NLRX1_HUMAN
ID NLRX1_HUMAN Reviewed; 975 AA.
AC Q86UT6; A8K6Q1; B3KPK2; B3KTA2; Q7RTR3; Q96D51; Q9H724;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=NLR family member X1;
DE AltName: Full=Caterpiller protein 11.3;
DE Short=CLR11.3;
DE AltName: Full=Nucleotide-binding oligomerization domain protein 5 {ECO:0000312|EMBL:ABO40480.1};
DE AltName: Full=Nucleotide-binding oligomerization domain protein 9 {ECO:0000303|PubMed:12766759};
DE Flags: Precursor;
GN Name=NLRX1;
GN Synonyms=NOD5 {ECO:0000312|EMBL:ABO40480.1},
GN NOD9 {ECO:0000303|PubMed:12766759};
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] (ISOFORM 1), AND VARIANTS SER-63 AND GLU-793.
RX PubMed=12766759; DOI=10.1038/nri1086;
RA Inohara N., Nunez G.;
RT "NODs: intracellular proteins involved in inflammation and apoptosis.";
RL Nat. Rev. Immunol. 3:371-382(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kronos K.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT "Identification of a 500-kb region of common allelic loss in chromosome
RT 11q23 in non-MYCN amplified type of neuroblastoma.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-63 AND
RP GLU-793.
RC TISSUE=Colon, Placenta, and Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 214-975 (ISOFORM 2), AND VARIANT GLU-793.
RC TISSUE=Bone, and Brain;
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 TISSUE SPECIFICITY.
RX PubMed=15952891; DOI=10.1146/annurev.biochem.74.082803.133347;
RA Inohara N., Chamaillard M., McDonald C., Nunez G.;
RT "NOD-LRR proteins: role in host-microbial interactions and inflammatory
RT disease.";
RL Annu. Rev. Biochem. 74:355-383(2005).
RN [7]
RP REVIEW.
RX PubMed=15771576; DOI=10.1146/annurev.immunol.23.021704.115616;
RA Ting J.P.-Y., Davis B.K.;
RT "CATERPILLER: a novel gene family important in immunity, cell death, and
RT diseases.";
RL Annu. Rev. Immunol. 23:387-414(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18219313; DOI=10.1038/sj.embor.7401161;
RA Tattoli I., Carneiro L.A., Jehanno M., Magalhaes J.G., Shu Y.,
RA Philpott D.J., Arnoult D., Girardin S.E.;
RT "NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and
RT JNK pathways by inducing reactive oxygen species production.";
RL EMBO Rep. 9:293-300(2008).
RN [9]
RP FUNCTION, INTERACTION WITH MAVS, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18200010; DOI=10.1038/nature06501;
RA Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E.,
RA Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z.,
RA Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y.;
RT "NLRX1 is a regulator of mitochondrial antiviral immunity.";
RL Nature 451:573-577(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TUFM.
RX PubMed=22749352; DOI=10.1016/j.immuni.2012.03.025;
RA Lei Y., Wen H., Yu Y., Taxman D.J., Zhang L., Widman D.G., Swanson K.V.,
RA Wen K.W., Damania B., Moore C.B., Giguere P.M., Siderovski D.P.,
RA Hiscott J., Razani B., Semenkovich C.F., Chen X., Ting J.P.;
RT "The mitochondrial proteins NLRX1 and TUFM form a complex that regulates
RT type I interferon and autophagy.";
RL Immunity 36:933-946(2012).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27393910; DOI=10.1016/j.molimm.2016.06.013;
RA Li H., Zhang S., Li F., Qin L.;
RT "NLRX1 attenuates apoptosis and inflammatory responses in myocardial
RT ischemia by inhibiting MAVS-dependent NLRP3 inflammasome activation.";
RL Mol. Immunol. 76:90-97(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 629-975, LRR REPEATS, AND
RP SUBUNIT.
RX PubMed=22386589; DOI=10.1016/j.immuni.2011.12.018;
RA Hong M., Yoon S.I., Wilson I.A.;
RT "Structure and functional characterization of the RNA-binding element of
RT the NLRX1 innate immune modulator.";
RL Immunity 36:337-347(2012).
