PELO_HUMAN
ID PELO_HUMAN Reviewed; 385 AA.
AC Q9BRX2; Q9GZS6; Q9Y306;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=PELO; ORFNames=CGI-17;
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], TISSUE SPECIFICITY, AND VARIANT MET-221.
RC TISSUE=Testis;
RX PubMed=11060452; DOI=10.1159/000015667;
RA Shamsadin R., Adham I.M., von Beust G., Engel W.;
RT "Molecular cloning, expression and chromosome location of the human pelota
RT gene PELO.";
RL Cytogenet. Cell Genet. 90:75-78(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-221.
RA Shamsadin R.;
RT "Gene structure prediction and evidence of alternative splicing in the
RT human pelota gene.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
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 MRNA], AND VARIANT MET-221.
RC TISSUE=Brain, Skin, and Uterus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND
RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=21448132; DOI=10.1038/emboj.2011.93;
RA Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V.;
RT "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes
RT and stalled elongation complexes.";
RL EMBO J. 30:1804-1817(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND
RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-162, AND IDENTIFICATION BY MASS
RP 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 [15]
RP FUNCTION, AND INTERACTION WITH PINK1; ABCE1 AND CNOT4.
RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007;
RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T.,
RA Montgomery S., Lu B.;
RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links
RT Co-translational Quality Control to PINK1-Directed Mitophagy.";
RL Cell Metab. 28:130-144.e7(2018).
RN [16]
RP STRUCTURE BY NMR OF 261-371.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal domain of the human pelota homolog
RT (CGI-17).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (PubMed:21448132, PubMed:29861391). In the presence
CC of ABCE1 and HBS1L, is required for 48S complex formation from 80S
CC ribosomes and dissociation of vacant 80S ribosomes (PubMed:21448132).
CC Together with HBS1L and in presence of ABCE1, recognizes stalled
CC ribosomes and promotes dissociation of elongation complexes assembled
CC on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA,
CC a mechanism to release non-functional ribosomes and to degrade damaged
CC mRNAs as part of the No-Go Decay (NGD) pathway (PubMed:21448132). As
CC part of the PINK1-regulated signaling, upon mitochondrial damage is
CC recruited to the ribosome/mRNA-ribonucleoprotein complex associated to
CC mitochondrial outer membrane thereby enabling the recruitment of
CC autophagy receptors and induction of mitophagy (PubMed:29861391).
CC {ECO:0000269|PubMed:21448132, ECO:0000269|PubMed:29861391}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P33309};
CC -!- SUBUNIT: Interacts with PINK1, ABCE1 and CNOT4.
CC {ECO:0000269|PubMed:29861391}.
CC -!- INTERACTION:
CC Q9BRX2; O95817: BAG3; NbExp=3; IntAct=EBI-1043580, EBI-747185;
CC Q9BRX2; P63172: DYNLT1; NbExp=3; IntAct=EBI-1043580, EBI-1176455;
CC Q9BRX2; O75821: EIF3G; NbExp=6; IntAct=EBI-1043580, EBI-366632;
CC Q9BRX2; P11362-2: FGFR1; NbExp=3; IntAct=EBI-1043580, EBI-25852941;
CC Q9BRX2; P21333-2: FLNA; NbExp=6; IntAct=EBI-1043580, EBI-9641086;
CC Q9BRX2; O00165: HAX1; NbExp=7; IntAct=EBI-1043580, EBI-357001;
CC Q9BRX2; D9YZV0: HBS1L; NbExp=3; IntAct=EBI-1043580, EBI-10297269;
CC Q9BRX2; Q9Y450: HBS1L; NbExp=4; IntAct=EBI-1043580, EBI-2868258;
CC Q9BRX2; P04792: HSPB1; NbExp=4; IntAct=EBI-1043580, EBI-352682;
CC Q9BRX2; P42858: HTT; NbExp=12; IntAct=EBI-1043580, EBI-466029;
CC Q9BRX2; P05362: ICAM1; NbExp=3; IntAct=EBI-1043580, EBI-1035358;
CC Q9BRX2; Q92993: KAT5; NbExp=3; IntAct=EBI-1043580, EBI-399080;
CC Q9BRX2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1043580, EBI-10975473;
CC Q9BRX2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-1043580, EBI-10176379;
CC Q9BRX2; Q8TAP4-4: LMO3; NbExp=9; IntAct=EBI-1043580, EBI-11742507;
CC Q9BRX2; P61968: LMO4; NbExp=3; IntAct=EBI-1043580, EBI-2798728;
CC Q9BRX2; P31153: MAT2A; NbExp=3; IntAct=EBI-1043580, EBI-1050743;
CC Q9BRX2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1043580, EBI-16439278;
CC Q9BRX2; Q9HB07: MYG1; NbExp=3; IntAct=EBI-1043580, EBI-709754;
CC Q9BRX2; P07196: NEFL; NbExp=3; IntAct=EBI-1043580, EBI-475646;
CC Q9BRX2; P62937-2: PPIA; NbExp=3; IntAct=EBI-1043580, EBI-25884072;
CC Q9BRX2; P17252: PRKCA; NbExp=3; IntAct=EBI-1043580, EBI-1383528;
CC Q9BRX2; P60891: PRPS1; NbExp=3; IntAct=EBI-1043580, EBI-749195;
CC Q9BRX2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1043580, EBI-9090795;
CC Q9BRX2; P78539: SRPX; NbExp=6; IntAct=EBI-1043580, EBI-2371213;
CC Q9BRX2; O76024: WFS1; NbExp=3; IntAct=EBI-1043580, EBI-720609;
CC Q9BRX2; P61981: YWHAG; NbExp=3; IntAct=EBI-1043580, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11060452}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000305}.
