Q8LDP4 (CP19D_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP19-4
Short name=PPIase CYP19-4
EC=5.2.1.8

Alternative name(s):
Cyclophilin of 19 kDa 4
Cyclophilin-5
Rotamase CYP19-4

Gene names

Name:	CYP19-4
Synonyms:	CYP5
Ordered Locus Names:	At2g29960
ORF Names:	F23F1.12

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	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. May be involved during embryogenesis and organ development by regulating the folding of EMB30/GNOM, and thus, by modulating its activity. Ref.6
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. Ref.6
Subunit structure	Interacts with EMB30/GNOM. Ref.6
Subcellular location	Cytoplasm. Membrane. Endoplasmic reticulum. Note: Mostly cytoplasmic, also membrane-associated. Present in endoplasmic reticulum and barely secreted. Ref.1 Ref.6
Tissue specificity	Ubiquitous, mostly in aerial organs (at protein level). Ref.1 Ref.6 Ref.7
Developmental stage	Mostly expressed in both apical and basal regions in peduncles and stems (including upper roots) before the bolting stage. Later restricted in the apical region. During embryogenesis, accumulates in all cells during globular stage. From the heart stage, more expressed in inner cells than in epidermal cells (at protein level). Ref.1 Ref.6
Induction	Slightly induced by cold and salt stresses. Ref.1 Ref.6
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Cyclosporin
Molecular function	Chaperone Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi stack Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay Ref.6. Source: TAIR endoplasmic reticulum Inferred from direct assay. Source: TAIR membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay Ref.6. Source: TAIR multivesicular body 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 direct assay Ref.6. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8LDP4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 201	178	Peptidyl-prolyl cis-trans isomerase CYP19-4		PRO_0000044626
Regions
	Domain	35 – 198	164	PPIase cyclophilin-type
Experimental info
	Sequence conflict	30	1	V → I in AAB71401. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: FBE07EB9EC546109	FASTA	201	21,534
	10 20 30 40 50 60 MAKASFILLG TLFLFGAIAS IQAKEDLKEV THKVYFDVEI DGKSAGRVVI GLFGKAVPKT 70 80 90 100 110 120 AENFRALCTG EKGVGKSGKP LHYKGSKFHR IIPSFMIQGG DFTHGNGMGG ESIYGQKFAD 130 140 150 160 170 180 ENFKLKHTGP GVLSMANSGE DTNGSQFFIT TVTTSWLDGR HVVFGKVVQG MDVVYKIEAE 190 200 GKQSGTPKSK VVIADSGELP L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a gene for cyclophilin which contains an amino-terminal endoplasmic reticulum-targeting signal." Saito T., Niwa Y., Ashida H., Tanaka K., Kawamukai M., Matsuda H., Nakagawa T. Plant Cell Physiol. 40:77-87(1999) [PubMed: 10189705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INDUCTION. Strain: cv. Landsberg erecta.
[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]	"A conserved domain of the Arabidopsis GNOM protein mediates subunit interaction and cyclophilin 5 binding." Grebe M., Gadea J., Steinmann T., Kientz M., Rahfeld J.-U., Salchert K., Koncz C., Juergens G. Plant Cell 12:343-356(2000) [PubMed: 10715321] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH EMB30/GNOM.
[7]	"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.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020433 Genomic DNA. Translation: AAB71401.1. AC004680 Genomic DNA. Translation: AAC31856.1. CP002685 Genomic DNA. Translation: AEC08327.1. AY054593 mRNA. Translation: AAK96784.1. BT000068 mRNA. Translation: AAN15387.1. AY085875 mRNA. Translation: AAM63088.1.
IPI	IPI00544481.
PIR	T02489. T50837.
RefSeq	NP_180557.1. NM_128550.3.
UniGene	At.26460.
3D structure databases
ProteinModelPortal	Q8LDP4.
SMR	Q8LDP4. Positions 33-199.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8LDP4.
Proteomic databases
PRIDE	Q8LDP4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G29960.1; AT2G29960.1; AT2G29960.
GeneID	817546.
GenomeReviews	Gene locus AT2G29960 in contig CT485783_GR.
KEGG	ath:AT2G29960.
NMPDR	fig|3702.1.peg.10048.
Organism-specific databases
TAIR	At2g29960.
Phylogenomic databases
GeneTree	EPGT00070000028652.
HOGENOM	HBG610621.
InParanoid	Q8LDP4.
OMA	SMANSGE.
PhylomeDB	Q8LDP4.
ProtClustDB	CLSN2683841.
Gene expression databases
Genevestigator	Q8LDP4.
GermOnline	AT2G29960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP19D_ARATH

Accession

Primary (citable) accession number: Q8LDP4
Secondary accession number(s): O22515, O80876

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program