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 16-JUN-2009, entry version 32. DE RecName: Full=FK506-binding protein 10; DE EC=5.2.1.8; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE Short=Rotamase; DE Flags: Precursor; GN Name=FKBP10; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; 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 CC protein synthesis. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin, but not CC by cyclosporin A (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- PTM: Glycosylated and phosphorylated (By similarity). CC -!- SIMILARITY: Contains 2 EF-hand domains. CC -!- SIMILARITY: Contains 4 PPIase FKBP-type domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC113250; AAI13251.1; -; mRNA. DR IPI; IPI00697856; -. DR RefSeq; NP_001039868.1; -. DR UniGene; Bt.2698; -. DR Ensembl; ENSBTAG00000011454; Bos taurus. DR GeneID; 535310; -. DR KEGG; bta:535310; -. DR HOVERGEN; Q2HJ89; -. DR OMA; Q2HJ89; DRGLMGM. DR BRENDA; 5.2.1.8; 251. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR018247; EF_HAND_1. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR InterPro; IPR000886; ER_targeting_sequence. DR InterPro; IPR001179; PPIase_FKBP. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR PANTHER; PTHR10516; PPIase_FKBP; 1. DR Pfam; PF00254; FKBP_C; 4. DR SMART; SM00054; EFh; 2. 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; KW Phosphoprotein; Repeat; Rotamase; Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 583 FK506-binding protein 10. FT /FTId=PRO_0000285594. FT DOMAIN 63 151 PPIase FKBP-type 1. FT DOMAIN 175 263 PPIase FKBP-type 2. FT DOMAIN 287 375 PPIase FKBP-type 3. FT DOMAIN 400 487 PPIase FKBP-type 4. FT DOMAIN 498 533 EF-hand 1. FT DOMAIN 543 578 EF-hand 2. FT CA_BIND 511 522 1 (Potential). FT CA_BIND 556 567 2 (Potential). FT MOTIF 580 583 Prevents secretion from ER (Potential). FT CARBOHYD 71 71 N-linked (GlcNAc...) (Potential). FT CARBOHYD 183 183 N-linked (GlcNAc...) (Potential). FT CARBOHYD 295 295 N-linked (GlcNAc...) (Potential). 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 //