RN [13]
RP INTERACTION WITH INFLUENZA A VIRUS PROTEIN PB1-F2 (MICROBIAL INFECTION).
RX PubMed=24799673; DOI=10.1073/pnas.1322118111;
RA Jaworska J., Coulombe F., Downey J., Tzelepis F., Shalaby K., Tattoli I.,
RA Berube J., Rousseau S., Martin J.G., Girardin S.E., McCullers J.A.,
RA Divangahi M.;
RT "NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage
RT antiviral immunity by interacting with influenza virus PB1-F2 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2110-E2119(2014).
CC -!- FUNCTION: Participates in antiviral signaling. Acts as a negative
CC regulator of MAVS-mediated antiviral responses, through the inhibition
CC of the virus-induced RLH (RIG-like helicase)-MAVS interaction
CC (PubMed:18200010). Instead, promotes autophagy by interacting with TUFM
CC and subsequently recruiting the autophagy-related proteins ATG5 and
CC ATG12 (PubMed:22749352). Regulates also MAVS-dependent NLRP3
CC inflammasome activation to attenuate apoptosis (PubMed:27393910). Has
CC no inhibitory function on NF-kappa-B signaling pathway, but enhances
CC NF-kappa-B and JUN N-terminal kinase dependent signaling through the
CC production of reactive oxygen species (PubMed:18219313).
CC {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313,
CC ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:27393910}.
CC -!- SUBUNIT: Homohexamer. Interacts with MAVS (PubMed:18200010). Interacts
CC with TUFM (PubMed:22749352). {ECO:0000269|PubMed:18200010,
CC ECO:0000269|PubMed:22386589, ECO:0000269|PubMed:22749352}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus protein
CC PB1-F2. {ECO:0000269|PubMed:24799673}.
CC -!- INTERACTION:
CC Q86UT6; P49411: TUFM; NbExp=2; IntAct=EBI-3893071, EBI-359097;
CC Q86UT6; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-3893071, EBI-6117196;
CC Q86UT6-1; Q7Z434-1: MAVS; NbExp=3; IntAct=EBI-15680006, EBI-15577799;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313,
CC ECO:0000269|PubMed:27393910}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UT6-2; Sequence=VSP_027158, VSP_027159;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strongest expression in
CC mammary gland, heart and muscle. Detected in HeLa, HEK293T, THP-1, HL-
CC 60, Raji and Jurkat cell lines (at protein level).
CC {ECO:0000269|PubMed:15952891, ECO:0000269|PubMed:18200010,
CC ECO:0000269|PubMed:18219313}.
CC -!- DOMAIN: The LRRCT domain mediates homodimerization and LRRNT mediates
CC trimerization of the dimers.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15075.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG51714.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51714.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY245437; AAP31240.1; -; mRNA.
DR EMBL; BK001111; DAA01244.1; -; mRNA.
DR EMBL; EF452237; ABO40480.1; -; mRNA.
DR EMBL; AB094095; BAC76049.1; -; mRNA.
DR EMBL; AK025131; BAB15075.1; ALT_INIT; mRNA.
DR EMBL; AK056454; BAG51714.1; ALT_SEQ; mRNA.
DR EMBL; AK095247; BAG53014.1; -; mRNA.
DR EMBL; AK291716; BAF84405.1; -; mRNA.
DR EMBL; BC013199; AAH13199.3; -; mRNA.
DR EMBL; BC110890; AAI10891.1; -; mRNA.
DR CCDS; CCDS8416.1; -. [Q86UT6-1]
DR RefSeq; NP_001269072.1; NM_001282143.1. [Q86UT6-1]
DR RefSeq; NP_001269073.1; NM_001282144.1. [Q86UT6-1]
DR RefSeq; NP_001269287.1; NM_001282358.1. [Q86UT6-1]
DR RefSeq; NP_078894.2; NM_024618.3. [Q86UT6-1]
DR RefSeq; XP_005271726.1; XM_005271669.1. [Q86UT6-1]
DR RefSeq; XP_006718967.1; XM_006718904.1. [Q86UT6-2]
DR RefSeq; XP_011541282.1; XM_011542980.1. [Q86UT6-1]
DR PDB; 3UN9; X-ray; 2.65 A; A/B/C=629-975.
