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P62943 (FKB1A_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A

Short name=PPIase FKBP1A
EC=5.2.1.8
Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase
Gene names
Name:FKBP1A
Synonyms:FKBP1, FKBP12
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP1A per skeletal muscle RYR. 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 both FK506 and rapamycin.

Subunit structure

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation By similarity. Interacts with ACVR1B and SMAD7 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmicrosome

Inferred from direct assay. Source: AgBase

terminal cisterna

Inferred from direct assay Ref.1. Source: BHF-UCL

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1A
PRO_0000075291

Regions

Domain20 – 10889PPIase FKBP-type

Amino acid modifications

Modified residue91Phosphoserine By similarity
Modified residue531N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62943 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9CC8493C802540B4

FASTA10811,951
        10         20         30         40         50         60 
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW 

        70         80         90        100 
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE 

« Hide

References

[1]"FK506 binding protein associated with the calcium release channel (ryanodine receptor)."
Jayaraman T., Brillantes A.M., Timerman A.P., Fleischer S., Erdjument-Bromage H., Tempst P., Marks A.R.
J. Biol. Chem. 267:9474-9477(1992) [PubMed: 1374404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M89928 Genomic RNA. Translation: AAA31252.1.
PIRA42657.
RefSeqNP_001164597.1. NM_001171126.1.
UniGeneOcu.7704.

3D structure databases

ProteinModelPortalP62943.
SMRP62943. Positions 2-108.
ModBaseSearch...

Protein-protein interaction databases

STRINGP62943.

Proteomic databases

PRIDEP62943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100328942.

Organism-specific databases

CTD2280.

Phylogenomic databases

eggNOGmaNOG20348.
HOVERGENHBG051623.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP62943.
DrugBankDB01093. Dimethyl sulfoxide.

Entry information

Entry nameFKB1A_RABIT
AccessionPrimary (citable) accession number: P62943
Secondary accession number(s): P20071, Q9H103, Q9H566
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: October 19, 2011
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families