ERI1_HUMAN
ID ERI1_HUMAN Reviewed; 349 AA.
AC Q8IV48; A8K4U7; Q9NSX3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=3'-5' exoribonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=3'-5' exonuclease ERI1;
DE AltName: Full=Eri-1 homolog;
DE AltName: Full=Histone mRNA 3'-end-specific exoribonuclease;
DE AltName: Full=Histone mRNA 3'-exonuclease 1;
DE AltName: Full=Protein 3'hExo;
DE Short=HEXO;
GN Name=ERI1; Synonyms=3'EXO, THEX1;
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], PROTEIN SEQUENCE OF 2-23; 43-48; 53-67;
RP 161-172; 200-208; 225-237; 263-269 AND 284-291, FUNCTION, ACTIVITY
RP REGULATION, ENZYME ACTIVITY, AND RNA-BINDING.
RX PubMed=14536070; DOI=10.1016/s1097-2765(03)00278-8;
RA Dominski Z., Yang X.-C., Kaygun H., Dadlez M., Marzluff W.F.;
RT "A 3' exonuclease that specifically interacts with the 3' end of histone
RT mRNA.";
RL Mol. Cell 12:295-305(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-16.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP ENZYME ACTIVITY IN VITRO.
RX PubMed=14961122; DOI=10.1038/nature02302;
RA Kennedy S., Wang D., Ruvkun G.;
RT "A conserved siRNA-degrading RNase negatively regulates RNA interference in
RT C. elegans.";
RL Nature 427:645-649(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN A TERNARY COMPLEX, ENZYME ACTIVITY, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF LYS-92; ARG-96; LYS-99; LYS-104; ARG-105; TYR-109;
RP TYR-110; LYS-111; LYS-112; ASP-234; MET-235 AND ASP-298, AND RNA-BINDING.
RX PubMed=16912046; DOI=10.1074/jbc.m602947200;
RA Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.;
RT "Characterization of 3'hExo, a 3' exonuclease specifically interacting with
RT the 3' end of histone mRNA.";
RL J. Biol. Chem. 281:30447-30454(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-62, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 123-322 IN COMPLEX WITH MAGNESIUM
RP IONS AND AMP.
RX PubMed=15451662; DOI=10.1016/j.jmb.2004.08.055;
RA Cheng Y., Patel D.J.;
RT "Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh
RT family member, bound to rAMP.";
RL J. Mol. Biol. 343:305-312(2004).
CC -!- FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and
CC degrades them, suggesting that it plays an essential role in histone
CC mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last
CC nucleotide of the histone 3'-end is required for efficient degradation
CC of RNA substrates. Also able to degrade the 3'-overhangs of short
CC interfering RNAs (siRNAs) in vitro, suggesting a possible role as
CC regulator of RNA interference (RNAi). Requires for binding the 5'-
CC ACCCA-3' sequence present in stem-loop structure. Able to bind other
CC mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s
CC ribosomal RNA. Binds with high affinity to the stem-loop structure of
CC replication-dependent histone pre-mRNAs. {ECO:0000269|PubMed:14536070,
CC ECO:0000269|PubMed:16912046}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- ACTIVITY REGULATION: Although it can bind simultaneously with SLBP to
CC the 3'-end of histone mRNA, the presence of SLBP prevents the
CC exonuclease activity. {ECO:0000269|PubMed:14536070}.
CC -!- SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of
CC ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts in a cooperative
CC manner with SLBP to the mature 3'-end of histone mRNAs (By similarity).
CC Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes.
CC Found in a ternary complex with SLBP and the stem-loop structure of the
CC 3'-end of histone mRNAs. {ECO:0000250, ECO:0000269|PubMed:15451662,
CC ECO:0000269|PubMed:16912046}.
CC -!- INTERACTION:
CC Q8IV48; A9UHW6: MIF4GD; NbExp=2; IntAct=EBI-5459222, EBI-373498;
CC Q8IV48; Q14493: SLBP; NbExp=2; IntAct=EBI-5459222, EBI-2696402;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16912046}. Nucleus
CC {ECO:0000269|PubMed:16912046}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:16912046}.
