FKBP7_MOUSE
ID FKBP7_MOUSE Reviewed; 218 AA.
AC O54998;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP7;
DE Short=PPIase FKBP7;
DE EC=5.2.1.8;
DE AltName: Full=23 kDa FK506-binding protein;
DE Short=23 kDa FKBP;
DE Short=FKBP-23;
DE AltName: Full=FK506-binding protein 7;
DE Short=FKBP-7;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp7; Synonyms=Fkbp23;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, GLYCOSYLATION, AND CALCIUM-BINDING.
RC STRAIN=NIH Swiss; TISSUE=Embryonic heart;
RX PubMed=9806833; DOI=10.1006/geno.1998.5571;
RA Nakamura T., Yabe D., Kanazawa N., Tashiro K., Sasayama S., Honjo T.;
RT "Molecular cloning, characterization, and chromosomal localization of
RT FKBP23, a novel FK506-binding protein with Ca2+-binding ability.";
RL Genomics 54:89-98(1998).
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).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:9806833}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in heart, lung and
CC testis. Weakly expressed in kidney and lymph node. Little or no
CC expression detected in brain, thymus, spleen and liver.
CC {ECO:0000269|PubMed:9806833}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 8.5.
CC {ECO:0000269|PubMed:9806833}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9806833}.
CC -!- MISCELLANEOUS: Binds calcium.
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DR EMBL; AF040252; AAC79959.1; -; mRNA.
DR EMBL; BC032961; AAH32961.1; -; mRNA.
DR CCDS; CCDS16161.1; -.
DR RefSeq; NP_034352.1; NM_010222.2.
DR AlphaFoldDB; O54998; -.
DR SMR; O54998; -.
DR BioGRID; 199688; 6.
DR STRING; 10090.ENSMUSP00000002809; -.
DR GlyGen; O54998; 2 sites.
DR PhosphoSitePlus; O54998; -.
DR PaxDb; O54998; -.
DR PeptideAtlas; O54998; -.
DR PRIDE; O54998; -.
DR ProteomicsDB; 271700; -.
DR Antibodypedia; 2249; 172 antibodies from 24 providers.
DR DNASU; 14231; -.
DR Ensembl; ENSMUST00000002809; ENSMUSP00000002809; ENSMUSG00000002732.
DR GeneID; 14231; -.
DR KEGG; mmu:14231; -.
DR UCSC; uc008kfh.2; mouse.
DR CTD; 51661; -.
DR MGI; MGI:1336879; Fkbp7.
DR VEuPathDB; HostDB:ENSMUSG00000002732; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000159964; -.
DR HOGENOM; CLU_013615_5_0_1; -.
DR InParanoid; O54998; -.
DR OMA; FFYVWGI; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; O54998; -.
DR TreeFam; TF105296; -.
DR BioGRID-ORCS; 14231; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Fkbp7; mouse.
DR PRO; PR:O54998; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O54998; protein.
DR Bgee; ENSMUSG00000002732; Expressed in vault of skull and 254 other tissues.
DR ExpressionAtlas; O54998; baseline and differential.
DR Genevisible; O54998; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
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; 2.
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; Endoplasmic reticulum; Glycoprotein; Isomerase; Metal-binding;
KW Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..218
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP7"
FT /id="PRO_0000025514"
FT DOMAIN 49..141
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 141..176
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 185..218
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 197..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..218
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 218 AA; 24913 MW; DB0AE509E60EEEBA CRC64;
MNLLFRLAVF LSLWCCSDAQ GQTKEESTEE VKIEVLHRPE NCSKTSRKGD LLNAHYDGYL
AKDGSKFYCS RTQDEGHPKW FVLGVGHVIK GLDIAMMDMC PGEKRKVIIP PSFAYGKEGY
AEGKIPPNAT LMFEIELYAV TKGPRSIETF KQIDTDNDRQ LSKAEIELYL QKDFEKDANP
RDKSYQKAVL EDIFKKNDHN GDGFISPKEY NVHQHDEL
