FKBP9_BOVIN
ID FKBP9_BOVIN Reviewed; 574 AA.
AC Q2KJC8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP9;
DE Short=PPIase FKBP9;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 9;
DE Short=FKBP-9;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP9;
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=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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 -!- ACTIVITY REGULATION: Inhibited by FK506. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC105407; AAI05408.1; -; mRNA.
DR RefSeq; NP_001039837.1; NM_001046372.2.
DR AlphaFoldDB; Q2KJC8; -.
DR SMR; Q2KJC8; -.
DR STRING; 9913.ENSBTAP00000033613; -.
DR PaxDb; Q2KJC8; -.
DR PeptideAtlas; Q2KJC8; -.
DR PRIDE; Q2KJC8; -.
DR Ensembl; ENSBTAT00000033703; ENSBTAP00000033613; ENSBTAG00000016707.
DR GeneID; 534182; -.
DR KEGG; bta:534182; -.
DR CTD; 11328; -.
DR VEuPathDB; HostDB:ENSBTAG00000016707; -.
DR VGNC; VGNC:29027; FKBP9.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157125; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; Q2KJC8; -.
DR OMA; HTYDTYV; -.
DR OrthoDB; 1507309at2759; -.
DR TreeFam; TF105296; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000016707; Expressed in uterine horn and 102 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; Metal-binding;
KW Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..574
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP9"
FT /id="PRO_0000239738"
FT DOMAIN 58..146
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 170..258
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 282..369
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 393..481
FT /note="PPIase FKBP-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 492..527
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 537..572
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 571..574
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
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 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 550
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 574 AA; 63535 MW; 64F34A83AB3BB51A CRC64;
MAIRARSWRP PPPPLLLLLL WVTGQAAPVA GLGLGSDSEL QIERRFVPEE CPRTVRSGDF
VRYHYVGTFP DGQKFDSSYD RDSTFNVFVG KGQLIAGMDQ ALVGMCVNER RFVKIPPKLA
YGSDGVSGVI PPDSVLHFDV LLMDIWNSED QVQIHTYFKP PSCPRTIQVS DFVRYHYNGT
FLDGTLFDSS HNRMKTYDTY VGIGWLIPGM DKGLLGMCVG EKRIITIPPF LAYGEDGDGK
DIPGQASLVF DVALLDLHNP KDGISIENKV VPENCERRSQ SGDFLRYHYN GTLLDGTFFD
SSYSRNRTFD TYIGQGYVIP GIDEGLLGVC IGEKRRIVVP PHLGYGEEGR GNIPGSAVLV
FDIHVIDFHN PSDSISITSH YKPPDCSVLS KKGDYLKYHY NASLLDGTLL DSTWNLGKTY
NIVLGFGQVV LGMDMGLREM CVGEKRTVII PPHLGYGEAG VDGEVPGSAV LVFDIELLEL
VAGLPEGYMF VWNGEVSANL FEEIDKDGDG EVLLEEFSEY IHAQVASGKG KLAPGFDAEM
IVKNMFTNQD RNGDGKVTAE EFKLKDQETK HDEL
