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Q9D1M7 (FKB11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP11
Short name=PPIase FKBP11
EC=5.2.1.8
Alternative name(s):
19 kDa FK506-binding protein
Short name=19 kDa FKBP
Short name=FKBP-19
FK506-binding protein 11
Short name=FKBP-11
Rotamase
Gene names
Name:Fkbp11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins during protein synthesis.

Catalytic activity

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

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionFK506 binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidyl-prolyl cis-trans isomerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 201174Peptidyl-prolyl cis-trans isomerase FKBP11
PRO_0000025520

Regions

Transmembrane156 – 17621Helical; Potential
Domain57 – 14488PPIase FKBP-type

Experimental info

Sequence conflict531S → F in BAB31559. Ref.1
Sequence conflict1981S → R in BAB31559. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D1M7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 94D955C57264BD82

FASTA20122,137
        10         20         30         40         50         60 
MTLSPLLLPL QLLLLLLFSG AVCRAEAGPE TESPVRTLQV ETLVQPPESC TESAAIGDTL 

        70         80         90        100        110        120 
HIHYTGSLVD GRIIDTSLTR DPLVIELGQK QVIPGLEQSL LDMCVGEKRR AVIPSHLAYG 

       130        140        150        160        170        180 
KRGYPPSIPA DAVVQYDVEL IALIRANYWQ KLLKSILPLV GIAMVPALLG LIGYHLYRKA 

       190        200 
SRPKVSKKKL KEEKRNKSKK K

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK003331 mRNA. Translation: BAB22719.1.
AK019132 mRNA. Translation: BAB31559.1.
BC037596 mRNA. Translation: AAH37596.1.
IPIIPI00133931.
RefSeqNP_077131.2. NM_024169.3.
UniGeneMm.30729.

3D structure databases

ProteinModelPortalQ9D1M7.
SMRQ9D1M7. Positions 57-145.
ModBaseSearch...

PTM databases

PhosphoSiteQ9D1M7.

Proteomic databases

PaxDbQ9D1M7.
PRIDEQ9D1M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003445; ENSMUSP00000003445; ENSMUSG00000003355.
GeneID66120.
KEGGmmu:66120.
UCSCuc007xnm.1. mouse.

Organism-specific databases

CTD51303.
MGIMGI:1913370. Fkbp11.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00530000062784.
HOGENOMHOG000154887.
HOVERGENHBG051623.
InParanoidQ9D1M7.
KOK09576.
OMASRPKVSK.
OrthoDBEOG4T784J.

Gene expression databases

BgeeQ9D1M7.
CleanExMM_FKBP11.
GenevestigatorQ9D1M7.
GermOnlineENSMUSG00000003355. Mus musculus.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320690.
SOURCESearch...

Entry information

Entry nameFKB11_MOUSE
AccessionPrimary (citable) accession number: Q9D1M7
Secondary accession number(s): Q9CRE4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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