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}.
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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
//
