BACH1_HUMAN
ID BACH1_HUMAN Reviewed; 736 AA.
AC O14867; O43285; Q6ICU0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Transcription regulator protein BACH1 {ECO:0000305};
DE AltName: Full=BTB and CNC homolog 1 {ECO:0000303|PubMed:9544839};
DE AltName: Full=HA2303;
GN Name=BACH1 {ECO:0000303|PubMed:9544839, ECO:0000312|HGNC:HGNC:935};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9544839; DOI=10.1007/s004390050692;
RA Blouin J.-L., Duriaux Sail G., Guipponi M., Rossier C., Pappasavas M.-P.,
RA Antonarakis S.E.;
RT "Isolation of the human BACH1 transcription regulator gene, which maps to
RT chromosome 21q22.1.";
RL Hum. Genet. 102:282-288(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9479503; DOI=10.1006/geno.1997.5080;
RA Ohira M., Seki N., Nagase T., Ishikawa K., Nomura N., Ohara O.;
RT "Characterization of a human homolog (BACH1) of the mouse Bach1 gene
RT encoding a BTB-basic leucine zipper transcription factor and its mapping to
RT chromosome 21q22.1.";
RL Genomics 47:300-306(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J.,
RA Schattevoy R., Yaspo M.-L., Rosenthal A.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea {ECO:0000312|EMBL:BAG36528.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-364 AND SER-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=24035498; DOI=10.1016/j.molcel.2013.08.018;
RA Tan M.K., Lim H.J., Bennett E.J., Shi Y., Harper J.W.;
RT "Parallel SCF adaptor capture proteomics reveals a role for SCFFBXL17 in
RT NRF2 activation via BACH1 repressor turnover.";
RL Mol. Cell 52:9-24(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 7-128.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the bric-a-brac (BTB) domain of human BACH1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator that acts as repressor or
CC activator, depending on the context. Binds to NF-E2 DNA binding sites.
CC Plays important roles in coordinating transcription activation and
CC repression by MAFK (By similarity). Together with MAF, represses the
CC transcription of genes under the control of the NFE2L2 oxidative stress
CC pathway (PubMed:24035498). {ECO:0000250|UniProtKB:P97302,
CC ECO:0000269|PubMed:24035498}.
CC -!- SUBUNIT: Heterodimer of BACH1 and MAFK. {ECO:0000250|UniProtKB:P97302}.
CC -!- INTERACTION:
CC O14867; P15336: ATF2; NbExp=2; IntAct=EBI-1263541, EBI-1170906;
CC O14867; P35638: DDIT3; NbExp=2; IntAct=EBI-1263541, EBI-742651;
CC O14867; O75444: MAF; NbExp=2; IntAct=EBI-1263541, EBI-2805091;
CC O14867; Q9Y5Q3: MAFB; NbExp=3; IntAct=EBI-1263541, EBI-3649340;
CC O14867; Q9ULX9: MAFF; NbExp=4; IntAct=EBI-1263541, EBI-721128;
CC O14867; O15525: MAFG; NbExp=6; IntAct=EBI-1263541, EBI-713514;
CC O14867; O60260-5: PRKN; NbExp=3; IntAct=EBI-1263541, EBI-21251460;
CC O14867; P40337-2: VHL; NbExp=3; IntAct=EBI-1263541, EBI-12157263;
CC O14867; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-1263541, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:24035498}.
CC -!- PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its
CC degradation by the proteasome. {ECO:0000269|PubMed:24035498}.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR EMBL; AF026199; AAB84100.1; -; mRNA.
DR EMBL; AF026200; AAB84101.1; -; mRNA.
DR EMBL; AB002803; BAA24932.1; -; mRNA.
DR EMBL; AF124731; AAD14689.1; -; Genomic_DNA.
DR EMBL; AK313791; BAG36528.1; -; mRNA.
DR EMBL; CR450303; CAG29299.1; -; mRNA.
DR EMBL; AL163249; CAB90435.1; -; Genomic_DNA.
DR EMBL; AP001705; BAA95505.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09913.1; -; Genomic_DNA.
DR EMBL; BC063307; AAH63307.1; -; mRNA.
DR CCDS; CCDS13585.1; -.
DR PIR; T00023; T00023.
DR RefSeq; NP_001177.1; NM_001186.3.
DR RefSeq; NP_996749.1; NM_206866.2.
DR PDB; 2IHC; X-ray; 2.44 A; A/B/C/D=7-128.
DR PDBsum; 2IHC; -.
DR AlphaFoldDB; O14867; -.
DR SMR; O14867; -.
DR BioGRID; 107047; 87.
DR ComplexPortal; CPX-2491; bZIP transcription factor complex, BACH1-FOS.
DR ComplexPortal; CPX-2493; bZIP transcription factor complex, BACH1-MAFK.
DR ComplexPortal; CPX-2494; bZIP transcription factor complex, BACH1-CREB1.
DR ComplexPortal; CPX-2496; bZIP transcription factor complex, BACH1-DDIT3.
DR ComplexPortal; CPX-2497; bZIP transcription factor complex, BACH1-MAFB.
DR ComplexPortal; CPX-2500; bZIP transcription factor complex, BACH1-MAF.
DR ComplexPortal; CPX-2720; bZIP transcription factor complex, BACH1-BACH1.
DR ComplexPortal; CPX-2872; bZIP transcription factor complex, BACH1-MAFG.
DR ComplexPortal; CPX-6402; bZIP transcription factor complex, ATF1-BACH1.
DR ComplexPortal; CPX-6412; bZIP transcription factor complex, ATF2-BACH1.
