
PROSITE PS01096; PPIC_PPIASE_1; 1.
PS50198; PPIC_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9SL42; -.
Genome annotation databases
GeneID 816316; -.
GenomeReviews CT485783_GR; AT2G18040.
KEGG ath:AT2G18040; -.
NMPDR fig|3702.1.peg.8800; -.
Phylogenomic databases
OMA Q9SL42; EMQPSFE.
Other
ProtoNet Q9SL42.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Isomerase; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   119  119     Peptidyl-prolyl cis-trans isomerase 1. PRO_0000193440
DOMAIN   4   119  116     PpiC. 
STRAND   8    10  3      
STRAND   20    24  5      
HELIX   38    53  16      
HELIX   60    65  6      
HELIX   69    73  5      
STRAND   76    80  5      
STRAND   82    86  5      
HELIX   89    96  8      
STRAND   99   101  3      
STRAND   106   108  3      
STRAND   111   113  3      
Sequence information
Length: 119 AA [This is the length of the unprocessed precursor] Molecular weight: 13015 Da [This is the MW of the unprocessed precursor] CRC64: E926CB566E76A0A3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE DIVSGKANFE 

        70         80         90        100        110 
EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG DISDIVDTDS GVHIIKRTA 

Q9SL42 in FASTA format

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