Q2UGK2 (PPIB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Rotamase B

Gene names

Name:	cpr2
ORF Names:	AO090023000811

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus oryzae

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by cyclosporin A (CsA) By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – ?		Potential
	Chain	? – 192		Peptidyl-prolyl cis-trans isomerase B		PRO_0000233045
Regions
	Domain	23 – 180	158	PPIase cyclophilin-type
	Motif	189 – 192	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	124	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2UGK2 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 2D8B5BD7770C20FA	FASTA	192	21,081
	10 20 30 40 50 60 MTDLRSAEEI TSQQYSSGLA TVYFDIEHGN KPLGRVVLGL YGKTVPKTAE NFRALATGEK 70 80 90 100 110 120 GFGYEGSTFH RVIKEFMIQG GDFTRGDGTG GKSIYGEKFK DENFKIRHTK KGLLSMANAG 130 140 150 160 170 180 KDTNGSQFFI TTVATPWLDG RHVVFGEVLE GYEVVEAIEN VPKVPGDKPQ QVVKIVKSGE 190 LESEDKGSHE EL

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007157 Genomic DNA. Translation: BAE59313.1.
3D structure databases
ProteinModelPortal	Q2UGK2.
SMR	Q2UGK2. Positions 22-181.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00007900; CADAORAP00007739; CADAORAG00007900.
Phylogenomic databases
eggNOG	COG0652.
HOGENOM	HOG000065981.
OrthoDB	EOG4DZ54P.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
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. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPIB_ASPOR

Accession

Primary (citable) accession number: Q2UGK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program