SARM1_DROME
ID SARM1_DROME Reviewed; 1360 AA.
AC Q6IDD9; Q0E8H1; Q7KUA2; Q8SY48; Q9VSD2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=NAD(+) hydrolase sarm1 {ECO:0000305};
DE Short=NADase sarm1 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000269|PubMed:28334607};
DE AltName: Full=Sterile alpha and TIR motif-containing protein 1 {ECO:0000303|PubMed:22678360};
DE AltName: Full=Tir-1 homolog;
GN Name=Sarm {ECO:0000303|PubMed:22678360, ECO:0000312|FlyBase:FBgn0262579};
GN Synonyms=Ect4 {ECO:0000303|PubMed:22022271};
GN ORFNames=CG43119 {ECO:0000312|FlyBase:FBgn0262579};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
RA Akhouayri I., Turc C., Royet J., Charroux B.;
RT "Toll-8/Tollo negatively regulates antimicrobial response in the Drosophila
RT respiratory epithelium.";
RL PLoS Pathog. 7:E1002319-E1002319(2011).
RN [6]
RP REVIEW.
RX PubMed=22837513; DOI=10.1126/science.1226150;
RA Yu X.M., Luo L.;
RT "Neuroscience. dSarm-ing axon degeneration.";
RL Science 337:418-419(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22678360; DOI=10.1126/science.1223899;
RA Osterloh J.M., Yang J., Rooney T.M., Fox A.N., Adalbert R., Powell E.H.,
RA Sheehan A.E., Avery M.A., Hackett R., Logan M.A., MacDonald J.M.,
RA Ziegenfuss J.S., Milde S., Hou Y.J., Nathan C., Ding A., Brown R.H. Jr.,
RA Conforti L., Coleman M., Tessier-Lavigne M., Zuechner S., Freeman M.R.;
RT "dSarm/Sarm1 is required for activation of an injury-induced axon death
RT pathway.";
RL Science 337:481-484(2012).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28334607; DOI=10.1016/j.neuron.2017.02.022;
RA Essuman K., Summers D.W., Sasaki Y., Mao X., DiAntonio A., Milbrandt J.;
RT "The SARM1 Toll/Interleukin-1 receptor domain possesses intrinsic NAD+
RT cleavage activity that promotes pathological axonal degeneration.";
RL Neuron 93:1334-1343(2017).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
CC -!- FUNCTION: NAD(+) hydrolase, which plays a key role in axonal
CC degeneration following injury by regulating NAD(+) metabolism
CC (PubMed:22678360, PubMed:28334607). Acts as a negative regulator of
CC MYD88- and TRIF-dependent toll-like receptor signaling pathway by
CC promoting Wallerian degeneration, an injury-induced form of programmed
CC subcellular death which involves degeneration of an axon distal to the
CC injury site (PubMed:22678360). Wallerian degeneration is triggered by
CC NAD(+) depletion: in response to injury, it is activated and catalyzes
CC cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and
CC nicotinamide; NAD(+) cleavage promoting axon destruction
CC (PubMed:22678360, PubMed:28334607, PubMed:31439792). Involved in the
CC down-regulation of the tracheal immune response to Gram-negative
CC bacteria (PubMed:22022271). This is likely by mediating Tollo signaling
CC in the tracheal epithelium (PubMed:22022271).
CC {ECO:0000269|PubMed:22022271, ECO:0000269|PubMed:22678360,
CC ECO:0000269|PubMed:28334607, ECO:0000269|PubMed:31439792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000269|PubMed:28334607, ECO:0000269|PubMed:31439792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:28334607, ECO:0000269|PubMed:31439792};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) = cyclic ADP-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:73672;
CC Evidence={ECO:0000269|PubMed:28334607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612;
CC Evidence={ECO:0000269|PubMed:28334607};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6PDS3}. Cell
CC projection, axon {ECO:0000269|PubMed:22678360}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C;
CC IsoId=Q6IDD9-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q6IDD9-2; Sequence=VSP_013615, VSP_013616, VSP_013617;
CC -!- TISSUE SPECIFICITY: Widely expressed in larval brains and adult brains.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000250|UniProtKB:Q6SZW1}.
