Q9SL42 (PIN1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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 Reference 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	cytosol Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR plasmodesma Inferred from direct assay. Source: TAIR
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from genetic interaction. Source: TAIR protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGL24	O82794	4	EBI-2618990,EBI-592083
SOC1	O64645	3	EBI-2618990,EBI-592041

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 119

119

Peptidyl-prolyl cis-trans isomerase Pin1

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 [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]	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: 14593172] [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. , 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.
[7]	"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.
[8]	"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.
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.

IPI

IPI00529445.

PIR

E84559.

RefSeq

NP_179395.1. NM_127360.3.

UniGene

At.20592.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q9SL42.

SMR

Q9SL42. Positions 1-119.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9SL42. 2 interactions.

STRING

Q9SL42.

Proteomic databases

PRIDE

Q9SL42.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT2G18040.1; AT2G18040.1; AT2G18040.

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

GeneTree

EPGT00050000008211.

HOGENOM

HBG526275.

InParanoid

Q9SL42.

OMA

HIIKRTA.

PhylomeDB

Q9SL42.

ProtClustDB

CLSN2683929.

Gene expression databases

ArrayExpress

Q9SL42.

Genevestigator

Q9SL42.

GermOnline

AT2G18040. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
[Graphical view]

KO

K09578.

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:	November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program