AHRR_HUMAN
ID AHRR_HUMAN Reviewed; 701 AA.
AC A9YTQ3; A7MBN5; D6RAZ1; Q9HAZ3; Q9ULI6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aryl hydrocarbon receptor repressor;
DE Short=AhR repressor;
DE Short=AhRR;
DE AltName: Full=Class E basic helix-loop-helix protein 77;
DE Short=bHLHe77;
GN Name=AHRR; Synonyms=BHLHE77, KIAA1234;
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 [GENOMIC DNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP VARIANT PRO-114.
RX PubMed=11835227; DOI=10.1002/tera.1093;
RA Fujita H., Kosaki R., Yoshihashi H., Ogata T., Tomita M., Hasegawa T.,
RA Takahashi T., Matsuo N., Kosaki K.;
RT "Characterization of the aryl hydrocarbon receptor repressor gene and
RT association of its Pro185Ala polymorphism with micropenis.";
RL Teratology 65:10-18(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-189.
RA Karchner S.I., Evans B., Jenny M.J., Hahn M.E.;
RT "Identification and functional analysis of a human AHR repressor.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-189.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-189.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-189.
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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14672759; DOI=10.1016/j.lfs.2003.07.022;
RA Yamamoto J., Ihara K., Nakayama H., Hikino S., Satoh K., Kubo N., Iida T.,
RA Fujii Y., Hara T.;
RT "Characteristic expression of aryl hydrocarbon receptor repressor gene in
RT human tissues: organ-specific distribution and variable induction patterns
RT in mononuclear cells.";
RL Life Sci. 74:1039-1049(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17980155; DOI=10.1016/j.bbrc.2007.10.140;
RA Kanno Y., Miyama Y., Takane Y., Nakahama T., Inouye Y.;
RT "Identification of intracellular localization signals and of mechanisms
RT underlining the nucleocytoplasmic shuttling of human aryl hydrocarbon
RT receptor repressor.";
RL Biochem. Biophys. Res. Commun. 364:1026-1031(2007).
RN [9]
RP FUNCTION.
RX PubMed=17890447; DOI=10.1124/dmd.107.016253;
RA Haarmann-Stemmann T., Bothe H., Kohli A., Sydlik U., Abel J., Fritsche E.;
RT "Analysis of the transcriptional regulation and molecular function of the
RT aryl hydrocarbon receptor repressor in human cell lines.";
RL Drug Metab. Dispos. 35:2262-2269(2007).
RN [10]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=18172554; DOI=10.1172/jci30024;
RA Zudaire E., Cuesta N., Murty V., Woodson K., Adams L., Gonzalez N.,
RA Martinez A., Narayan G., Kirsch I., Franklin W., Hirsch F., Birrer M.,
RA Cuttitta F.;
RT "The aryl hydrocarbon receptor repressor is a putative tumor suppressor
RT gene in multiple human cancers.";
RL J. Clin. Invest. 118:640-650(2008).
RN [11]
RP POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALE INFERTILITY.
RX PubMed=15474075; DOI=10.1016/j.fertnstert.2004.06.027;
RA Watanabe M., Sueoka K., Sasagawa I., Nakabayashi A., Yoshimura Y.,
RA Ogata T.;
RT "Association of male infertility with Pro185Ala polymorphism in the aryl
RT hydrocarbon receptor repressor gene: implication for the susceptibility to
RT dioxins.";
RL Fertil. Steril. 82:1067-1071(2004).
RN [12]
RP POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO ENDOMETRIOSIS.
RX PubMed=16084889; DOI=10.1016/j.fertnstert.2005.01.130;
RA Tsuchiya M., Katoh T., Motoyama H., Sasaki H., Tsugane S., Ikenoue T.;
RT "Analysis of the AhR, ARNT, and AhRR gene polymorphisms: genetic
RT contribution to endometriosis susceptibility and severity.";
RL Fertil. Steril. 84:454-458(2005).
RN [13]
RP POLYMORPHISM, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALE INFERTILITY.
RX PubMed=17559847; DOI=10.1016/j.fertnstert.2006.12.041;
RA Merisalu A., Punab M., Altmaee S., Haller K., Tiido T., Peters M.,
RA Salumets A.;
RT "The contribution of genetic variations of aryl hydrocarbon receptor
RT pathway genes to male factor infertility.";
RL Fertil. Steril. 88:854-859(2007).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-577 AND LYS-660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-577 AND LYS-660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16] {ECO:0007744|PDB:5Y7Y}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 27-280 IN COMPLEX WITH ARNT, AND
RP INTERACTION WITH ARNT.
