FKB14_MOUSE
ID FKB14_MOUSE Reviewed; 211 AA.
AC P59024;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP14;
DE Short=PPIase FKBP14;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q9NWM8};
DE AltName: Full=FK506-binding protein 14;
DE Short=FKBP-14;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp14;
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 TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: PPIase which accelerates the folding of proteins during
CC protein synthesis. Has a preference for substrates containing 4-
CC hydroxylproline modifications, including type III collagen. May also
CC target type VI and type X collagens. {ECO:0000250|UniProtKB:Q9NWM8}.
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 Evidence={ECO:0000250|UniProtKB:Q9NWM8};
CC -!- ACTIVITY REGULATION: Inhibited by tacrolimus/FK506.
CC {ECO:0000250|UniProtKB:Q9NWM8}.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with type III, type IV and type
CC X collagens. {ECO:0000250|UniProtKB:Q9NWM8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
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DR EMBL; BC029109; AAH29109.1; -; mRNA.
DR CCDS; CCDS20157.1; -.
DR RefSeq; NP_705801.1; NM_153573.1.
DR AlphaFoldDB; P59024; -.
DR SMR; P59024; -.
DR BioGRID; 231206; 1.
DR STRING; 10090.ENSMUSP00000046070; -.
DR GlyConnect; 2578; 1 N-Linked glycan (1 site).
DR GlyGen; P59024; 1 site, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; P59024; -.
DR PaxDb; P59024; -.
DR PeptideAtlas; P59024; -.
DR PRIDE; P59024; -.
DR ProteomicsDB; 271892; -.
DR Antibodypedia; 2831; 217 antibodies from 26 providers.
DR DNASU; 231997; -.
DR Ensembl; ENSMUST00000046520; ENSMUSP00000046070; ENSMUSG00000038074.
DR GeneID; 231997; -.
DR KEGG; mmu:231997; -.
DR UCSC; uc009bzy.1; mouse.
DR CTD; 55033; -.
DR MGI; MGI:2387639; Fkbp14.
DR VEuPathDB; HostDB:ENSMUSG00000038074; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157858; -.
DR HOGENOM; CLU_013615_5_0_1; -.
DR InParanoid; P59024; -.
DR OMA; VVNDSHH; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; P59024; -.
DR TreeFam; TF105296; -.
DR BioGRID-ORCS; 231997; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fkbp14; mouse.
DR PRO; PR:P59024; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P59024; protein.
DR Bgee; ENSMUSG00000038074; Expressed in humerus cartilage element and 235 other tissues.
DR ExpressionAtlas; P59024; baseline and differential.
DR Genevisible; P59024; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Metal-binding; Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..211
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP14"
FT /id="PRO_0000025522"
FT DOMAIN 45..135
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 135..170
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 179..211
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 208..211
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..96
FT /evidence="ECO:0000250|UniProtKB:Q9NWM8"
SQ SEQUENCE 211 AA; 24252 MW; AB81F686794A8CDD CRC64;
MRFFLWNAIL ALWVTVLSGA LIPEPEVKIE VLQKPFICHR KTKGGDLMLV HYEGYLEKDG
SLFHSTHKHN NGQPVWFTLG ILEVLKGWDQ GLKGMCVGEK RKLTVPPALG YGKEGKGKIP
PESTLIFNID LLEIRNGPRS HESFQEMDLN DDWRLSKHEV KVYLQKEFEK HGAVVNESHH
DALVEDIFDK EDEDKDGFIS AREFTYVHDE L
