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FKB14_PONAB
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   03-AUG-2022, entry version 87.
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   GeneID; 100174527; -.
DR   KEGG; pon:100174527; -.
DR   CTD; 55033; -.
DR   eggNOG; KOG0549; Eukaryota.
DR   InParanoid; Q5R941; -.
DR   OrthoDB; 1507309at2759; -.
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   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; PF13499; EF-hand_7; 1.
DR   Pfam; PF00254; FKBP_C; 1.
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; 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
 
 
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