CC -!- DISRUPTION PHENOTYPE: Severed axons in wild-type flies disappear
CC completely within a week of injury, whereas axons of neurons homozygous
CC for any one of the three loss-of-function alleles: l(3)896, l(3)4621,
CC and l(3)4705 persist for several weeks after severing
CC (PubMed:22678360). After infection with Gram-negative bacteria, the
CC respiratory epithelium displays an over-active immune response with a
CC greater increase in expression of Drs compared to wild-type larvae
CC (PubMed:22022271). {ECO:0000269|PubMed:22022271,
CC ECO:0000269|PubMed:22678360}.
CC -!- SIMILARITY: Belongs to the SARM1 family. {ECO:0000305}.
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DR EMBL; AE014296; AAN12011.1; -; Genomic_DNA.
DR EMBL; AE014296; ABI31243.1; -; Genomic_DNA.
DR EMBL; AY075346; AAL68207.1; -; mRNA.
DR EMBL; BT014666; AAT27290.1; -; mRNA.
DR RefSeq; NP_001036594.1; NM_001043129.3. [Q6IDD9-1]
DR RefSeq; NP_729327.1; NM_168254.2. [Q6IDD9-2]
DR PDB; 7LCY; X-ray; 3.35 A; A/B/C=314-678.
DR PDB; 7LCZ; X-ray; 1.65 A; A/B=370-678.
DR PDB; 7M6K; X-ray; 1.69 A; A/B=369-678.
DR PDB; 7RTC; X-ray; 3.31 A; A/B/C=315-678.
DR PDBsum; 7LCY; -.
DR PDBsum; 7LCZ; -.
DR PDBsum; 7M6K; -.
DR PDBsum; 7RTC; -.
DR AlphaFoldDB; Q6IDD9; -.
DR SMR; Q6IDD9; -.
DR BioGRID; 64320; 16.
DR STRING; 7227.FBpp0293535; -.
DR PaxDb; Q6IDD9; -.
DR PRIDE; Q6IDD9; -.
DR DNASU; 38895; -.
DR EnsemblMetazoa; FBtr0304994; FBpp0293531; FBgn0262579. [Q6IDD9-2]
DR EnsemblMetazoa; FBtr0304995; FBpp0293532; FBgn0262579. [Q6IDD9-1]
DR GeneID; 38895; -.
DR KEGG; dme:Dmel_CG43119; -.
DR UCSC; CG34373-RE; d. melanogaster. [Q6IDD9-1]
DR CTD; 38895; -.
DR FlyBase; FBgn0262579; Sarm.
DR VEuPathDB; VectorBase:FBgn0262579; -.
DR eggNOG; KOG3678; Eukaryota.
DR GeneTree; ENSGT00390000004155; -.
DR HOGENOM; CLU_003286_1_1_1; -.
DR InParanoid; Q6IDD9; -.
DR PhylomeDB; Q6IDD9; -.
DR BioGRID-ORCS; 38895; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38895; -.
DR PRO; PR:Q6IDD9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262579; Expressed in adult hindgut (Drosophila) and 73 other tissues.
DR ExpressionAtlas; Q6IDD9; baseline and differential.
DR Genevisible; Q6IDD9; DM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:1901214; P:regulation of neuron death; IMP:FlyBase.
DR GO; GO:0048678; P:response to axon injury; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR039184; SARM1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR22998; PTHR22998; 1.
DR Pfam; PF07647; SAM_2; 2.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; Hydrolase;
KW Immunity; Innate immunity; NAD; Reference proteome; Repeat.
