位置:首页 > 蛋白库 > FKBP3_RABIT
FKBP3_RABIT
ID   FKBP3_RABIT             Reviewed;         224 AA.
AC   O46638;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE            Short=PPIase FKBP3;
DE            EC=5.2.1.8;
DE   AltName: Full=25 kDa FK506-binding protein;
DE            Short=25 kDa FKBP;
DE            Short=FKBP-25;
DE   AltName: Full=FK506-binding protein 3;
DE            Short=FKBP-3;
DE   AltName: Full=Immunophilin FKBP25;
DE   AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE   AltName: Full=Rotamase;
GN   Name=FKBP3; Synonyms=FKBP25;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-224.
RC   TISSUE=Cornea;
RX   PubMed=8876379;
RA   Kitagawa H., Hotta Y., Fujiki K., Kanai A.;
RT   "Cloning and high expression of rabbit FKBP25 in cornea.";
RL   Jpn. J. Ophthalmol. 40:133-141(1996).
CC   -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a
CC       family of receptors for the two immunosuppressants which inhibit T-cell
CC       proliferation by arresting two distinct cytoplasmic signal transmission
CC       pathways. PPIases accelerate the folding of proteins (By similarity).
CC       {ECO:0000250}.
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 preferentially by rapamycin over FK506.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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; D82876; BAA24412.1; -; mRNA.
DR   RefSeq; XP_002718212.1; XM_002718166.3.
DR   AlphaFoldDB; O46638; -.
DR   BMRB; O46638; -.
DR   SMR; O46638; -.
DR   STRING; 9986.ENSOCUP00000006516; -.
DR   GeneID; 100009004; -.
DR   KEGG; ocu:100009004; -.
DR   CTD; 2287; -.
DR   eggNOG; KOG0544; Eukaryota.
DR   HOGENOM; CLU_013615_12_2_1; -.
DR   InParanoid; O46638; -.
DR   OMA; FKGTEPV; -.
DR   OrthoDB; 1328688at2759; -.
DR   TreeFam; TF105293; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR043368; FKBP3.
DR   InterPro; IPR041200; FKBP3_BTHB.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR46493; PTHR46493; 1.
DR   Pfam; PF18410; BTHB; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isomerase; Nucleus; Phosphoprotein; Reference proteome;
KW   Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   CHAIN           2..224
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP3"
FT                   /id="PRO_0000075309"
FT   DOMAIN          128..224
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          87..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62446"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
FT   MOD_RES         170
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00688"
SQ   SEQUENCE   224 AA;  25188 MW;  9E6E54AACB0E079D CRC64;
     MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ DHGSDSFLAE HKLLGNIKNV AKTANKDHLV
     TAYNHLFETK RFKGSENVTK VSEQVKNVKL NEDKPKETKS EETPDEGPPK YTKSVLKKGD
     KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSSKKKKNAK PLSFKVGVGK VIRGWDEALL
     TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLIFEVEL VDID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024