FKBP2_MOUSE
ID FKBP2_MOUSE Reviewed; 140 AA.
AC P45878;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
DE Short=PPIase FKBP2;
DE EC=5.2.1.8;
DE AltName: Full=13 kDa FK506-binding protein;
DE Short=13 kDa FKBP;
DE Short=FKBP-13;
DE AltName: Full=FK506-binding protein 2;
DE Short=FKBP-2;
DE AltName: Full=Immunophilin FKBP13;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp2; Synonyms=Fkbp13;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=7505249; DOI=10.1016/0378-1119(93)90106-d;
RA Hendrickson B.A., Zhang W., Craig R.J., Jin Y.J., Bierer R.E.,
RA Burakoff S.J., Dilella A.G.;
RT "Structural organization of the genes encoding human and murine FK506-
RT binding protein (FKBP) 13 and comparison to FKBP1.";
RL Gene 134:271-275(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
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 INTERACTION WITH EPB41L2.
RX PubMed=9531554; DOI=10.1083/jcb.141.1.143;
RA Walensky L.D., Gascard P., Fields M.E., Blackshaw S., Conboy J.G.,
RA Mohandas N., Snyder S.H.;
RT "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue
RT of the erythrocyte membrane cytoskeletal protein 4.1.";
RL J. Cell Biol. 141:143-153(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of EPB41L2.
CC {ECO:0000269|PubMed:9531554}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; M77831; AAA37631.1; -; Genomic_DNA.
DR EMBL; BC031824; AAH31824.1; -; mRNA.
DR EMBL; BC053692; AAH53692.1; -; mRNA.
DR CCDS; CCDS29515.1; -.
DR PIR; I49668; I49668.
DR RefSeq; NP_001159840.1; NM_001166368.1.
DR RefSeq; NP_032046.1; NM_008020.3.
DR RefSeq; XP_006526736.1; XM_006526673.1.
DR RefSeq; XP_006526737.1; XM_006526674.1.
DR RefSeq; XP_006526738.1; XM_006526675.2.
DR AlphaFoldDB; P45878; -.
DR SMR; P45878; -.
DR BioGRID; 199684; 6.
DR STRING; 10090.ENSMUSP00000066839; -.
DR iPTMnet; P45878; -.
DR PhosphoSitePlus; P45878; -.
DR EPD; P45878; -.
DR jPOST; P45878; -.
DR PaxDb; P45878; -.
DR PeptideAtlas; P45878; -.
DR PRIDE; P45878; -.
DR ProteomicsDB; 267477; -.
DR DNASU; 14227; -.
DR Ensembl; ENSMUST00000070878; ENSMUSP00000066839; ENSMUSG00000056629.
DR Ensembl; ENSMUST00000177752; ENSMUSP00000136438; ENSMUSG00000056629.
DR GeneID; 14227; -.
DR KEGG; mmu:14227; -.
DR UCSC; uc008gjt.2; mouse.
DR CTD; 2286; -.
DR MGI; MGI:95542; Fkbp2.
DR VEuPathDB; HostDB:ENSMUSG00000056629; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT01030000240160; -.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; P45878; -.
DR OMA; WAYGSRG; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; P45878; -.
DR TreeFam; TF105292; -.
DR BioGRID-ORCS; 14227; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Fkbp2; mouse.
DR PRO; PR:P45878; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P45878; protein.
DR Bgee; ENSMUSG00000056629; Expressed in seminal vesicle and 259 other tissues.
DR ExpressionAtlas; P45878; baseline and differential.
DR Genevisible; P45878; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Endoplasmic reticulum; Isomerase; Membrane; Reference proteome; Rotamase;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..140
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP2"
FT /id="PRO_0000025507"
FT DOMAIN 47..135
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT MOTIF 137..140
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
SQ SEQUENCE 140 AA; 15344 MW; F4E7FCC7766A0416 CRC64;
MRLSWILTIL SICLSALAAA TGAEGKRKLQ IGVKKRVDHC PIKSRKGDVL HMHYTGKLED
GTEFDSSLPQ NQPFVFSLGT GQVIKGWDQG LLGMCEGEKR KLVIPSELGY GERGAPPKIP
GGATLVFEVE LLKIERRSEL
