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Protein

Peptidyl-prolyl cis-trans isomerase FKBP7

Gene

FKBP7

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi158 – 169121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi202 – 213122PROSITE-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 FKBP7 (EC:5.2.1.8)
Short name:
PPIase FKBP7
Alternative name(s):
FK506-binding protein 7
Short name:
FKBP-7
Rotamase
Gene namesi
Name:FKBP7
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 222199Peptidyl-prolyl cis-trans isomerase FKBP7PRO_0000025515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5RET2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 14593PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST
Domaini145 – 18036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini189 – 22234EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi219 – 2224Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG051623.
InParanoidiQ5RET2.
KOiK09573.

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.
PfamiPF13499. EF-hand_7. 1 hit.
PF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5RET2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPKTMHFLFR FIVFFYLWGL FTAQRQKKEE RTEEVKIEVL HRPENCSKTS
60 70 80 90 100
KKGDLLNAHY DGYLAKDGSK FYCSRTQNEG HPKWFVLGVG QVIKGLDIAM
110 120 130 140 150
TDMCPGEKRK VVIPPSFAYG KEGYAEGKIP PDATLIFEIE LYAVTKGPRS
160 170 180 190 200
TETFKQIDMD SDRQLSKAEI NLYLQREFEK DEKPRDKSYQ DAVLEDIFKK
210 220
NDHDGDGFIS PKEYNVYQHD EL
Length:222
Mass (Da):25,824
Last modified:December 21, 2004 - v1
Checksum:i505149CC0E68DE07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857434 mRNA. Translation: CAH89725.1.
RefSeqiNP_001124786.1. NM_001131314.1.
UniGeneiPab.12281.

Genome annotation databases

GeneIDi100171639.
KEGGipon:100171639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857434 mRNA. Translation: CAH89725.1.
RefSeqiNP_001124786.1. NM_001131314.1.
UniGeneiPab.12281.

3D structure databases

ProteinModelPortaliQ5RET2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100171639.
KEGGipon:100171639.

Organism-specific databases

CTDi51661.

Phylogenomic databases

HOVERGENiHBG051623.
InParanoidiQ5RET2.
KOiK09573.

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.
PfamiPF13499. EF-hand_7. 1 hit.
PF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiFKBP7_PONAB
AccessioniPrimary (citable) accession number: Q5RET2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 21, 2004
Last modified: January 7, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds calcium.By similarity

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.