CC -!- DOMAIN: The SAP domain is necessary for binding to the stem-loop
CC structure of histone mRNAs and to form the ternary complex with SLBP,
CC but not for 3'-end histone mRNA exonuclease activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70871.2; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB70871.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY310909; AAQ21219.1; -; mRNA.
DR EMBL; AK291062; BAF83751.1; -; mRNA.
DR EMBL; AL137679; CAB70871.2; ALT_SEQ; mRNA.
DR EMBL; BC035279; AAH35279.1; -; mRNA.
DR CCDS; CCDS5972.1; -.
DR PIR; T46432; T46432.
DR RefSeq; NP_699163.2; NM_153332.3.
DR PDB; 1W0H; X-ray; 1.59 A; A=123-322.
DR PDB; 1ZBH; X-ray; 3.00 A; A/B/C/D=51-349.
DR PDB; 1ZBU; X-ray; 3.00 A; A/B/C/D=1-349.
DR PDB; 4L8R; X-ray; 2.60 A; B/E=55-349.
DR PDB; 4QOZ; X-ray; 2.30 A; B/E=55-349.
DR PDBsum; 1W0H; -.
DR PDBsum; 1ZBH; -.
DR PDBsum; 1ZBU; -.
DR PDBsum; 4L8R; -.
DR PDBsum; 4QOZ; -.
DR AlphaFoldDB; Q8IV48; -.
DR SMR; Q8IV48; -.
DR BioGRID; 124718; 45.
DR DIP; DIP-61409N; -.
DR IntAct; Q8IV48; 16.
DR MINT; Q8IV48; -.
DR STRING; 9606.ENSP00000429615; -.
DR iPTMnet; Q8IV48; -.
DR PhosphoSitePlus; Q8IV48; -.
DR BioMuta; ERI1; -.
DR DMDM; 45476938; -.
DR EPD; Q8IV48; -.
DR jPOST; Q8IV48; -.
DR MassIVE; Q8IV48; -.
DR MaxQB; Q8IV48; -.
DR PaxDb; Q8IV48; -.
DR PeptideAtlas; Q8IV48; -.
DR PRIDE; Q8IV48; -.
DR ProteomicsDB; 70659; -.
DR Antibodypedia; 8346; 301 antibodies from 31 providers.
DR DNASU; 90459; -.
DR Ensembl; ENST00000250263.8; ENSP00000250263.7; ENSG00000104626.15.
DR Ensembl; ENST00000519292.5; ENSP00000430190.1; ENSG00000104626.15.
DR GeneID; 90459; -.
DR KEGG; hsa:90459; -.
DR MANE-Select; ENST00000250263.8; ENSP00000250263.7; NM_153332.4; NP_699163.2.
DR UCSC; uc003wsk.2; human.
DR CTD; 90459; -.
DR DisGeNET; 90459; -.
DR GeneCards; ERI1; -.
DR HGNC; HGNC:23994; ERI1.
DR HPA; ENSG00000104626; Low tissue specificity.
DR MIM; 608739; gene.
DR neXtProt; NX_Q8IV48; -.
DR OpenTargets; ENSG00000104626; -.
DR PharmGKB; PA164719226; -.
DR VEuPathDB; HostDB:ENSG00000104626; -.
DR eggNOG; KOG0542; Eukaryota.
DR GeneTree; ENSGT00530000063205; -.
DR HOGENOM; CLU_037266_4_1_1; -.
DR OMA; QLSEFCI; -.
DR OrthoDB; 809000at2759; -.
DR PhylomeDB; Q8IV48; -.
DR TreeFam; TF313449; -.
DR PathwayCommons; Q8IV48; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q8IV48; -.
DR BioGRID-ORCS; 90459; 35 hits in 1090 CRISPR screens.