RX PubMed=28904176; DOI=10.1074/jbc.m117.812974;
RA Sakurai S., Shimizu T., Ohto U.;
RT "The crystal structure of the AhRR-ARNT heterodimer reveals the structural
RT basis of the repression of AhR-mediated transcription.";
RL J. Biol. Chem. 292:17609-17616(2017).
CC -!- FUNCTION: Mediates dioxin toxicity and is involved in regulation of
CC cell growth and differentiation. Represses the transcription activity
CC of AHR by competing with this transcription factor for heterodimer
CC formation with the ARNT and subsequently binding to the xenobiotic
CC response element (XRE) sequence present in the promoter regulatory
CC region of variety of genes. Represses CYP1A1 by binding the XRE
CC sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its
CC expression by associating with its own XRE site.
CC {ECO:0000269|PubMed:17890447, ECO:0000269|PubMed:18172554}.
CC -!- SUBUNIT: Interacts with ANKRA2, HDAC4 and HDAC5. Interacts with ARNT;
CC forms a heterodimer with ARNT (PubMed:28904176). {ECO:0000250,
CC ECO:0000269|PubMed:28904176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}.
CC Note=Predominantly in the nuclear compartment. First cytoplasmic,
CC translocates into the nuclear compartment upon interaction with ARNT in
CC the cytoplasmic compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A9YTQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A9YTQ3-2; Sequence=VSP_033564;
CC Name=3;
CC IsoId=A9YTQ3-3; Sequence=VSP_033563, VSP_033564;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, lung, ovary, spleen and
CC pancreas. Highly expressed in mononuclear cells (MNCs) from umbilical
CC cord blood. Isoform 3 is highly expressed in lung, kidney, spleen and
CC thymus. Down-regulated malignant tissue from different anatomical
CC origins, including colon, breast, lung, stomach, cervix, and ovary.
CC {ECO:0000269|PubMed:11835227, ECO:0000269|PubMed:14672759,
CC ECO:0000269|PubMed:18172554}.
CC -!- INDUCTION: By 3-methylcholanthrene (3-MC) in MNCs from adults. By the
CC heterodimer AHR/ARNT. {ECO:0000269|PubMed:14672759}.
CC -!- POLYMORPHISM: The Ala-189 allele may be a susceptibility factor for
CC dioxin-related male infertility. Homozygosity for Ala-189 is observed
CC in azoospermic individuals at higher frequency than in normozoospermic
CC individuals (PubMed:15474075, PubMed:17559847). Might also be
CC associated with susceptibility to and severity of endometriosis.
CC {ECO:0000269|PubMed:15474075, ECO:0000269|PubMed:17559847}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABX89616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA86548.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF293639; AAG33381.1; -; Genomic_DNA.
DR EMBL; AF293629; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293630; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293631; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293632; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293633; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293634; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293635; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293636; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293637; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; AF293638; AAG33381.1; JOINED; Genomic_DNA.
DR EMBL; EU293605; ABX89616.1; ALT_INIT; mRNA.
DR EMBL; AB033060; BAA86548.1; ALT_INIT; mRNA.
DR EMBL; AC010442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471235; EAW50992.1; -; Genomic_DNA.
DR EMBL; BC151852; AAI51853.1; -; mRNA.
DR EMBL; BC152406; AAI52407.1; -; mRNA.
DR RefSeq; NP_001229341.1; NM_001242412.1.
DR RefSeq; NP_065782.2; NM_020731.4.
DR PDB; 5Y7Y; X-ray; 2.40 A; A=27-280.
DR PDBsum; 5Y7Y; -.
DR AlphaFoldDB; A9YTQ3; -.
DR SMR; A9YTQ3; -.
DR BioGRID; 121558; 7.
DR STRING; 9606.ENSP00000323816; -.
DR iPTMnet; A9YTQ3; -.
DR PhosphoSitePlus; A9YTQ3; -.
DR BioMuta; AHRR; -.
DR MassIVE; A9YTQ3; -.
DR PaxDb; A9YTQ3; -.
DR PeptideAtlas; A9YTQ3; -.
DR PRIDE; A9YTQ3; -.
DR ProteomicsDB; 2518; -. [A9YTQ3-1]
DR ProteomicsDB; 2519; -. [A9YTQ3-2]
DR ProteomicsDB; 2520; -. [A9YTQ3-3]
DR Antibodypedia; 8774; 125 antibodies from 18 providers.
DR DNASU; 57491; -.
