ID   FKB11_BOVIN             Reviewed;         203 AA.
AC   Q2YDL5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP11;
DE            Short=PPIase FKBP11;
DE            EC=5.2.1.8;
DE   AltName: Full=FK506-binding protein 11;
DE            Short=FKBP-11;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=FKBP11;
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 (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC       synthesis. {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   -!- SUBUNIT: Interacts with IFITM5. {ECO:0000250|UniProtKB:Q9D1M7}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {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; BC110165; AAI10166.1; -; mRNA.
DR   RefSeq; NP_001039397.1; NM_001045932.1.
DR   AlphaFoldDB; Q2YDL5; -.
DR   SMR; Q2YDL5; -.
DR   STRING; 9913.ENSBTAP00000021025; -.
DR   PaxDb; Q2YDL5; -.
DR   PeptideAtlas; Q2YDL5; -.
DR   PRIDE; Q2YDL5; -.
DR   GeneID; 506043; -.
DR   KEGG; bta:506043; -.
DR   CTD; 51303; -.
DR   eggNOG; KOG0549; Eukaryota.
DR   InParanoid; Q2YDL5; -.
DR   OrthoDB; 1507309at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Isomerase; Membrane; Reference proteome; Rotamase; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..203
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP11"
FT                   /id="PRO_0000285595"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          59..146
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   203 AA;  22475 MW;  62345FFA86344A45 CRC64;
     MTLRPSLLPL RLLLLLLLLL RGAVCQAEAG SETESPVRTL QVETLVEPPE PCAEPATFGD
     TLHIHYSGSL VDGRIFDTSL TRDPLVIELG QKQVIPGLEQ SLLDMCVGEK RRVIIPSHLA
     YGKRGFPPSI PADAELHFDV ELIALIRANY WQKLVKGILP LVGMAMVPAL LGLIGYHLYR
     KASSPKISKN KLKEEKRNKS KKK