DR ComplexPortal; CPX-6781; bZIP transcription factor complex, ATF7-BACH1.
DR ComplexPortal; CPX-7012; bZIP transcription factor complex, BACH1-BATF.
DR ComplexPortal; CPX-7165; bZIP transcription factor complex, BACH1-MAFF.
DR CORUM; O14867; -.
DR DIP; DIP-24223N; -.
DR IntAct; O14867; 49.
DR MINT; O14867; -.
DR STRING; 9606.ENSP00000382805; -.
DR ChEMBL; CHEMBL4295651; -.
DR iPTMnet; O14867; -.
DR PhosphoSitePlus; O14867; -.
DR BioMuta; BACH1; -.
DR EPD; O14867; -.
DR jPOST; O14867; -.
DR MassIVE; O14867; -.
DR PaxDb; O14867; -.
DR PeptideAtlas; O14867; -.
DR PRIDE; O14867; -.
DR ProteomicsDB; 48277; -.
DR Antibodypedia; 920; 386 antibodies from 39 providers.
DR DNASU; 571; -.
DR Ensembl; ENST00000286800.8; ENSP00000286800.3; ENSG00000156273.16.
DR Ensembl; ENST00000399921.5; ENSP00000382805.1; ENSG00000156273.16.
DR GeneID; 571; -.
DR KEGG; hsa:571; -.
DR MANE-Select; ENST00000286800.8; ENSP00000286800.3; NM_001186.4; NP_001177.1.
DR UCSC; uc002ynj.4; human.
DR CTD; 571; -.
DR DisGeNET; 571; -.
DR GeneCards; BACH1; -.
DR HGNC; HGNC:935; BACH1.
DR HPA; ENSG00000156273; Tissue enhanced (bone).
DR MIM; 602751; gene.
DR neXtProt; NX_O14867; -.
DR OpenTargets; ENSG00000156273; -.
DR PharmGKB; PA25234; -.
DR VEuPathDB; HostDB:ENSG00000156273; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00940000158923; -.
DR HOGENOM; CLU_015243_2_0_1; -.
DR InParanoid; O14867; -.
DR OMA; RKKCFPS; -.
DR OrthoDB; 521871at2759; -.
DR PhylomeDB; O14867; -.
DR TreeFam; TF326681; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; O14867; -.
DR Reactome; R-HSA-9707587; Regulation of HMOX1 expression and activity.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; O14867; -.
DR SIGNOR; O14867; -.
DR BioGRID-ORCS; 571; 15 hits in 1137 CRISPR screens.
DR ChiTaRS; BACH1; human.
DR EvolutionaryTrace; O14867; -.
DR GeneWiki; BACH1; -.
DR GenomeRNAi; 571; -.
DR Pharos; O14867; Tbio.
DR PRO; PR:O14867; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O14867; protein.
DR Bgee; ENSG00000156273; Expressed in secondary oocyte and 178 other tissues.
DR ExpressionAtlas; O14867; baseline and differential.
DR Genevisible; O14867; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; NAS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0019222; P:regulation of metabolic process; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000117; P:regulation of transcription involved in G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd14719; bZIP_BACH; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043321; bZIP_BACH.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..736
FT /note="Transcription regulator protein BACH1"
FT /id="PRO_0000076454"
FT DOMAIN 34..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 557..620
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 286..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..578
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 582..589
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 680..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VARIANT 314
FT /note="S -> P (in dbSNP:rs35474725)"
FT /id="VAR_048441"
FT CONFLICT 158
FT /note="S -> T (in Ref. 1; AAB84100)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> G (in Ref. 1; AAB84100)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:2IHC"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2IHC"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:2IHC"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:2IHC"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2IHC"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2IHC"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2IHC"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:2IHC"
SQ SEQUENCE 736 AA; 81958 MW; CAAEECC63D46571B CRC64;
MSLSENSVFA YESSVHSTNV LLSLNDQRKK DVLCDVTIFV EGQRFRAHRS VLAACSSYFH
SRIVGQADGE LNITLPEEVT VKGFEPLIQF AYTAKLILSK ENVDEVCKCV EFLSVHNIEE
SCFQFLKFKF LDSTADQQEC PRKKCFSSHC QKTDLKLSLL DQRDLETDEV EEFLENKNVQ
TPQCKLRRYQ GNAKASPPLQ DSASQTYESM CLEKDAALAL PSLCPKYRKF QKAFGTDRVR
TGESSVKDIH ASVQPNERSE NECLGGVPEC RDLQVMLKCD ESKLAMEPEE TKKDPASQCP
TEKSEVTPFP HNSSIDPHGL YSLSLLHTYD QYGDLNFAGM QNTTVLTEKP LSGTDVQEKT
FGESQDLPLK SDLGTREDSS VASSDRSSVE REVAEHLAKG FWSDICSTDT PCQMQLSPAV
AKDGSEQISQ KRSECPWLGI RISESPEPGQ RTFTTLSSVN CPFISTLSTE GCSSNLEIGN
DDYVSEPQQE PCPYACVISL GDDSETDTEG DSESCSAREQ ECEVKLPFNA QRIISLSRND
FQSLLKMHKL TPEQLDCIHD IRRRSKNRIA AQRCRKRKLD CIQNLESEIE KLQSEKESLL
KERDHILSTL GETKQNLTGL CQKVCKEAAL SQEQIQILAK YSAADCPLSF LISEKDKSTP
DGELALPSIF SLSDRPPAVL PPCARGNSEP GYARGQESQQ MSTATSEQAG PAEQCRQSGG
ISDFCQQMTD KCTTDE
