ID   FKBP2_BOVIN             Reviewed;         140 AA.
AC   Q32PA9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
DE            Short=PPIase FKBP2;
DE            EC=5.2.1.8;
DE   AltName: Full=FK506-binding protein 2;
DE            Short=FKBP-2;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=FKBP2;
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 [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of EPB41L2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC108190; AAI08191.1; -; mRNA.
DR   RefSeq; NP_001032558.1; NM_001037481.1.
DR   RefSeq; XP_005227204.1; XM_005227147.3.
DR   RefSeq; XP_005227205.1; XM_005227148.3.
DR   AlphaFoldDB; Q32PA9; -.
DR   SMR; Q32PA9; -.
DR   STRING; 9913.ENSBTAP00000018091; -.
DR   PaxDb; Q32PA9; -.
DR   PeptideAtlas; Q32PA9; -.
DR   PRIDE; Q32PA9; -.
DR   GeneID; 538998; -.
DR   KEGG; bta:538998; -.
DR   CTD; 2286; -.
DR   eggNOG; KOG0549; Eukaryota.
DR   HOGENOM; CLU_013615_8_2_1; -.
DR   InParanoid; Q32PA9; -.
DR   Proteomes; UP000009136; Unplaced.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Isomerase; Membrane; Reference proteome; Rotamase;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..140
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP2"
FT                   /id="PRO_0000285596"
FT   DOMAIN          47..135
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   140 AA;  15404 MW;  F34527DD4AD43480 CRC64;
     MRLSWVLTVL SICLSALVTA TGTEGKRKLQ IGVKKRVDHC PIKSRKGDVL HMHYTGKLED
     GTEFDSSLPQ NQPFVFSLGT GQVIKGWDQG LLGMCEGEKR KLVIPSELGY GERGAPPKIP
     GGATLVFEVE LLKIERRSEL