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DR EMBL; AF139828; AAG22574.1; -; mRNA.
DR EMBL; AF143952; AAG22575.1; -; Genomic_DNA.
DR EMBL; AY117399; AAM89414.1; -; mRNA.
DR EMBL; AF132951; AAD27726.1; -; mRNA.
DR EMBL; AC026230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005889; AAH05889.1; -; mRNA.
DR EMBL; BC007249; AAH07249.1; -; mRNA.
DR EMBL; BC007650; AAH07650.1; -; mRNA.
DR EMBL; BC022789; AAH22789.1; -; mRNA.
DR CCDS; CCDS3956.1; -.
DR RefSeq; NP_057030.3; NM_015946.4.
DR PDB; 1X52; NMR; -; A=261-371.
DR PDB; 5EO3; X-ray; 2.60 A; A/B=265-385.
DR PDB; 5LZW; EM; 3.53 A; ii=1-385.
DR PDB; 5LZX; EM; 3.67 A; ii=1-385.
DR PDB; 5LZY; EM; 3.99 A; ii=1-385.
DR PDB; 5LZZ; EM; 3.47 A; ii=1-385.
DR PDBsum; 1X52; -.
DR PDBsum; 5EO3; -.
DR PDBsum; 5LZW; -.
DR PDBsum; 5LZX; -.
DR PDBsum; 5LZY; -.
DR PDBsum; 5LZZ; -.
DR AlphaFoldDB; Q9BRX2; -.
DR SMR; Q9BRX2; -.
DR BioGRID; 119818; 149.
DR IntAct; Q9BRX2; 53.
DR MINT; Q9BRX2; -.
DR STRING; 9606.ENSP00000274311; -.
DR iPTMnet; Q9BRX2; -.
DR MetOSite; Q9BRX2; -.
DR PhosphoSitePlus; Q9BRX2; -.
DR BioMuta; PELO; -.
DR DMDM; 322510057; -.
DR EPD; Q9BRX2; -.
DR jPOST; Q9BRX2; -.
DR MassIVE; Q9BRX2; -.
DR MaxQB; Q9BRX2; -.
DR PaxDb; Q9BRX2; -.
DR PeptideAtlas; Q9BRX2; -.
DR PRIDE; Q9BRX2; -.
DR ProteomicsDB; 78846; -.
DR Antibodypedia; 23309; 151 antibodies from 25 providers.
DR DNASU; 53918; -.
DR Ensembl; ENST00000274311.3; ENSP00000274311.2; ENSG00000152684.11.
DR GeneID; 53918; -.
DR KEGG; hsa:53918; -.
DR MANE-Select; ENST00000274311.3; ENSP00000274311.2; NM_015946.5; NP_057030.3.
DR UCSC; uc003jos.5; human.
DR CTD; 53918; -.
DR DisGeNET; 53918; -.
DR GeneCards; PELO; -.
DR HGNC; HGNC:8829; PELO.
DR HPA; ENSG00000152684; Low tissue specificity.
DR MIM; 605757; gene.
DR neXtProt; NX_Q9BRX2; -.
DR OpenTargets; ENSG00000152684; -.
DR PharmGKB; PA33174; -.
DR VEuPathDB; HostDB:ENSG00000152684; -.
DR eggNOG; KOG2869; Eukaryota.
DR GeneTree; ENSGT00390000016326; -.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; Q9BRX2; -.
DR OMA; DDLWHLK; -.
DR PhylomeDB; Q9BRX2; -.
DR TreeFam; TF105733; -.
DR PathwayCommons; Q9BRX2; -.
DR SignaLink; Q9BRX2; -.
DR BioGRID-ORCS; 53918; 588 hits in 1089 CRISPR screens.
DR EvolutionaryTrace; Q9BRX2; -.
DR GeneWiki; PELO; -.
DR GenomeRNAi; 53918; -.
DR Pharos; Q9BRX2; Tbio.
DR PRO; PR:Q9BRX2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BRX2; protein.
DR Bgee; ENSG00000152684; Expressed in vena cava and 195 other tissues.
DR Genevisible; Q9BRX2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IEA:Ensembl.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IBA:GO_Central.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 2.30.30.870; -; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR038069; Pelota/DOM34_N.
DR InterPro; IPR004405; Transl-rel_pelota.
DR PANTHER; PTHR10853; PTHR10853; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF159065; SSF159065; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Endonuclease;
KW Hydrolase; Isopeptide bond; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..385
FT /note="Protein pelota homolog"
FT /id="PRO_0000143188"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 162
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 221
FT /note="L -> M (in dbSNP:rs1499280)"
FT /evidence="ECO:0000269|PubMed:10810093,
FT ECO:0000269|PubMed:11060452, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.2"
FT /id="VAR_019777"
FT CONFLICT 135
FT /note="A -> D (in Ref. 1; AAG22574/AAG22575)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> G (in Ref. 3; AAD27726)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..264
FT /note="AS -> LA (in Ref. 3; AAD27726)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="F -> S (in Ref. 3; AAD27726)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="S -> Y (in Ref. 1; AAG22574/AAG22575)"
FT /evidence="ECO:0000305"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:5EO3"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5EO3"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5EO3"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:5EO3"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:5EO3"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:5EO3"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:5EO3"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5EO3"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:5EO3"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:5EO3"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:5EO3"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:5EO3"
SQ SEQUENCE 385 AA; 43359 MW; 8A0D264202995B76 CRC64;
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT
GVAAILRFPV PELSDQEGDS SSEED