DR PDBsum; 3UN9; -.
DR AlphaFoldDB; Q86UT6; -.
DR SMR; Q86UT6; -.
DR BioGRID; 122796; 81.
DR DIP; DIP-60637N; -.
DR IntAct; Q86UT6; 29.
DR STRING; 9606.ENSP00000387334; -.
DR iPTMnet; Q86UT6; -.
DR PhosphoSitePlus; Q86UT6; -.
DR BioMuta; NLRX1; -.
DR DMDM; 74759406; -.
DR EPD; Q86UT6; -.
DR jPOST; Q86UT6; -.
DR MassIVE; Q86UT6; -.
DR MaxQB; Q86UT6; -.
DR PaxDb; Q86UT6; -.
DR PeptideAtlas; Q86UT6; -.
DR PRIDE; Q86UT6; -.
DR ProteomicsDB; 69887; -. [Q86UT6-1]
DR ProteomicsDB; 69888; -. [Q86UT6-2]
DR Antibodypedia; 45879; 239 antibodies from 36 providers.
DR DNASU; 79671; -.
DR Ensembl; ENST00000292199.6; ENSP00000292199.2; ENSG00000160703.16. [Q86UT6-1]
DR Ensembl; ENST00000409109.6; ENSP00000387334.1; ENSG00000160703.16. [Q86UT6-1]
DR Ensembl; ENST00000409265.8; ENSP00000386858.5; ENSG00000160703.16. [Q86UT6-1]
DR Ensembl; ENST00000409991.5; ENSP00000386851.1; ENSG00000160703.16. [Q86UT6-1]
DR Ensembl; ENST00000525863.1; ENSP00000433442.1; ENSG00000160703.16. [Q86UT6-2]
DR GeneID; 79671; -.
DR KEGG; hsa:79671; -.
DR MANE-Select; ENST00000409109.6; ENSP00000387334.1; NM_001282144.2; NP_001269073.1.
DR UCSC; uc001pvu.5; human. [Q86UT6-1]
DR CTD; 79671; -.
DR DisGeNET; 79671; -.
DR GeneCards; NLRX1; -.
DR HGNC; HGNC:29890; NLRX1.
DR HPA; ENSG00000160703; Tissue enhanced (esophagus).
DR MIM; 611947; gene.
DR neXtProt; NX_Q86UT6; -.
DR OpenTargets; ENSG00000160703; -.
DR PharmGKB; PA162398052; -.
DR VEuPathDB; HostDB:ENSG00000160703; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000159493; -.
DR HOGENOM; CLU_016769_0_0_1; -.
DR InParanoid; Q86UT6; -.
DR OMA; NQPDCGC; -.
DR OrthoDB; 114368at2759; -.
DR PhylomeDB; Q86UT6; -.
DR TreeFam; TF331068; -.
DR PathwayCommons; Q86UT6; -.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR SignaLink; Q86UT6; -.
DR SIGNOR; Q86UT6; -.
DR BioGRID-ORCS; 79671; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; NLRX1; human.
DR GeneWiki; NLRX1; -.
DR GenomeRNAi; 79671; -.
DR Pharos; Q86UT6; Tbio.
DR PRO; PR:Q86UT6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86UT6; protein.
DR Bgee; ENSG00000160703; Expressed in lower esophagus mucosa and 186 other tissues.
DR ExpressionAtlas; Q86UT6; baseline and differential.