FT CHAIN 1..1360
FT /note="NAD(+) hydrolase sarm1"
FT /id="PRO_0000097588"
FT DOMAIN 690..754
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 760..828
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 837..981
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 919
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 846..847
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 876
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT VAR_SEQ 1..215
FT /note="MKAAEIKRDLTNIQKSMSEINDLAKERITGGPGSISTTSASAITAPSTMSQT
FT TTSRLAPKLTSAHPSIDDLRGLSRQDKITQLQKKIRASFENLVDHDDSNVIVTLPDDDD
FT CPHNHFGSGLNLTHPTAAQLSASGLSGSSKTIDTIKFQEKSMKTESKTKVVTDGFSSEQ
FT ATSNSAEMKRLQAGDIDYQESKGASAMRNRLEVDGVKTEENAAVI -> MSNQAPWPVR
FT KGIFRSSGQSDFTPTRSPSPIVEMPLSPPPVATPSNRFGINSPLSPPPQPIQVVAGSTT
FT ATTMSTASAARVSGAAASTSSSSSSSSSSQCSSQTSSSSSSHTRVRKSSNPPPQPITSC
FT PLSPPPPPPPQQQQQLPQQLPPPTPINNTNHSAITTPNHNNNHNCNQMRNVREIPIEVE
FT QS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_013615"
FT VAR_SEQ 1048..1078
FT /note="ANHQANRYRQSPSPARQRGSTSQLSGYSRAP -> GGPTSTTSTTSSTPNSN
FT SSSSSNQSPPAAPA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_013616"
FT VAR_SEQ 1079..1360
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_013617"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:7RTC"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:7LCZ"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 391..404
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:7LCZ"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:7LCZ"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:7LCY"
FT HELIX 461..474
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 503..519
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 522..530
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 563..572
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 578..584
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 603..609
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 610..614
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 618..638
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 642..646
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 650..657
FT /evidence="ECO:0007829|PDB:7LCZ"
FT HELIX 662..675
FT /evidence="ECO:0007829|PDB:7LCZ"
SQ SEQUENCE 1360 AA; 147884 MW; F3838F5AF4FE934D CRC64;
MKAAEIKRDL TNIQKSMSEI NDLAKERITG GPGSISTTSA SAITAPSTMS QTTTSRLAPK
LTSAHPSIDD LRGLSRQDKI TQLQKKIRAS FENLVDHDDS NVIVTLPDDD DCPHNHFGSG
LNLTHPTAAQ LSASGLSGSS KTIDTIKFQE KSMKTESKTK VVTDGFSSEQ ATSNSAEMKR
LQAGDIDYQE SKGASAMRNR LEVDGVKTEE NAAVIKEALS LRTGDITQQA SNNVAASSIT
VQSENFSADK KAISQSQQSQ TMTSNGIISQ EKHVSSASQA NYSMSHKGVS STGSSMITSS
SQMSAMNGQM LKLADLKLDD LKSLTAGSGQ QEIEQTINKY SNMLTSIVSS LQEDERGGSA
ITVHDVGGKK SQYLEKINEV IRRAWAVPTH GHELGYSLCN SLRQSGGLDL LMKNCVKPDL
QFSSAQLLEQ CLTTENRKHV VDNGLDKVVN VACVCTKNSN MEHSRVGTGI LEHLFKHSEG
TCSDVIRLGG LDAVLFECRT SDLETLRHCA SALANLSLYG GAENQEEMIL RKVPMWLFPL
AFHNDDNIKY YACLAIAVLV ANKEIEAEVL KSGCLDLVEP FVTSHDPSAF ARSNLAHAHG
QSKHWLKRLV PVLSSNREEA RNLAAFHFCM EAGIKREQGN TDIFREINAI EALKNVASCP
NAIASKFAAQ ALRLIGETVP HKLSQQVPLW SVEDVQEWVK QIGFNDYIDK FNESQVDGDL
LLKLNQDNLR ADIGIGNGIL LKRFERELQN LKRMADYSSK DTAKMHQFLS EIGTDYCTYT
YAMLNAGIDK CALPHVNEDM LMTECGIHNS IHRLRILNAV KNLENSLPSS SEENMAKTLD
VFVSYRRSNG SQLASLLKVH LQLRGFSVFI DVERLEAGKF DNGLLNSIRQ AKNFVLVLTP
DALHRCINDE DCKDWVHREI VAALNSNCNI IPIIDQQFDW PEVERLPEDM RSVAHFNGVN
WIHDYQDACI DKLERFLRGE KNIDRIAAMV PGTPGSVSYQ RMHSNDSDYQ SGGAGAGSGA
GTGGGGGGGV TGSVVDGLMV AANGSGQANH QANRYRQSPS PARQRGSTSQ LSGYSRAPSK
RSQILTPYRT QQAALLHKTG AGSASMQNMM PLAYLPPRRS SAAGLGHGSG SGMGSGYRSH
SVDGLLDQAG STPEQRIAAA AAKVTAGSTA LTNASSTSTL QPEEEVTDAA LNDSVTRRDK
HTLSPPGNVQ QHRKSRSLDH ILSKQTLAEL LPPSSELADG TQSMQNLAIP MTPQPQRRDT
SSSSKSPTPE RPPQPAMERV RERQSPEGVS ATESEREDQP EECLRHGNQQ RASASVHRGA
SLTSNKTSNS SLGSNFSAGG NNKTIFNRTM KKVRSLIKKP
