ID   FKBP3_BOVIN             Reviewed;         224 AA.
AC   P26884; Q32KT9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE            Short=PPIase FKBP3;
DE            EC=5.2.1.8;
DE   AltName: Full=25 kDa FK506-binding protein;
DE            Short=25 kDa FKBP;
DE            Short=FKBP-25;
DE   AltName: Full=FK506-binding protein 3;
DE            Short=FKBP-3;
DE   AltName: Full=Immunophilin FKBP25;
DE   AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE   AltName: Full=Rotamase;
GN   Name=FKBP3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Lippke J.A., Hsiao K., Peattie D.A.;
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 9-224.
RC   TISSUE=Brain, Spleen, and Thymus;
RX   PubMed=1371698; DOI=10.1021/bi00123a031;
RA   Galat A., Lane W.S., Standaert R.F., Schreiber S.L.;
RT   "A rapamycin-selective 25-kDa immunophilin.";
RL   Biochemistry 31:2427-2434(1992).
CC   -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a
CC       family of receptors for the two immunosuppressants which inhibit T-cell
CC       proliferation by arresting two dinstinct cytoplasmic signal
CC       transmission pathways. PPIases accelerate the folding of proteins.
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 preferentially by rapamycin over FK506.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; M95123; AAA30348.1; -; mRNA.
DR   EMBL; BC109932; AAI09933.1; -; mRNA.
DR   PIR; A42212; A40050.
DR   RefSeq; NP_001033201.1; NM_001038112.3.
DR   AlphaFoldDB; P26884; -.
DR   BMRB; P26884; -.
DR   SMR; P26884; -.
DR   STRING; 9913.ENSBTAP00000003377; -.
DR   PaxDb; P26884; -.
DR   PRIDE; P26884; -.
DR   Ensembl; ENSBTAT00000003377; ENSBTAP00000003377; ENSBTAG00000002610.
DR   GeneID; 515069; -.
DR   KEGG; bta:515069; -.
DR   CTD; 2287; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002610; -.
DR   VGNC; VGNC:29022; FKBP3.
DR   eggNOG; KOG0544; Eukaryota.
DR   GeneTree; ENSGT00940000154514; -.
DR   HOGENOM; CLU_013615_12_2_1; -.
DR   InParanoid; P26884; -.
DR   OMA; FKGTEPV; -.
DR   OrthoDB; 1328688at2759; -.
DR   TreeFam; TF105293; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000002610; Expressed in gluteus medius and 103 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR043368; FKBP3.
DR   InterPro; IPR041200; FKBP3_BTHB.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR46493; PTHR46493; 1.
DR   Pfam; PF18410; BTHB; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Isomerase; Nucleus; Phosphoprotein;
KW   Reference proteome; Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   CHAIN           2..224
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP3"
FT                   /id="PRO_0000075306"
FT   DOMAIN          128..224
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          89..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62446"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         170
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   CONFLICT        207..209
FT                   /note="KIP -> IXQ (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   224 AA;  25191 MW;  93DA5F8FB79A01FD CRC64;
     MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ DHGSDSFLAE HKLLGNIKNV AKTANKDHLV
     TAYNHLFESK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD
     KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSSKKKKNAK PLSFKVGIGK VIRGWDEALL
     TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLIFEVEL VDID