ID KEAP1_HUMAN STANDARD; PRT; 624 AA. AC Q14145; Q6LEP0; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-SEP-2006, entry version 58. DE Kelch-like ECH-associated protein 1 (Cytosolic inhibitor of Nrf2) DE (Kelch-like protein 19). GN Name=KEAP1; Synonyms=KIAA0132, KLHL19; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX MEDLINE=96127530; PubMed=8590280; DOI=10.1093/dnares/2.4.167; RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. IV. RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 2:167-174(1995). RN [2] RP INTERACTION WITH NF2L2/NRF2 AND FALZ, FUNCTION, TISSUE SPECIFICITY, RP AND SUBCELLULAR LOCATION. RX PubMed=15379550; DOI=10.1021/bi0494166; RA Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., RA Bowser R., Jordan-Sciutto K.L.; RT "Fetal Alz-50 clone 1 interacts with the human orthologue of the RT Kelch-like Ech-associated protein."; RL Biochemistry 43:12113-12122(2004). CC -!- FUNCTION: Retains NFE2L2/NRF2 in the cytosol thus resulting in the CC suppression of its transcriptional activity and the repression of CC antioxidant response element-mediated detoxifying enzyme gene CC expression (By similarity). May also retain FALZ in the cytosol. CC -!- SUBUNIT: Interacts with the N-terminal regulatory domain of CC NF2L2/NRF2. Interacts with FALZ. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in CC skeletal muscle. CC -!- DOMAIN: The Kelch repeats mediate interaction with NF2L2/NRF2 and CC FALZ. CC -!- SIMILARITY: Contains 1 BTB (POZ) domain. CC -!- SIMILARITY: Contains 6 Kelch repeats. 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; D50922; BAA09481.2; ALT_INIT; mRNA. DR PDB; 1U6D; X-ray; X=321-609. DR PDB; 1ZGK; X-ray; A=321-609. DR Ensembl; ENSG00000079999; Homo sapiens. DR H-InvDB; HIX0014747; -. DR HGNC; HGNC:23177; KEAP1. DR MIM; 606016; gene. DR ArrayExpress; Q14145; -. DR RZPD-ProtExp; IOH5732; -. DR RZPD-ProtExp; M0487; -. DR RZPD-ProtExp; T2883; -. DR InterPro; IPR011705; BACK. DR InterPro; IPR000210; BTB. DR InterPro; IPR013069; BTB_POZ. DR InterPro; IPR011043; Gal_oxid_central. DR InterPro; IPR006651; Kelch. DR InterPro; IPR006652; Kelch_rep. DR Pfam; PF07707; BACK; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01344; Kelch_1; 6. DR PRINTS; PR00501; KELCHREPEAT. DR SMART; SM00225; BTB; 1. DR SMART; SM00612; Kelch; 6. DR PROSITE; PS50097; BTB; 1. KW 3D-structure; Kelch repeat; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1 624 Kelch-like ECH-associated protein 1. FT /FTId=PRO_0000119093. FT DOMAIN 77 149 BTB. FT REPEAT 327 372 Kelch 1. FT REPEAT 373 423 Kelch 2. FT REPEAT 424 470 Kelch 3. FT REPEAT 471 517 Kelch 4. FT REPEAT 518 564 Kelch 5. FT REPEAT 565 611 Kelch 6. FT STRAND 327 331 FT STRAND 334 338 FT STRAND 342 345 FT TURN 347 349 FT STRAND 352 354 FT STRAND 359 360 FT STRAND 363 364 FT STRAND 366 370 FT TURN 371 372 FT STRAND 373 377 FT STRAND 380 383 FT TURN 384 385 FT STRAND 386 389 FT STRAND 393 396 FT TURN 398 400 FT STRAND 403 405 FT STRAND 410 411 FT STRAND 414 414 FT TURN 415 415 FT STRAND 417 421 FT TURN 422 423 FT STRAND 424 428 FT STRAND 431 432 FT TURN 433 434 FT STRAND 435 436 FT STRAND 440 444 FT TURN 445 448 FT STRAND 449 452 FT STRAND 457 458 FT STRAND 461 462 FT STRAND 464 468 FT TURN 469 470 FT STRAND 471 475 FT STRAND 478 478 FT STRAND 480 481 FT STRAND 483 483 FT STRAND 487 491 FT TURN 492 495 FT STRAND 496 499 FT STRAND 504 505 FT STRAND 508 509 FT STRAND 511 515 FT TURN 516 517 FT STRAND 518 522 FT STRAND 525 525 FT STRAND 527 530 FT STRAND 534 538 FT TURN 539 542 FT STRAND 543 547 FT STRAND 551 552 FT STRAND 555 556 FT STRAND 558 562 FT TURN 563 564 FT STRAND 565 569 FT STRAND 572 572 FT STRAND 574 575 FT STRAND 577 577 FT STRAND 580 585 FT TURN 586 589 FT STRAND 590 596 FT STRAND 598 599 FT STRAND 602 603 FT STRAND 605 609 SQ SEQUENCE 624 AA; 69665 MW; 7052EF3BF43B6C90 CRC64; MQPDPRPSGA GACCRFLPLQ SQCPEGAGDA VMYASTECKA EVTPSQHGNR TFSYTLEDHT KQAFGIMNEL RLSQQLCDVT LQVKYQDAPA AQFMAHKVVL ASSSPVFKAM FTNGLREQGM EVVSIEGIHP KVMERLIEFA YTASISMGEK CVLHVMNGAV MYQIDSVVRA CSDFLVQQLD PSNAIGIANF AEQIGCVELH QRAREYIYMH FGEVAKQEEF FNLSHCQLVT LISRDDLNVR CESEVFHACI NWVKYDCEQR RFYVQALLRA VRCHSLTPNF LQMQLQKCEI LQSDSRCKDY LVKIFEELTL HKPTQVMPCR APKVGRLIYT AGGYFRQSLS YLEAYNPSNG TWLRLADLQV PRSGLAGCVV GGLLYAVGGR NNSPDGNTDS SALDCYNPMT NQWSPCAPMS VPRNRIGVGV IDGHIYAVGG SHGCIHHNSV ERYEPERDEW HLVAPMLTRR IGVGVAVLNR LLYAVGGFDG TNRLNSAECY YPERNEWRMI TAMNTIRSGA GVCVLHNCIY AAGGYDGQDQ LNSVERYDVE TETWTFVAPM KHRRSALGIT VHQGRIYVLG GYDGHTFLDS VECYDPDTDT WSEVTRMTSG RSGVGVAVTM EPCRKQIDQQ NCTC //