RED1_MOUSE
ID RED1_MOUSE Reviewed; 711 AA.
AC Q91ZS8; C3TTQ1; Q3UHM7; Q8K3X1; Q91ZS6; Q91ZS7; Q91ZS9; Q99MU8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Double-stranded RNA-specific editase 1;
DE EC=3.5.4.37;
DE AltName: Full=RNA-editing deaminase 1;
DE AltName: Full=RNA-editing enzyme 1;
DE AltName: Full=dsRNA adenosine deaminase;
GN Name=Adarb1; Synonyms=Adar2, Red1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RA Slavov D.B., Gardiner K.;
RT "Phylogenetic comparison of ADAR2 genes and transcripts: conservation and
RT diversity in editing site sequence and alternative splicing patterns.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12709013; DOI=10.1046/j.1365-2567.2003.01598.x;
RA Yang J.-H., Luo X., Nie Y., Su Y., Zhao Q., Kabir K., Zhang D.-X.,
RA Rabinovici R.;
RT "Widespread inosine-containing mRNA in lymphocytes regulated by ADAR1 in
RT response to inflammation.";
RL Immunology 109:15-23(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 6).
RX PubMed=19156214; DOI=10.1371/journal.pone.0004225;
RA Maas S., Gommans W.M.;
RT "Novel exon of mammalian ADAR2 extends open reading frame.";
RL PLoS ONE 4:E4225-E4225(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=17369310; DOI=10.1261/rna.349107;
RA Ohlson J., Pedersen J.S., Haussler D., Ohman M.;
RT "Editing modifies the GABA(A) receptor subunit alpha3.";
RL RNA 13:698-703(2007).
RN [7]
RP REVIEW.
RX PubMed=21182352; DOI=10.1089/jir.2010.0097;
RA George C.X., Gan Z., Liu Y., Samuel C.E.;
RT "Adenosine deaminases acting on RNA, RNA editing, and interferon action.";
RL J. Interferon Cytokine Res. 31:99-117(2011).
RN [8]
RP STRUCTURE BY NMR OF 231-301 IN COMPLEX WITH RNA.
RX PubMed=20946981; DOI=10.1016/j.cell.2010.09.026;
RA Stefl R., Oberstrass F.C., Hood J.L., Jourdan M., Zimmermann M.,
RA Skrisovska L., Maris C., Peng L., Hofr C., Emeson R.B., Allain F.H.;
RT "The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-
RT specific readout of the minor groove.";
RL Cell 143:225-237(2010).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine
CC in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This
CC may affect gene expression and function in a number of ways that
CC include mRNA translation by changing codons and hence the amino acid
CC sequence of proteins; pre-mRNA splicing by altering splice site
CC recognition sequences; RNA stability by changing sequences involved in
CC nuclease recognition; genetic stability in the case of RNA virus
CC genomes by changing sequences during viral RNA replication; and RNA
CC structure-dependent activities such as microRNA production or targeting
CC or protein-RNA interactions. Can edit both viral and cellular RNAs and
CC can edit RNAs at multiple sites (hyper-editing) or at specific sites
CC (site-specific editing). Its cellular RNA substrates include: bladder
CC cancer-associated protein (BLCAP), neurotransmitter receptors for
CC glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor
CC (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA
CC editing of transcripts encoding these proteins results in amino acid
CC substitutions which consequently alter their functional activities.
CC Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the
CC adenosine in hotspot1 much less efficiently. Can inhibit cell
CC proliferation and migration and can stimulate exocytosis.
CC {ECO:0000269|PubMed:17369310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in
CC double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA-
CC COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:82852; EC=3.5.4.37;
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000250};
CC Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Homodimerization is essential for its catalytic
CC activity. Can form heterodimers with isoform 5 of ADAR/ADAR1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=Shuttles between nucleoli and the nucleoplasm.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q91ZS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZS8-2; Sequence=VSP_013711;
CC Name=3;
CC IsoId=Q91ZS8-3; Sequence=VSP_013710, VSP_013711;
CC Name=4;
CC IsoId=Q91ZS8-4; Sequence=VSP_013709;
CC Name=5;
CC IsoId=Q91ZS8-5; Sequence=VSP_013709, VSP_013711;
CC Name=6;
CC IsoId=Q91ZS8-6; Sequence=VSP_041423;
CC -!- MISCELLANEOUS: [Isoform 6]: Likely expressed from an alternative
CC promoter. Contains a region highly similar to the so-called ssRNA-
CC binding R-domain of ADARB2. {ECO:0000305}.
