FKB10_BOVIN
ID FKB10_BOVIN Reviewed; 583 AA.
AC Q2HJ89;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP10;
DE Short=PPIase FKBP10;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 10;
DE Short=FKBP-10;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP10;
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=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin, but not by
CC cyclosporin A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- PTM: Glycosylated and phosphorylated. {ECO:0000250}.
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DR EMBL; BC113250; AAI13251.1; -; mRNA.
DR RefSeq; NP_001039868.1; NM_001046403.1.
DR AlphaFoldDB; Q2HJ89; -.
DR SMR; Q2HJ89; -.
DR IntAct; Q2HJ89; 1.
DR STRING; 9913.ENSBTAP00000015220; -.
DR PaxDb; Q2HJ89; -.
DR PRIDE; Q2HJ89; -.
DR Ensembl; ENSBTAT00000015220; ENSBTAP00000015220; ENSBTAG00000011454.
DR GeneID; 535310; -.
DR KEGG; bta:535310; -.
DR CTD; 60681; -.
DR VEuPathDB; HostDB:ENSBTAG00000011454; -.
DR VGNC; VGNC:29017; FKBP10.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000156331; -.
DR InParanoid; Q2HJ89; -.
DR OMA; SYNRKQT; -.
DR OrthoDB; 1507309at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000011454; Expressed in theca cell and 99 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005528; F:FK506 binding; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IEA:Ensembl.
DR GO; GO:0018208; P:peptidyl-proline modification; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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; PF13202; EF-hand_5; 2.
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 Phosphoprotein; Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..583
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP10"
FT /id="PRO_0000285594"
FT DOMAIN 63..151
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 175..263
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 287..375
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 400..487
FT /note="PPIase FKBP-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 498..533
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 543..578
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 534..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 580..583
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 560..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
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 558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 567
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 583 AA; 64484 MW; E651201D6D74D5F6 CRC64;
MLRAGPPSHT LLRLPLLQLL LLLLVQAVGR GLGRASPAGG PLEDVVIERY HIPRVCPREV
QMGDFVRYHY NGTFEDGKKF DSSYDRHTLV AIVVGVGRLI TGMDRGLMGM CVNERRRLIV
PPHLGYGSIG VAGLIPPDAT LYFDVVLLDV WNKEDTVQVS TLLRPPHCPR MVQDSDFVRY
HYNGTLLDGT AFDTSYSKGG TYDTYVGSGW LIKGMDQGLL GMCPGERRKI VIPPFLAYGE
KGYGTVIPSQ ASLVFHVLLI DVHNPKDTVQ LETLELPPGC VRRAVAGDFM RYHYNGSLMD
GTLFDSSYSR NHTYNTYVGQ GYIIPGMDQG LQGSCMGERR RITIPPHLAY GENGTGDKIP
GSAVLIFDVH VIDFHNPADP VEIKTLSRPL ETCNETAKLG DFVHYHYNCS LLDGTRLFSS
HDYGAPQEAT LGAHKVIEGL DTGLQGMCVG ERRQLVVPPH LAHGESGARG VPGSAVLLFE
VELVSREDGL PTGYLFVWHE DPPAHLFEHM DLNKDGEVPV EEFSTFIKAQ VSEGKGRLLP
GQDPEKTIGD MFQNQDRNQD GKITAEELKL KSDEDQDRVH EEL
