ERN2_HUMAN
ID ERN2_HUMAN Reviewed; 926 AA.
AC Q76MJ5; Q6ZNC0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE2;
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 2;
DE AltName: Full=Inositol-requiring protein 2;
DE Short=hIRE2p;
DE AltName: Full=Ire1-beta;
DE Short=IRE1b;
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE Includes:
DE RecName: Full=Endoribonuclease;
DE EC=3.1.26.-;
DE Flags: Precursor;
GN Name=ERN2 {ECO:0000312|HGNC:HGNC:16942};
GN Synonyms=IRE2 {ECO:0000250|UniProtKB:O75460};
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] {ECO:0000305, ECO:0000312|EMBL:BAB21297.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-548, AND VARIANTS GLN-271 AND
RP THR-487.
RC TISSUE=Fetal lung fibroblast {ECO:0000312|EMBL:BAB21297.1};
RX PubMed=11175748; DOI=10.1038/35055065;
RA Iwawaki T., Hosoda A., Okuda T., Kamigori Y., Nomura-Furuwatari C.,
RA Kimata Y., Tsuru A., Kohno K.;
RT "Translational control by the ER transmembrane kinase/ribonuclease IRE1
RT under ER stress.";
RL Nat. Cell Biol. 3:158-164(2001).
RN [2] {ECO:0000312|EMBL:BAD18455.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD18455.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-69; CYS-118; CYS-184; GLN-271; THR-318;
RP PHE-410; THR-487; PHE-504; GLN-537 AND TYR-858.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Induces translational repression through 28S ribosomal RNA
CC cleavage in response to ER stress. Pro-apoptotic. Appears to play no
CC role in the unfolded-protein response, unlike closely related proteins.
CC {ECO:0000269|PubMed:11175748}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11175748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11175748};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: The kinase domain is activated by trans-
CC autophosphorylation. Kinase activity is required for activation of the
CC endoribonuclease domain (By similarity).
CC {ECO:0000250|UniProtKB:O75460}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11175748}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11175748}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11175748}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18455.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB047079; BAB21297.1; -; mRNA.
DR EMBL; AK131280; BAD18455.1; ALT_INIT; mRNA.
DR EMBL; AC012317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32407.2; -.
DR RefSeq; NP_001295149.2; NM_001308220.1.
DR RefSeq; NP_150296.4; NM_033266.3.
DR AlphaFoldDB; Q76MJ5; -.
DR SMR; Q76MJ5; -.
DR BioGRID; 115843; 3.
DR IntAct; Q76MJ5; 20.
DR STRING; 9606.ENSP00000256797; -.
DR BindingDB; Q76MJ5; -.
DR ChEMBL; CHEMBL4105932; -.
DR iPTMnet; Q76MJ5; -.
DR PhosphoSitePlus; Q76MJ5; -.
DR BioMuta; ERN2; -.
DR DMDM; 327478597; -.
DR jPOST; Q76MJ5; -.
DR MassIVE; Q76MJ5; -.
DR PaxDb; Q76MJ5; -.
DR PeptideAtlas; Q76MJ5; -.
DR PRIDE; Q76MJ5; -.
DR ProteomicsDB; 68688; -.
DR Antibodypedia; 12645; 215 antibodies from 30 providers.
DR DNASU; 10595; -.
DR Ensembl; ENST00000256797.9; ENSP00000256797.5; ENSG00000134398.15.
DR GeneID; 10595; -.
DR KEGG; hsa:10595; -.
DR MANE-Select; ENST00000256797.9; ENSP00000256797.5; NM_033266.4; NP_150296.4.
DR UCSC; uc002dma.5; human.
DR CTD; 10595; -.
DR DisGeNET; 10595; -.
DR GeneCards; ERN2; -.
DR HGNC; HGNC:16942; ERN2.
DR HPA; ENSG00000134398; Group enriched (cervix, gallbladder, intestine, salivary gland, stomach).
DR MIM; 604034; gene.
DR neXtProt; NX_Q76MJ5; -.
DR OpenTargets; ENSG00000134398; -.
DR PharmGKB; PA134889542; -.
DR VEuPathDB; HostDB:ENSG00000134398; -.
DR eggNOG; KOG1027; Eukaryota.
DR GeneTree; ENSGT00940000160812; -.
DR InParanoid; Q76MJ5; -.
DR OMA; EKTPDSY; -.
DR OrthoDB; 1019877at2759; -.
DR PhylomeDB; Q76MJ5; -.
DR TreeFam; TF313986; -.
DR PathwayCommons; Q76MJ5; -.
DR SignaLink; Q76MJ5; -.
DR BioGRID-ORCS; 10595; 5 hits in 1072 CRISPR screens.
DR ChiTaRS; ERN2; human.
DR GenomeRNAi; 10595; -.
DR Pharos; Q76MJ5; Tbio.
DR PRO; PR:Q76MJ5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q76MJ5; protein.