DR ChiTaRS; ERI1; human.
DR EvolutionaryTrace; Q8IV48; -.
DR GenomeRNAi; 90459; -.
DR Pharos; Q8IV48; Tbio.
DR PRO; PR:Q8IV48; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8IV48; protein.
DR Bgee; ENSG00000104626; Expressed in secondary oocyte and 141 other tissues.
DR ExpressionAtlas; Q8IV48; baseline and differential.
DR Genevisible; Q8IV48; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0071207; F:histone pre-mRNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031125; P:rRNA 3'-end processing; ISS:UniProtKB.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:14536070"
FT CHAIN 2..349
FT /note="3'-5' exoribonuclease 1"
FT /id="PRO_0000187007"
FT DOMAIN 76..110
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 130..306
FT /note="Exonuclease"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 136
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15451662"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 137
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15451662"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 293
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15451662"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 16
FT /note="L -> P (in dbSNP:rs2288672)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_018107"
FT MUTAGEN 92
FT /note="K->A: Does not inhibit RNA-binding to the stem-loop
FT structure. Does not inhibit RNA-binding to the stem-loop
FT structure, when associated with A-104."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 96
FT /note="R->A: Does not inhibit RNA-binding to the stem-loop
FT structure."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 99
FT /note="K->A: Reduces slightly RNA-binding to the stem-loop
FT structure."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 104
FT /note="K->A: Does not inhibit RNA-binding to the stem-loop
FT structure. Does not inhibit RNA-binding to the stem-loop
FT structure, when associated with A-92."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 105
FT /note="R->A: Inhibits RNA-binding to the stem-loop
FT structure."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 109
FT /note="Y->A: Reduces slightly RNA-binding to the stem-loop
FT structure; when associated with A-110."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 110
FT /note="Y->A: Reduces slightly RNA-binding to the stem-loop
FT structure; when associated with A-109."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 111
FT /note="K->A: Reduces RNA-binding to the stem-loop structure
FT but not 3'-end histone mRNA exonuclease activity; when
FT associated with A-112."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 112
FT /note="K->A: Reduces RNA-binding to the stem-loop structure
FT but not 3'-end histone mRNA exonuclease activity; when
FT associated with A-111."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 234
FT /note="D->A: Inhibits 3'-end histone mRNA exonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 235
FT /note="M->A: Inhibits RNA-binding to the stem-loop
FT structure and 3'-end histone mRNA exonuclease activity."
FT /evidence="ECO:0000269|PubMed:16912046"
FT MUTAGEN 298
FT /note="D->A: Inhibits 3'-end histone mRNA exonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:16912046"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1ZBU"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1ZBU"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1ZBU"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:4QOZ"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:4QOZ"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:4QOZ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1ZBU"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:1W0H"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1ZBU"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:1W0H"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:1W0H"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:1W0H"
FT HELIX 295..311
FT /evidence="ECO:0007829|PDB:1W0H"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4QOZ"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4QOZ"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1ZBH"
SQ SEQUENCE 349 AA; 40064 MW; D5837AA05F09410C CRC64;
MEDPQSKEPA GEAVALALLE SPRPEGGEEP PRPSPEETQQ CKFDGQETKG SKFITSSASD
FSDPVYKEIA ITNGCINRMS KEELRAKLSE FKLETRGVKD VLKKRLKNYY KKQKLMLKES
NFADSYYDYI CIIDFEATCE EGNPPEFVHE IIEFPVVLLN THTLEIEDTF QQYVRPEINT
QLSDFCISLT GITQDQVDRA DTFPQVLKKV IDWMKLKELG TKYKYSLLTD GSWDMSKFLN
IQCQLSRLKY PPFAKKWINI RKSYGNFYKV PRSQTKLTIM LEKLGMDYDG RPHCGLDDSK
NIARIAVRML QDGCELRINE KMHAGQLMSV SSSLPIEGTP PPQMPHFRK
