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Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

FKBP1A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by both FK506 and rapamycin.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-BTA-2173789. TGF-beta receptor signaling activates SMADs.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
Short name:
PPIase FKBP1A
Alternative name(s):
12 kDa FK506-binding protein
Short name:
12 kDa FKBP
Short name:
FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name:
FKBP-1A
Immunophilin FKBP12
Rotamase
Gene namesi
Name:FKBP1A
Synonyms:FKBP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved4 Publications
ChainiPRO_00000752882 – 108Peptidyl-prolyl cis-trans isomerase FKBP1AAdd BLAST107

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysine; alternateBy similarity1
Modified residuei53N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP18203.
PeptideAtlasiP18203.
PRIDEiP18203.

Expressioni

Gene expression databases

BgeeiENSBTAG00000008303.

Interactioni

Subunit structurei

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010928.

Chemistry databases

BindingDBiP18203.

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi22 – 31Combined sources10
Beta strandi36 – 40Combined sources5
Turni41 – 44Combined sources4
Beta strandi47 – 50Combined sources4
Beta strandi53 – 56Combined sources4
Helixi58 – 65Combined sources8
Beta strandi72 – 77Combined sources6
Helixi79 – 81Combined sources3
Turni82 – 86Combined sources5
Turni89 – 91Combined sources3
Beta strandi98 – 108Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FKKX-ray2.20A2-108[»]
1FKLX-ray1.70A2-108[»]
1TCOX-ray2.50C2-108[»]
ProteinModelPortaliP18203.
SMRiP18203.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18203.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 108PPIase FKBP-typePROSITE-ProRule annotationAdd BLAST89

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOVERGENiHBG051623.
InParanoidiP18203.
KOiK09568.
OMAiCRSTPPV.
OrthoDBiEOG091G02W1.
TreeFamiTF105291.

Family and domain databases

InterProiIPR001179. PPIase_FKBP_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18203-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFV
60 70 80 90 100
LGKQEVIRGW EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPNATLIF

DVELLKLE
Length:108
Mass (Da):11,910
Last modified:January 23, 2007 - v2
Checksum:i9CD0F1278039C5B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021075 mRNA. Translation: AAX09092.1.
PIRiA61431.
RefSeqiNP_001030533.1. NM_001035456.1.
UniGeneiBt.63982.

Genome annotation databases

EnsembliENSBTAT00000010928; ENSBTAP00000010928; ENSBTAG00000008303.
GeneIDi614795.
KEGGibta:614795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021075 mRNA. Translation: AAX09092.1.
PIRiA61431.
RefSeqiNP_001030533.1. NM_001035456.1.
UniGeneiBt.63982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FKKX-ray2.20A2-108[»]
1FKLX-ray1.70A2-108[»]
1TCOX-ray2.50C2-108[»]
ProteinModelPortaliP18203.
SMRiP18203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010928.

Chemistry databases

BindingDBiP18203.

Proteomic databases

PaxDbiP18203.
PeptideAtlasiP18203.
PRIDEiP18203.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000010928; ENSBTAP00000010928; ENSBTAG00000008303.
GeneIDi614795.
KEGGibta:614795.

Organism-specific databases

CTDi2280.

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOVERGENiHBG051623.
InParanoidiP18203.
KOiK09568.
OMAiCRSTPPV.
OrthoDBiEOG091G02W1.
TreeFamiTF105291.

Enzyme and pathway databases

ReactomeiR-BTA-2173789. TGF-beta receptor signaling activates SMADs.

Miscellaneous databases

EvolutionaryTraceiP18203.

Gene expression databases

BgeeiENSBTAG00000008303.

Family and domain databases

InterProiIPR001179. PPIase_FKBP_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFKB1A_BOVIN
AccessioniPrimary (citable) accession number: P18203
Secondary accession number(s): Q5E945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be protein kinase C inhibitor 2 (PKCI-2 or 12 kDa inhibitor of protein kinase C), but has since been experimentally shown not to inhibit protein kinase C (PubMed:1868545 and PubMed:1710782).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.