FKB11_MOUSE
ID FKB11_MOUSE Reviewed; 201 AA.
AC Q9D1M7; Q9CRE4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP11;
DE Short=PPIase FKBP11;
DE EC=5.2.1.8;
DE AltName: Full=19 kDa FK506-binding protein;
DE Short=19 kDa FKBP;
DE Short=FKBP-19;
DE AltName: Full=FK506-binding protein 11;
DE Short=FKBP-11;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH IFITM5.
RX PubMed=20838829; DOI=10.1007/s00774-010-0221-0;
RA Hanagata N., Li X., Morita H., Takemura T., Li J., Minowa T.;
RT "Characterization of the osteoblast-specific transmembrane protein IFITM5
RT and analysis of IFITM5-deficient mice.";
RL J. Bone Miner. Metab. 29:279-290(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Interacts with IFITM5. {ECO:0000269|PubMed:20838829}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AK003331; BAB22719.1; -; mRNA.
DR EMBL; AK019132; BAB31559.1; -; mRNA.
DR EMBL; BC037596; AAH37596.1; -; mRNA.
DR CCDS; CCDS27803.1; -.
DR RefSeq; NP_077131.2; NM_024169.3.
DR AlphaFoldDB; Q9D1M7; -.
DR SMR; Q9D1M7; -.
DR BioGRID; 211229; 3.
DR STRING; 10090.ENSMUSP00000003445; -.
DR PhosphoSitePlus; Q9D1M7; -.
DR EPD; Q9D1M7; -.
DR jPOST; Q9D1M7; -.
DR MaxQB; Q9D1M7; -.
DR PaxDb; Q9D1M7; -.
DR PeptideAtlas; Q9D1M7; -.
DR PRIDE; Q9D1M7; -.
DR ProteomicsDB; 267591; -.
DR Antibodypedia; 25734; 200 antibodies from 24 providers.
DR DNASU; 66120; -.
DR Ensembl; ENSMUST00000003445; ENSMUSP00000003445; ENSMUSG00000003355.
DR GeneID; 66120; -.
DR KEGG; mmu:66120; -.
DR UCSC; uc007xnm.1; mouse.
DR CTD; 51303; -.
DR MGI; MGI:1913370; Fkbp11.
DR VEuPathDB; HostDB:ENSMUSG00000003355; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000159521; -.
DR HOGENOM; CLU_013615_8_0_1; -.
DR InParanoid; Q9D1M7; -.
DR OMA; VFTCGLA; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q9D1M7; -.
DR TreeFam; TF105296; -.
DR BioGRID-ORCS; 66120; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Fkbp11; mouse.
DR PRO; PR:Q9D1M7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D1M7; protein.
DR Bgee; ENSMUSG00000003355; Expressed in parotid gland and 200 other tissues.
DR Genevisible; Q9D1M7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Membrane; Reference proteome; Rotamase; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..201
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP11"
FT /id="PRO_0000025520"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 57..144
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT CONFLICT 53
FT /note="S -> F (in Ref. 1; BAB31559)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> R (in Ref. 1; BAB31559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22137 MW; 94D955C57264BD82 CRC64;
MTLSPLLLPL QLLLLLLFSG AVCRAEAGPE TESPVRTLQV ETLVQPPESC TESAAIGDTL
HIHYTGSLVD GRIIDTSLTR DPLVIELGQK QVIPGLEQSL LDMCVGEKRR AVIPSHLAYG
KRGYPPSIPA DAVVQYDVEL IALIRANYWQ KLLKSILPLV GIAMVPALLG LIGYHLYRKA
SRPKVSKKKL KEEKRNKSKK K
