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Protein

Peptidyl-prolyl cis-trans isomerase FKBP10

Gene

FKBP10

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

PPIases accelerate the folding of proteins during protein synthesis.

Catalytic activityi

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

Enzyme regulationi

Inhibited by both FK506 and rapamycin, but not by cyclosporin A.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi511 – 522121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi556 – 567122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP10 (EC:5.2.1.8)
Short name:
PPIase FKBP10
Alternative name(s):
FK506-binding protein 10
Short name:
FKBP-10
Rotamase
Gene namesi
Name:FKBP10
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

  1. Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 583556Peptidyl-prolyl cis-trans isomerase FKBP10PRO_0000285594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated and phosphorylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ2HJ89.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015220.

Structurei

3D structure databases

ProteinModelPortaliQ2HJ89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 15189PPIase FKBP-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini175 – 26389PPIase FKBP-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 37589PPIase FKBP-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 48788PPIase FKBP-type 4PROSITE-ProRule annotationAdd
BLAST
Domaini498 – 53336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini543 – 57836EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi580 – 5834Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 4 PPIase FKBP-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000230960.
HOVERGENiHBG051620.
InParanoidiQ2HJ89.
KOiK09575.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF13202. EF-hand_5. 2 hits.
PF00254. FKBP_C. 4 hits.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2HJ89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRAGPPSHT LLRLPLLQLL LLLLVQAVGR GLGRASPAGG PLEDVVIERY
60 70 80 90 100
HIPRVCPREV QMGDFVRYHY NGTFEDGKKF DSSYDRHTLV AIVVGVGRLI
110 120 130 140 150
TGMDRGLMGM CVNERRRLIV PPHLGYGSIG VAGLIPPDAT LYFDVVLLDV
160 170 180 190 200
WNKEDTVQVS TLLRPPHCPR MVQDSDFVRY HYNGTLLDGT AFDTSYSKGG
210 220 230 240 250
TYDTYVGSGW LIKGMDQGLL GMCPGERRKI VIPPFLAYGE KGYGTVIPSQ
260 270 280 290 300
ASLVFHVLLI DVHNPKDTVQ LETLELPPGC VRRAVAGDFM RYHYNGSLMD
310 320 330 340 350
GTLFDSSYSR NHTYNTYVGQ GYIIPGMDQG LQGSCMGERR RITIPPHLAY
360 370 380 390 400
GENGTGDKIP GSAVLIFDVH VIDFHNPADP VEIKTLSRPL ETCNETAKLG
410 420 430 440 450
DFVHYHYNCS LLDGTRLFSS HDYGAPQEAT LGAHKVIEGL DTGLQGMCVG
460 470 480 490 500
ERRQLVVPPH LAHGESGARG VPGSAVLLFE VELVSREDGL PTGYLFVWHE
510 520 530 540 550
DPPAHLFEHM DLNKDGEVPV EEFSTFIKAQ VSEGKGRLLP GQDPEKTIGD
560 570 580
MFQNQDRNQD GKITAEELKL KSDEDQDRVH EEL
Length:583
Mass (Da):64,484
Last modified:March 21, 2006 - v1
Checksum:iE651201D6D74D5F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113250 mRNA. Translation: AAI13251.1.
RefSeqiNP_001039868.1. NM_001046403.1.
UniGeneiBt.2698.

Genome annotation databases

GeneIDi535310.
KEGGibta:535310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113250 mRNA. Translation: AAI13251.1.
RefSeqiNP_001039868.1. NM_001046403.1.
UniGeneiBt.2698.

3D structure databases

ProteinModelPortaliQ2HJ89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015220.

Proteomic databases

PRIDEiQ2HJ89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi535310.
KEGGibta:535310.

Organism-specific databases

CTDi60681.

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000230960.
HOVERGENiHBG051620.
InParanoidiQ2HJ89.
KOiK09575.

Miscellaneous databases

NextBioi20876693.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF13202. EF-hand_5. 2 hits.
PF00254. FKBP_C. 4 hits.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.

Entry informationi

Entry nameiFKB10_BOVIN
AccessioniPrimary (citable) accession number: Q2HJ89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 21, 2006
Last modified: January 7, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.