DR GeneID; 57491; -.
DR UCSC; uc003jav.4; human. [A9YTQ3-1]
DR CTD; 57491; -.
DR DisGeNET; 57491; -.
DR GeneCards; AHRR; -.
DR HGNC; HGNC:346; AHRR.
DR HPA; ENSG00000063438; Tissue enriched (testis).
DR MIM; 606517; gene.
DR neXtProt; NX_A9YTQ3; -.
DR PharmGKB; PA24639; -.
DR VEuPathDB; HostDB:ENSG00000063438; -.
DR VEuPathDB; HostDB:ENSG00000288622; -.
DR eggNOG; KOG3560; Eukaryota.
DR HOGENOM; CLU_023661_0_0_1; -.
DR InParanoid; A9YTQ3; -.
DR OrthoDB; 325707at2759; -.
DR PhylomeDB; A9YTQ3; -.
DR TreeFam; TF352074; -.
DR PathwayCommons; A9YTQ3; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-211981; Xenobiotics.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR SignaLink; A9YTQ3; -.
DR BioGRID-ORCS; 57491; 12 hits in 1092 CRISPR screens.
DR ChiTaRS; AHRR; human.
DR GenomeRNAi; 57491; -.
DR Pharos; A9YTQ3; Tbio.
DR PRO; PR:A9YTQ3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A9YTQ3; protein.
DR ExpressionAtlas; A9YTQ3; baseline and differential.
DR Genevisible; A9YTQ3; HS.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR039091; AHR/AHRR.
DR InterPro; IPR039092; AHRR.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR PANTHER; PTHR10649; PTHR10649; 1.
DR PANTHER; PTHR10649:SF3; PTHR10649:SF3; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..701
FT /note="Aryl hydrocarbon receptor repressor"
FT /id="PRO_0000333857"
FT DOMAIN 28..81
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 112..182
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..701
FT /note="Needed for transcriptional repression"
FT /evidence="ECO:0000250"
FT COMPBIAS 371..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..4
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_033563"
FT VAR_SEQ 240
FT /note="L -> LARGSQAWQLRLCCPEPLM (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033564"
FT VARIANT 114
FT /note="L -> P (in dbSNP:rs35008248)"
FT /evidence="ECO:0000269|PubMed:11835227"
FT /id="VAR_043308"
FT VARIANT 189
FT /note="P -> A (in dbSNP:rs2292596)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.5"
FT /id="VAR_043309"
FT VARIANT 373
FT /note="G -> V (in dbSNP:rs2303738)"
FT /id="VAR_043310"
FT VARIANT 627
FT /note="D -> H (in dbSNP:rs34453673)"
FT /id="VAR_043311"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 67..89
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 235..250
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:5Y7Y"
SQ SEQUENCE 701 AA; 76265 MW; 488F6D41298760E0 CRC64;
MPRTMIPPGE CTYAGRKRRR PLQKQRPAVG AEKSNPSKRH RDRLNAELDH LASLLPFPPD
IISKLDKLSV LRLSVSYLRV KSFFQVVQEQ SSRQPAAGAP SPGDSCPLAG SAVLEGRLLL
ESLNGFALVV SAEGTIFYAS ATIVDYLGFH QTDVMHQNIY DYIHVDDRQD FCRQLHWAMD
PPQVVFGQPP PLETGDDAIL GRLLRAQEWG TGTPTEYSAF LTRCFICRVR CLLDSTSGFL
TMQFQGKLKF LFGQKKKAPS GAMLPPRLSL FCIAAPVLLP SAAEMKMRSA LLRAKPRADT
AATADAKVKA TTSLCESELH GKPNYSAGRS SRESGVLVLR EQTDAGRWAQ VPARAPCLCL
RGGPDLVLDP KGGSGDREEE QHRMLSRASG VTGRRETPGP TKPLPWTAGK HSEDGARPRL
QPSKNDPPSL RPMPRGSCLP CPCVQGTFRN SPISHPPSPS PSAYSSRTSR PMRDVGEDQV
HPPLCHFPQR SLQHQLPQPG AQRFATRGYP MEDMKLQGVP MPPGDLCGPT LLLDVSIKME
KDSGCEGAAD GCVPSQVWLG ASDRSHPATF PTRMHLKTEP DSRQQVYISH LGHGVRGAQP
HGRATAGRSR ELTPFHPAHC ACLEPTDGLP QSEPPHQLCA RGRGEQSCTC RAAEAAPVVK
REPLDSPQWA THSQGMVPGM LPKSALATLV PPQASGCTFL P