ID FKB14_PONAB Reviewed; 211 AA. AC Q5R941; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 90. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP14; DE Short=PPIase FKBP14; DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q9NWM8}; DE AltName: Full=FK506-binding protein 14; DE Short=FKBP-14; DE AltName: Full=Rotamase; DE Flags: Precursor; GN Name=FKBP14; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIase which accelerates the folding of proteins during CC protein synthesis. Has a preference for substrates containing 4- CC hydroxylproline modifications, including type III collagen. May also CC target type VI and type X collagens. {ECO:0000250|UniProtKB:Q9NWM8}. 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 Evidence={ECO:0000250|UniProtKB:Q9NWM8}; CC -!- ACTIVITY REGULATION: Inhibited by tacrolimus/FK506. CC {ECO:0000250|UniProtKB:Q9NWM8}. CC -!- SUBUNIT: Monomer. Homodimer. Interacts with type III, type IV and type CC X collagens. {ECO:0000250|UniProtKB:Q9NWM8}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138}. 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; CR859554; CAH91719.1; -; mRNA. DR RefSeq; NP_001127454.1; NM_001133982.1. DR AlphaFoldDB; Q5R941; -. DR SMR; Q5R941; -. DR STRING; 9601.ENSPPYP00000019820; -. DR GlyCosmos; Q5R941; 1 site, No reported glycans. DR GeneID; 100174527; -. DR KEGG; pon:100174527; -. DR CTD; 55033; -. DR eggNOG; KOG0549; Eukaryota. DR InParanoid; Q5R941; -. DR OrthoDB; 25281at2759; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.50.40; -; 1. 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; PTHR46222:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP14; 1. DR PANTHER; PTHR46222; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP7/14; 1. DR Pfam; PF00254; FKBP_C; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF54534; FKBP-like; 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; 1. PE 2: Evidence at transcript level; KW Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; KW Metal-binding; Reference proteome; Repeat; Rotamase; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000250" FT CHAIN 20..211 FT /note="Peptidyl-prolyl cis-trans isomerase FKBP14" FT /id="PRO_0000025523" FT DOMAIN 45..135 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277" FT DOMAIN 135..170 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 179..211 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOTIF 208..211 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT BINDING 148 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 150 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 152 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 154 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 159 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 192 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 194 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 196 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CARBOHYD 176 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 38..96 FT /evidence="ECO:0000250|UniProtKB:Q9NWM8" SQ SEQUENCE 211 AA; 24172 MW; 858184954FE10029 CRC64; MRLFLWNAVL TLFVTSLIGA LIPEPEVKIE VLQKPFICHR KTKGGDLMLV HYEGYLEKDG SLFHSTHKHN NGQPIWFTLG ILEALKGWDQ GLKGMCVGEK RKLIIPPALG YGKEGKGKIP PESTLIFNID LLEIRNGPRS HESFQEMDLN DDWKLSKDEV KAYLKKEFEK HGAVVNESHH DALVEDIFDK EDEDKDGFIS AREFTYKHDE L //