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Q99615 Proteins with TPR Repeats
Uniprot ID: Q99615
Protein name : DnaJ homolog subfamily C member 7
Gene : DNAJC7 TPR2 TTC2
Protein Families :
Squence Length : 494
Sequence
>Q99615 495 MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
Repeat regions
REPEAT 28 61 TPR 1 REPEAT 62 95 TPR 2 REPEAT 96 129 TPR 3 REPEAT 142 175 TPR 4 REPEAT 177 209 TPR 5 REPEAT 210 243 TPR 6 REPEAT 256 289 TPR 7 REPEAT 294 327 TPR 8 REPEAT 328 361 TPR 9
Sequence region of repeats
28- 61 TFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNAS 62- 95 YYGNRAATLMMLGRFREALGDAQQSVRLDDSFVR 96- 129 GHLREGKCHLSLGNAMAACRSFQRALELDHKNAQ 142- 175 EYEKIAETDFEKRDFRKVVFCMDRALEFAPACHR 177- 209 KILKAECLAMLGRYPEAQSVASDILRMDSTNAD 210- 243 ALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEK 256- 289 AKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIK 294- 327 LYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIK 328- 361 AYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEH
Domains
DOMAIN 381 451 J
Function
"Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity)"
Mutation
101 101 R->A: Impairs interaction with HSP90AA1 and HSPA1A/B when associated with A-333 and A-409 333 333 R->A: Impairs interaction with HSP90AA1 and HSPA1A/B when associated with A-101 and A-409 409 409 H->A: Predominantly nuclear localization when associated with A-101 and A-333