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DR EMBL; AF403106; AAL01301.1; -; mRNA.
DR EMBL; AF403107; AAL01302.1; -; mRNA.
DR EMBL; AF403108; AAL01303.1; -; mRNA.
DR EMBL; AF403109; AAL01304.1; -; mRNA.
DR EMBL; AF525421; AAM83099.1; -; mRNA.
DR EMBL; AY162454; AAN86546.1; -; mRNA.
DR EMBL; AF291049; AAK17102.1; -; mRNA.
DR EMBL; FJ169505; ACN49026.1; -; mRNA.
DR EMBL; AK141777; BAE24831.1; -; mRNA.
DR EMBL; AK147298; BAE27830.1; -; mRNA.
DR EMBL; CH466553; EDL31813.1; -; Genomic_DNA.
DR CCDS; CCDS35948.1; -. [Q91ZS8-1]
DR CCDS; CCDS35949.1; -. [Q91ZS8-2]
DR RefSeq; NP_001020008.1; NM_001024837.2. [Q91ZS8-1]
DR RefSeq; NP_570965.2; NM_130895.3. [Q91ZS8-2]
DR RefSeq; XP_006513128.1; XM_006513065.1.
DR PDB; 2L2K; NMR; -; B=231-301.
DR PDBsum; 2L2K; -.
DR AlphaFoldDB; Q91ZS8; -.
DR BMRB; Q91ZS8; -.
DR SMR; Q91ZS8; -.
DR BioGRID; 225680; 1.
DR STRING; 10090.ENSMUSP00000095976; -.
DR iPTMnet; Q91ZS8; -.
DR PhosphoSitePlus; Q91ZS8; -.
DR EPD; Q91ZS8; -.
DR MaxQB; Q91ZS8; -.
DR PaxDb; Q91ZS8; -.
DR PeptideAtlas; Q91ZS8; -.
DR PRIDE; Q91ZS8; -.
DR ProteomicsDB; 253195; -. [Q91ZS8-1]
DR ProteomicsDB; 253196; -. [Q91ZS8-2]
DR ProteomicsDB; 253197; -. [Q91ZS8-3]
DR ProteomicsDB; 253198; -. [Q91ZS8-4]
DR ProteomicsDB; 253199; -. [Q91ZS8-5]
DR ProteomicsDB; 253200; -. [Q91ZS8-6]
DR Antibodypedia; 10404; 140 antibodies from 27 providers.
DR DNASU; 110532; -.
DR Ensembl; ENSMUST00000020496; ENSMUSP00000020496; ENSMUSG00000020262. [Q91ZS8-2]
DR Ensembl; ENSMUST00000098374; ENSMUSP00000095976; ENSMUSG00000020262. [Q91ZS8-1]
DR Ensembl; ENSMUST00000105406; ENSMUSP00000101046; ENSMUSG00000020262. [Q91ZS8-1]
DR GeneID; 110532; -.
DR KEGG; mmu:110532; -.
DR UCSC; uc007fvl.2; mouse. [Q91ZS8-3]
DR UCSC; uc007fvm.2; mouse. [Q91ZS8-1]
DR UCSC; uc007fvn.2; mouse. [Q91ZS8-5]
DR UCSC; uc007fvp.2; mouse. [Q91ZS8-2]
DR CTD; 104; -.
DR MGI; MGI:891999; Adarb1.
DR VEuPathDB; HostDB:ENSMUSG00000020262; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000155992; -.
DR HOGENOM; CLU_005382_3_1_1; -.
DR InParanoid; Q91ZS8; -.
