{"metadata":{"accession":"T1KWK4","id":"T1KWK4_TETUR","source_organism":{"taxId":"32264","scientificName":"Tetranychus urticae","fullName":"Tetranychus urticae (Two-spotted spider mite)"},"name":"DnaJ homolog subfamily B member 9","description":["Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production"],"length":120,"sequence":"MSKDCYKILGISEDASVGEIKKAYRELALKYHPDKNQDANAKVKFQQVSYAYKTLMDEKSRDMPQAMQTDCDLDSDIKDFLILAGITLAGVSALYCVLQGQSGGYEDETEKDKEHQSGKE","proteome":"UP000015104","gene":"107367893","go_terms":null,"protein_evidence":4,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"500088c3adc88e8af670fe08554083396acf46f3","counters":{"domain_architectures":98256,"entries":11,"isoforms":0,"proteomes":1,"sets":2,"structures":0,"taxa":1,"dbEntries":{"cathgene3d":1,"smart":1,"ssf":1,"cdd":1,"pfam":1,"profile":1,"panther":1,"prints":1,"interpro":3},"proteome":1,"taxonomy":1,"similar_proteins":98256}}}