FKBP5_PONAB
ID FKBP5_PONAB Reviewed; 457 AA.
AC Q5RF88;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP5;
DE Short=PPIase FKBP5;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 5;
DE Short=FKBP-5;
DE AltName: Full=Rotamase;
GN Name=FKBP5;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Immunophilin protein with PPIase and co-chaperone activities.
CC Component of unligated steroid receptors heterocomplexes through
CC interaction with heat-shock protein 90 (HSP90). Plays a role in the
CC intracellular trafficking of heterooligomeric forms of steroid hormone
CC receptors maintaining the complex into the cytoplasm when unliganded.
CC Acts as a regulator of Akt/AKT1 activity by promoting the interaction
CC between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and
CC subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which
CC facilitates IKK complex assembly leading to increased IKBKE and IKBKB
CC kinase activity, NF-kappaB activation, and IFN production.
CC {ECO:0000250|UniProtKB:Q13451}.
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 by FK506 but not cyclosporin.
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of a heteromultimeric cytoplasmic complex with HSP90AA1,
CC HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates
CC from the complex and FKBP4 takes its place. Interacts with functionally
CC mature heterooligomeric progesterone receptor complexes along with
CC HSP90 and TEBP (By similarity). Interacts with IFI44L; this interaction
CC modulates the kinase activity of IKBKB AND IKBKE (By similarity).
CC Interacts with IKBKB and IKBKE (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; CR857273; CAH89569.1; -; mRNA.
DR RefSeq; NP_001124689.1; NM_001131217.1.
DR AlphaFoldDB; Q5RF88; -.
DR SMR; Q5RF88; -.
DR STRING; 9601.ENSPPYP00000018489; -.
DR GeneID; 100171536; -.
DR KEGG; pon:100171536; -.
DR CTD; 2289; -.
DR eggNOG; KOG0543; Eukaryota.
DR InParanoid; Q5RF88; -.
DR OrthoDB; 897391at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005528; F:FK506 binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR031210; FKBP5.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10516:SF26; PTHR10516:SF26; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..457
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP5"
FT /id="PRO_0000075326"
FT DOMAIN 50..138
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 165..251
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 268..301
FT /note="TPR 1"
FT REPEAT 317..350
FT /note="TPR 2"
FT REPEAT 351..384
FT /note="TPR 3"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13451"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13451"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13451"
SQ SEQUENCE 457 AA; 51026 MW; 673C03D3667D7AC2 CRC64;
MTTDEGAKNN GESPTATVAE QGEDITSKKD RGVLKIVKRV GNGEETPMIG DKVYVHYKGK
LSNGKKFDSS HDRNEPFVFS LGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGSAGSLP
KIPSNATLFF EIELLDFKGE DLFEDGGIIR RTKRKGEGYS NPNEGATVEI HLEGRCGGRM
FDCRDVAFTV GEGEDHVIPI GIDKALEKMQ REEQCILYLG PRYGFGEAGK PKFGIEPNAE
LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYMQAVIQ YGKIVSWLEM
EYGLSEKESK ASESFLLAAF LNLAMCYSKL REYTKAVECC DKALGLDSAN GKGLYRRGEA
QLLMNEFESA KGDFEKVLEV NPQNKAARLQ ISMCQKKAKE HNERDRRIYA NMFKKFAEQD
AKEEANKAMG KKTSEGVTNE KGTDSQAMEE EKPEGHV