DR OMA; ACLFKAF; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q91ZS8; -.
DR TreeFam; TF315806; -.
DR Reactome; R-MMU-75102; C6 deamination of adenosine.
DR Reactome; R-MMU-77042; Formation of editosomes by ADAR proteins.
DR BioGRID-ORCS; 110532; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Adarb1; mouse.
DR EvolutionaryTrace; Q91ZS8; -.
DR PRO; PR:Q91ZS8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91ZS8; protein.
DR Bgee; ENSMUSG00000020262; Expressed in medial dorsal nucleus of thalamus and 213 other tissues.
DR ExpressionAtlas; Q91ZS8; baseline and differential.
DR Genevisible; Q91ZS8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; ISS:HGNC-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:HGNC-UCL.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
DR GO; GO:0016553; P:base conversion or substitution editing; ISO:MGI.
DR GO; GO:0021610; P:facial nerve morphogenesis; IMP:MGI.
DR GO; GO:0021618; P:hypoglossal nerve morphogenesis; IMP:MGI.
DR GO; GO:0060384; P:innervation; IMP:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0016556; P:mRNA modification; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0060415; P:muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0050685; P:positive regulation of mRNA processing; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0006396; P:RNA processing; ISS:HGNC-UCL.
DR GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IMP:MGI.
DR CDD; cd19895; DSRM_RED1_rpt1; 1.
DR CDD; cd19898; DSRM_RED1_rpt2; 1.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044458; ADAR2_DSRM_1.
DR InterPro; IPR044459; ADAR2_DSRM_2.
DR InterPro; IPR014720; dsRBD_dom.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Metal-binding;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc.
FT CHAIN 1..711
FT /note="Double-stranded RNA-specific editase 1"
FT /id="PRO_0000171780"
FT DOMAIN 78..144
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 231..298
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 370..707
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..88
FT /note="Interaction with substrate RNA"
FT /evidence="ECO:0000250"
FT REGION 104..105
FT /note="Interaction with substrate RNA"
FT /evidence="ECO:0000250"
FT REGION 176..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..242
FT /note="Interaction with substrate RNA"
FT /evidence="ECO:0000250"
FT REGION 259
FT /note="Interaction with substrate RNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 400
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 529
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 639
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 672
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 700
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78563"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013709"
FT VAR_SEQ 1..10
FT /note="MDIEDEENMS -> MPLG (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013710"
FT VAR_SEQ 1
FT /note="M -> MASLGLGTLTVGAFFSFVGRRYKRRRKKRSERKDKRGLRQSRSPQKC
FT FTM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:19156214"
FT /id="VSP_041423"
FT VAR_SEQ 466..475
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12709013, ECO:0000303|Ref.1"
FT /id="VSP_013711"
FT CONFLICT 65
FT /note="Y -> C (in Ref. 2; AAK17102)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="S -> G (in Ref. 2; AAK17102)"
FT /evidence="ECO:0000305"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:2L2K"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2L2K"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:2L2K"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2L2K"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:2L2K"
SQ SEQUENCE 711 AA; 78001 MW; A5C87E894C867DE1 CRC64;
MDIEDEENMS SSSTDIKENR NLDNMPPKDS STPGPGEGIP LSNGGGGSTS RKRPLEEGSN
GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYMLLSQ TGPVHAPLFV MSVEVNGQVF
EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF
ETPDKSEPPF YVGSNGDDSF SSSGDVSLSA SPVPASLTQP PLPIPPPFPP PSGKNPVMIL
NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALATVFNLH
LDQTPSRQPV LSEGLQLHLP QVLADAVSRL VLGKFSDLTD NFSSPHARRK VLSGVVMTTG
TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYAQ LELYLNNKED
QKKSIFQKSE RGGFRLKDTV QFHLYISTSP CGDARIFSPH EPVLEGMTPD SHQLTEPADR
HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG
SLLSIFVEPI YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR
QPGKAPNFSV NWTVGDATIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH GKVPPHLLRT
KITKPTTYHE SKLAAREYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSFT P