DR Genevisible; Q86UT6; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF05729; NACHT; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Host-virus interaction;
KW Immunity; Innate immunity; Leucine-rich repeat; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT CHAIN 87..975
FT /note="NLR family member X1"
FT /id="PRO_0000296190"
FT DOMAIN 160..483
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT DOMAIN 667..694
FT /note="LRRNT"
FT REPEAT 695..718
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 724..747
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 749..777
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 778..801
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 811..834
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 835..857
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 858..877
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:22386589"
FT REPEAT 878..899
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:22386589"
FT DOMAIN 906..970
FT /note="LRRCT"
FT REGION 75..556
FT /note="Required for interaction with MAVS"
FT /evidence="ECO:0000269|PubMed:18200010"
FT REGION 556..974
FT /note="Required for the repression of MAVS-induced
FT interferon signaling"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT VAR_SEQ 869..921
FT /note="HLYFNELSSEGRQVLRDLGGAAEGGARVVVSLTEGTAVSEYWSVILSEVQRN
FT L -> QGVAIQMCWKLPLLPYAHLWTPRMPSHWCFLLILMPPLPQWYDGLVAPRGRCT
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027158"
FT VAR_SEQ 922..975
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027159"
FT VARIANT 63
FT /note="P -> S (in dbSNP:rs643423)"
FT /evidence="ECO:0000269|PubMed:12766759,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_034614"
FT VARIANT 125
FT /note="R -> L (in dbSNP:rs3809045)"
FT /id="VAR_034615"
FT VARIANT 793
FT /note="A -> E (in dbSNP:rs4245191)"
FT /evidence="ECO:0000269|PubMed:12766759,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_034616"
FT VARIANT 843
FT /note="A -> S (in dbSNP:rs35500631)"
FT /id="VAR_034617"
FT CONFLICT 325
FT /note="R -> C (in Ref. 4; BAG53014)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="A -> T (in Ref. 4; BAG51714)"
FT /evidence="ECO:0000305"
FT HELIX 672..686
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 688..695
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 710..720
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 727..731
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 739..744
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 746..750
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 752..756
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 764..775
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 792..804
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 820..830
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 849..861
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 877..885
FT /evidence="ECO:0007829|PDB:3UN9"
FT STRAND 895..897
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 907..920
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 926..945
FT /evidence="ECO:0007829|PDB:3UN9"
FT HELIX 950..969
FT /evidence="ECO:0007829|PDB:3UN9"
SQ SEQUENCE 975 AA; 107616 MW; 25B6624FC13217FF CRC64;
MRWGHHLPRA SWGSGFRRAL QRPDDRIPFL IHWSWPLQGE RPFGPPRAFI RHHGSSVDSA
PPPGRHGRLF PSASATEAIQ RHRRNLAEWF SRLPREERQF GPTFALDTVH VDPVIRESTP
DELLRPPAEL ALEHQPPQAG LPPLALSQLF NPDACGRRVQ TVVLYGTVGT GKSTLVRKMV
LDWCYGRLPA FELLIPFSCE DLSSLGPAPA SLCQLVAQRY TPLKEVLPLM AAAGSHLLFV
LHGLEHLNLD FRLAGTGLCS DPEEPQEPAA IIVNLLRKYM LPQASILVTT RPSAIGRIPS
KYVGRYGEIC GFSDTNLQKL YFQLRLNQPY CGYAVGGSGV SATPAQRDHL VQMLSRNLEG
HHQIAAACFL PSYCWLVCAT LHFLHAPTPA GQTLTSIYTS FLRLNFSGET LDSTDPSNLS
LMAYAARTMG KLAYEGVSSR KTYFSEEDVC GCLEAGIRTE EEFQLLHIFR RDALRFFLAP
CVEPGRAGTF VFTVPAMQEY LAALYIVLGL RKTTLQKVGK EVAELVGRVG EDVSLVLGIM
AKLLPLRALP LLFNLIKVVP RVFGRMVGKS REAVAQAMVL EMFREEDYYN DDVLDQMGAS
ILGVEGPRRH PDEPPEDEVF ELFPMFMGGL LSAHNRAVLA QLGCPIKNLD ALENAQAIKK
KLGKLGRQVL PPSELLDHLF FHYEFQNQRF SAEVLSSLRQ LNLAGVRMTP VKCTVVAAVL
GSGRHALDEV NLASCQLDPA GLRTLLPVFL RARKLGLQLN SLGPEACKDL RDLLLHDQCQ
ITTLRLSNNP LTAAGVAVLM EGLAGNTSVT HLSLLHTGLG DEGLELLAAQ LDRNRQLQEL
NVAYNGAGDT AALALARAAR EHPSLELLHL YFNELSSEGR QVLRDLGGAA EGGARVVVSL
TEGTAVSEYW SVILSEVQRN LNSWDRARVQ RHLELLLRDL EDSRGATLNP WRKAQLLRVE
GEVRALLEQL GSSGS
