Reviewed, UniProtKB/Swiss-Prot Q41649 (FKB15_VICFA)

Names and origin

Protein names

Recommended name:
    FK506-binding protein 2
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    15 kDa FKBP
    FKBP-15

Gene names

Name:

FKBP15

Organism

Vicia faba (Broad bean)

Taxonomic identifier

3906 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Vicia

Protein attributes

Sequence length	151 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by both FK506 and rapamycin.
Subcellular location	Endoplasmic reticulum lumen Potential.
Tissue specificity	Ubiquitously expressed.
Induction	By heat shock.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP2 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Isomerase Rotamase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 – 22	22	Ref.1
	Chain	23 – 151	129	FK506-binding protein 2		PRO_0000025510
Regions
	Domain	49 – 137	89	PPIase FKBP-type
	Motif	148 – 151	4	Prevents secretion from ER Potential

Sequences

	Sequence		Length	Mass (Da)
	Q41649-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0363CB99B20C5D19	FASTA	151	16,224
	10 20 30 40 50 60 MKLFSIFLIF TIFIIASALV AAKSAADVTE LQIGVKYKPA SCEVQAHKGD KVKVHYRGKL 70 80 90 100 110 120 TDGTVFDSSF ERNSPIDFEL GGGQVIKGWD QGLLGMCLGE KRKLKIPAKL GYGEQGSPPT 130 140 150 IPGGATLIFD TELVGVNDKS LSEEKSTSSE L

References

[1]	"Molecular characterization of a FKBP-type immunophilin from higher plants." Luan S., Kudla J., Gruissem W., Schreiber S.L. Proc. Natl. Acad. Sci. U.S.A. 93:6964-6969(1996) [PubMed: 8692927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U52045 mRNA. Translation: AAC49392.1.
PIR	T12090.
3D structure databases
HSSP	HSSP built from PDB template 1KT0 based on UniProtKB Q13451.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.2.1.8. 30.
Family and domain databases
InterPro	IPR001179. PPIase_FKBP. [Graphical view]
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FKB15_VICFA

Accession

Primary (citable) accession number: Q41649

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)