Reviewed, UniProtKB/Swiss-Prot Q9SL42 (PIN1_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Isomerase Rotamase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell cycle Traceable author statement. Source: TAIR
Cellular component	plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from genetic interaction. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 119

119

Peptidyl-prolyl cis-trans isomerase 1

PRO_0000193440

Regions

Domain

4 – 119

116

PpiC

Secondary structure

1

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119

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Beta strand

20 – 24

5

Helix

38 – 53

16

Helix

60 – 65

6

Helix

69 – 73

5

Beta strand

76 – 80

5

Beta strand

82 – 86

5

Helix

89 – 96

8

Beta strand

99 – 101

3

Beta strand

106 – 108

3

Beta strand

111 – 113

3

Sequences

	Sequence		Length	Mass (Da)
	Q9SL42-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E926CB566E76A0A3	FASTA	119	13,015
	10 20 30 40 50 60 MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE DIVSGKANFE 70 80 90 100 110 EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG DISDIVDTDS GVHIIKRTA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00529445.

PIR

E84559.

RefSeq

NP_179395.1.

UniGene

At.20592

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J6Y	NMR	-	A	1-119	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9SL42.

Proteomic databases

PRIDE

Q9SL42.

Genome annotation databases

GeneID

816316.

GenomeReviews

Gene locus AT2G18040 in contig CT485783_GR.

KEGG

ath:AT2G18040.

NMPDR

fig|3702.1.peg.8800.

Organism-specific databases

TAIR

At2g18040.

Phylogenomic databases

HOGENOM

HBG526275.

InParanoid

Q9SL42.

OMA

EMQPSFE.

PhylomeDB

Q9SL42.

Enzyme and pathway databases

BRENDA

5.2.1.8. 302.

Gene expression databases

ArrayExpress

Q9SL42.

Genevestigator

Q9SL42.

GermOnline

AT2G18040. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
[Graphical view]

Pfam

PF00639. Rotamase. 1 hit.
[Graphical view]

PROSITE

PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PIN1_ARATH

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)