DR Bgee; ENSG00000134398; Expressed in nasal cavity epithelium and 185 other tissues.
DR ExpressionAtlas; Q76MJ5; baseline and differential.
DR Genevisible; Q76MJ5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0030263; P:apoptotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR Gene3D; 1.20.1440.180; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR033523; IRE2.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; PTHR13954; 1.
DR PANTHER; PTHR13954:SF15; PTHR13954:SF15; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Endoplasmic reticulum; Hydrolase; Kinase;
KW Magnesium; Membrane; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..926
FT /note="Serine/threonine-protein kinase/endoribonuclease
FT IRE2"
FT /id="PRO_0000024329"
FT TOPO_DOM 35..430
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 520..781
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 784..912
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 478..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 637
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 526..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 69
FT /note="V -> I (in dbSNP:rs9932495)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040495"
FT VARIANT 118
FT /note="R -> C (in dbSNP:rs56117885)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040496"
FT VARIANT 184
FT /note="R -> C (in dbSNP:rs34683474)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040497"
FT VARIANT 271
FT /note="R -> Q (in dbSNP:rs55772851)"
FT /evidence="ECO:0000269|PubMed:11175748,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_040498"
FT VARIANT 318
FT /note="A -> T (in dbSNP:rs56191901)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040499"
FT VARIANT 410
FT /note="L -> F (in dbSNP:rs55687638)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040500"
FT VARIANT 487
FT /note="S -> T (in dbSNP:rs26764)"
FT /evidence="ECO:0000269|PubMed:11175748,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_040501"
FT VARIANT 504
FT /note="L -> F (in dbSNP:rs56001432)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040502"
FT VARIANT 537
FT /note="R -> Q (in dbSNP:rs56176960)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040503"
FT VARIANT 858
FT /note="H -> Y (in dbSNP:rs56137182)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040504"
FT MUTAGEN 548
FT /note="K->A: Loss of autophosphorylation, of induction of
FT apoptosis and of 28S rRNA cleavage, attenuation of
FT repression of protein synthesis."
FT /evidence="ECO:0000269|PubMed:11175748"
FT CONFLICT 99
FT /note="Q -> L (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="E -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> E (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> M (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="T -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> T (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> P (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="T -> I (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="Missing (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="A -> V (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..474
FT /note="FAH -> TAD (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="A -> V (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..491
FT /note="RRSQ -> LRSK (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="R -> H (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="S -> T (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="D -> N (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="A -> V (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="G -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="P -> L (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="P -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="V -> M (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="A -> T (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="T -> I (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="R -> Q (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="A -> V (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="R -> G (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="T -> A (in Ref. 1; BAB21297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 102480 MW; B580794191B66DA2 CRC64;
MASAVRGSRP WPRLGLQLQF AALLLGTLSP QVHTLRPENL LLVSTLDGSL HALSKQTGDL
KWTLRDDPVI EGPMYVTEMA FLSDPADGSL YILGTQKQQG LMKLPFTIPE LVHASPCRSS
DGVFYTGRKQ DAWFVVDPES GETQMTLTTE GPSTPRLYIG RTQYTVTMHD PRAPALRWNT
TYRRYSAPPM DGSPGKYMSH LASCGMGLLL TVDPGSGTVL WTQDLGVPVM GVYTWHQDGL
RQLPHLTLAR DTLHFLALRW GHIRLPASGP RDTATLFSTL DTQLLMTLYV GKDETGFYVS
KALVHTGVAL VPRGLTLAPA DGPTTDEVTL QVSGEREGSP STAVRYPSGS VALPSQWLLI
GHHELPPVLH TTMLRVHPTL GSGTAETRPP ENTQAPAFFL ELLSLSREKL WDSELHPEEK
TPDSYLGLGP QDLLAASLTA VLLGGWILFV MRQQQPQVVE KQQETPLAPA DFAHISQDAQ
SLHSGASRRS QKRLQSPSKQ AQPLDDPEAE QLTVVGKISF NPKDVLGRGA GGTFVFRGQF
EGRAVAVKRL LRECFGLVRR EVQLLQESDR HPNVLRYFCT ERGPQFHYIA LELCRASLQE
YVENPDLDRG GLEPEVVLQQ LMSGLAHLHS LHIVHRDLKP GNILITGPDS QGLGRVVLSD
FGLCKKLPAG RCSFSLHSGI PGTEGWMAPE LLQLLPPDSP TSAVDIFSAG CVFYYVLSGG
SHPFGDSLYR QANILTGAPC LAHLEEEVHD KVVARDLVGA MLSPLPQPRP SAPQVLAHPF
FWSRAKQLQF FQDVSDWLEK ESEQEPLVRA LEAGGCAVVR DNWHEHISMP LQTDLRKFRS
YKGTSVRDLL RAVRNKKHHY RELPVEVRQA LGQVPDGFVQ YFTNRFPRLL LHTHRAMRSC
ASESLFLPYY PPDSEARRPC PGATGR
