FKB10_MOUSE
ID FKB10_MOUSE Reviewed; 581 AA.
AC Q61576; A2A4I0; Q8VHI1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP10;
DE Short=PPIase FKBP10;
DE EC=5.2.1.8 {ECO:0000269|PubMed:7493967};
DE AltName: Full=65 kDa FK506-binding protein;
DE Short=65 kDa FKBP;
DE Short=FKBP-65 {ECO:0000303|PubMed:7493967};
DE AltName: Full=FK506-binding protein 10;
DE Short=FKBP-10;
DE AltName: Full=Immunophilin FKBP65;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp10; Synonyms=Fkbp-rs, Fkbp1-rs, Fkbp6, Fkbp65, Fkbprp;
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.
RC STRAIN=JB6; TISSUE=Epidermis;
RX PubMed=7507077; DOI=10.1006/geno.1993.1485;
RA Simek S.L., Kozak C.A., Winterstein D., Hegamyer G., Colburn N.H.;
RT "Sequence and localization of a novel FK506-binding protein to mouse
RT chromosome 11.";
RL Genomics 18:407-409(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=7493967; DOI=10.1074/jbc.270.49.29336;
RA Coss M.C., Winterstein D., Sowder R.C. II, Simek S.L.;
RT "Molecular cloning, DNA sequence analysis, and biochemical characterization
RT of a novel 65-kDa FK506-binding protein (FKBP65).";
RL J. Biol. Chem. 270:29336-29341(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12036304; DOI=10.1006/geno.2002.6777;
RA Patterson C.E., Gao J., Rooney A.P., Davis E.C.;
RT "Genomic organization of mouse and human 65 kDa FK506-binding protein genes
RT and evolution of the FKBP multigene family.";
RL Genomics 79:881-889(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 [7]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=11071917; DOI=10.1091/mbc.11.11.3925;
RA Patterson C.E., Schaub T., Coleman E.J., Davis E.C.;
RT "Developmental regulation of FKBP65: an ER localized extracellular matrix-
RT binding protein.";
RL Mol. Biol. Cell 11:3925-3935(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, 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 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; Evidence={ECO:0000269|PubMed:7493967};
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin, but not by
CC cyclosporin A.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:11071917}.
CC -!- TISSUE SPECIFICITY: Expressed in aorta, brain, heart, kidney, lung,
CC spleen and testis (PubMed:7493967, PubMed:11071917). Not detected in
CC liver (PubMed:7493967). {ECO:0000269|PubMed:11071917,
CC ECO:0000269|PubMed:7493967}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 12-day-old mouse; no or barely
CC detectable expression is found in adult tissues.
CC {ECO:0000269|PubMed:11071917}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7493967}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:7493967}.
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DR EMBL; L07063; AAC37678.1; -; mRNA.
DR EMBL; AF456413; AAL57621.1; -; Genomic_DNA.
DR EMBL; AF456412; AAL57621.1; JOINED; Genomic_DNA.
DR EMBL; AL590968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466662; EDL02562.1; -; Genomic_DNA.
DR EMBL; BC029546; AAH29546.1; -; mRNA.
DR CCDS; CCDS25422.1; -.
DR PIR; I49669; I49669.
DR RefSeq; NP_034351.2; NM_010221.2.
DR AlphaFoldDB; Q61576; -.
DR SMR; Q61576; -.
DR BioGRID; 199687; 10.
DR DIP; DIP-448N; -.
DR STRING; 10090.ENSMUSP00000001595; -.
DR GlyConnect; 2577; 3 N-Linked glycans (1 site).
DR GlyGen; Q61576; 7 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q61576; -.
DR MaxQB; Q61576; -.
DR PaxDb; Q61576; -.
DR PeptideAtlas; Q61576; -.
DR PRIDE; Q61576; -.
DR ProteomicsDB; 271769; -.
DR Antibodypedia; 28953; 279 antibodies from 30 providers.
DR DNASU; 14230; -.
DR Ensembl; ENSMUST00000001595; ENSMUSP00000001595; ENSMUSG00000001555.
DR GeneID; 14230; -.
DR KEGG; mmu:14230; -.
DR UCSC; uc007llb.2; mouse.
DR CTD; 60681; -.
DR MGI; MGI:104769; Fkbp10.
DR VEuPathDB; HostDB:ENSMUSG00000001555; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000156331; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; Q61576; -.
DR OMA; SYNRKQT; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q61576; -.
DR TreeFam; TF105296; -.
DR BRENDA; 5.2.1.8; 3474.
DR BioGRID-ORCS; 14230; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Fkbp10; mouse.
DR PRO; PR:Q61576; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61576; protein.
DR Bgee; ENSMUSG00000001555; Expressed in vault of skull and 199 other tissues.
DR ExpressionAtlas; Q61576; baseline and differential.
DR Genevisible; Q61576; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005528; F:FK506 binding; IDA:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:MGI.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0085029; P:extracellular matrix assembly; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IMP:MGI.
DR GO; GO:0018208; P:peptidyl-proline modification; IDA:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.10.50.40; -; 4.
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; PF13202; EF-hand_5; 2.
DR Pfam; PF00254; FKBP_C; 4.
DR SMART; SM00054; EFh; 2.
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; 4.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..581
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP10"
FT /id="PRO_0000025518"
FT DOMAIN 61..149
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 173..261
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 285..373
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 398..485
FT /note="PPIase FKBP-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 496..531
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 541..576
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 533..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 578..581
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 558..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 554
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="L -> V (in Ref. 2; AAC37678)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> G (in Ref. 2; AAC37678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 64697 MW; FD6F777940AD91E9 CRC64;
MFLVGSSSHT LHRLRILPLL LLLQTLERGL GRASPAGAPL EDVVIERYHI PRACPREVQM
GDFVRYHYNG TFEDGKKFDS SYDRSTLVAI VVGVGRLITG MDRGLMGMCV NERRRLIVPP
HLGYGSIGVA GLIPPDATLY FDVVLLDVWN KADTVQSTIL LRPPYCPRMV QNSDFVRYHY
NGTLLDGTAF DNSYSRGGTY DTYIGSGWLI KGMDQGLLGM CPGEKRKIII PPFLAYGEKG
YGTVIPPQAS LVFYVLLLDV HNPKDTVQLE TLELPQGCVR RAVAGDFMRY HYNGSLMDGT
LFDSSYSRNH TYNTYVGQGY IIPGMDQGLQ GACIGERRRI TVPPHLAYGE NGTGDKIPGS
AVLIFDVHVI DFHNPSDPVE IKTLSRPPEN CNETSKIGDF IRYHYNCSLL DGTRLFSSHD
YEAPQEITLG ANKVIEGLDR GLQGMCVGER RQLIVPPHLA HGENGARGVP GSAVLLFEVE
LVSREDGLPT GYLFVWYQDP STSLFEDMDL NKDGEVPPEE FSSFIKAQVN EGKGRLMPGQ
DPDKTISDMF QNQDRNQDGK ITAEELKLKS DEDQERVHEE L
