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 27-MAR-2024, entry version 120. 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}. 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; 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 GlyCosmos; Q2HJ89; 3 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000015220; -. DR Ensembl; ENSBTAT00000015220.5; ENSBTAP00000015220.5; ENSBTAG00000011454.5. 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; YDRHTLV; -. DR OrthoDB; 25281at2759; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000011454; Expressed in theca cell and 99 other cell types or 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: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 Gene3D; 1.10.238.10; EF-hand; 1. 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 PANTHER; PTHR46046:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP10; 1. DR PANTHER; PTHR46046; PEPTIDYLPROLYL ISOMERASE; 1. DR Pfam; PF13202; EF-hand_5; 2. DR Pfam; PF00254; FKBP_C; 4. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF54534; FKBP-like; 4. 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 //