Reviewed, UniProtKB/Swiss-Prot Q42406 (CP18D_ARATH)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase CYP18-4
      Short name=PPIase CYP18-4
    EC=5.2.1.8
Alternative name(s):
    Rotamase cyclophilin-5
    Cyclophilin of 18 kDa 4
      Short name=Cyclophilin-1

Gene names

Name:	CYP18-4
Synonyms:	43H1, CYP1, ROC5
Ordered Locus Names:	At4g34870
ORF Names:	T11I11.110

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase By similarity.
Subcellular location	Cytoplasm Probable.
Tissue specificity	Ubiquitous, with higher levels in roots and flowers. Confined to vascular tissues. Also detected in stigmas, base of siliques and anthers. Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Chaperone Isomerase Rotamase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 172	172	Peptidyl-prolyl cis-trans isomerase CYP18-4		PRO_0000064134
Regions
	Domain	7 – 170	164	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q42406-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C6E082F594E73913	FASTA	172	18,378
	10 20 30 40 50 60 MSNPRVFFDM SLSGTPIGRI EMELFADTTP NTAENFRALC TGEKGMGKLG KPLHFKGSIF 70 80 90 100 110 120 HRVIPGFMCQ GGDFTAKNGT GGESIYGAKF KDENFIKKHT GAGILSMANS GPNTNGSQFF 130 140 150 160 170 ICTDKTSWLD GKHVVFGQVV KGLDVVKAIE KVGSDSGKTS KVVTITDCGQ LS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide and deduced amino acid sequences of a peptidyl-prolyl cis-trans isomerase from Arabidopsis thaliana." Hayman G.T., Miernyk J.A. Biochim. Biophys. Acta 1219:536-538(1994) [PubMed: 7918654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Cloning and sequence analysis of genes for cyclophilin from Arabidopsis thaliana." Saito T., Ishiguro S., Ashida H., Kawamukai M., Matsuda H., Ochiai H., Nakagawa T. Plant Cell Physiol. 36:377-382(1995) [PubMed: 7767603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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]	"Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins." Chou I.T., Gasser C.S. Plant Mol. Biol. 35:873-892(1997) [PubMed: 9426607] [Abstract] Cited for: TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Leaf.
[7]	"Two cytosolic cyclophilin genes of Arabidopsis thaliana differently regulated in temporal- and organ-specific expression." Saito T., Tadakuma K., Takahashi N., Ashida H., Tanaka K., Kawamukai M., Matsuda H., Nakagawa T. Biosci. Biotechnol. Biochem. 63:632-637(1999) [PubMed: 10361676] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis." He Z., Li L., Luan S. Plant Physiol. 134:1248-1267(2004) [PubMed: 15047905] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"The Arabidopsis cyclophilin gene family." Romano P.G.N., Horton P., Gray J.E. Plant Physiol. 134:1268-1282(2004) [PubMed: 15051864] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U07276 mRNA. Translation: AAA66197.1. U32186 Genomic DNA. Translation: AAA75512.1. AL079347 Genomic DNA. Translation: CAB45448.1. AL161586 Genomic DNA. Translation: CAB80204.1. AY054468 mRNA. Translation: AAK96660.1. BT006560 mRNA. Translation: AAP21368.1. AY087606 mRNA. Translation: AAM65147.1.
IPI	IPI00534382.
PIR	S50141.
RefSeq	NP_195213.1.
UniGene	At.421 At.71932
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
SMR	Q42406. Positions 1-171.
ModBase	Search...
Proteomic databases
PRIDE	Q42406.
ProMEX	Q42406.
Genome annotation databases
GeneID	829639.
GenomeReviews	Gene locus AT4G34870 in contig CT486007_GR.
KEGG	ath:AT4G34870.
NMPDR	fig|3702.1.peg.21561.
Organism-specific databases
GeneFarm	5174.
TAIR	At4g34870.
Phylogenomic databases
OMA	Q42406. PAGRVEM.
Enzyme and pathway databases
BRENDA	5.2.1.8. 302.
Gene expression databases
ArrayExpress	Q42406.
GermOnline	AT4G34870. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP18D_ARATH

Accession

Primary (citable) accession number: Q42406

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)