"accession"	"counters"	"description"	"gene"	"go_terms"	"id"	"ida_accession"	"in_alphafold"	"in_bfvd"	"is_fragment"	"length"	"name"	"protein_evidence"	"proteome"	"sequence"	"source_database"	"source_organism"
"T1KWK4"	"{'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}"	"['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']"	"107367893"	""	"T1KWK4_TETUR"	"500088c3adc88e8af670fe08554083396acf46f3"	True	False	False	120	"DnaJ homolog subfamily B member 9"	4	"UP000015104"	"MSKDCYKILGISEDASVGEIKKAYRELALKYHPDKNQDANAKVKFQQVSYAYKTLMDEKSRDMPQAMQTDCDLDSDIKDFLILAGITLAGVSALYCVLQGQSGGYEDETEKDKEHQSGKE"	"unreviewed"	"{'taxId': '32264', 'scientificName': 'Tetranychus urticae', 'fullName': 'Tetranychus urticae (Two-spotted spider mite)'}"