TRPM2_DANRE
ID TRPM2_DANRE Reviewed; 1470 AA.
AC A0A0R4IMY7; A0A0R4IF00;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 2;
GN Name=trpm2 {ECO:0000312|ZFIN:ZDB-GENE-061214-4};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF APOPROTEIN AND IN
RP COMPLEX WITH ADP-RIBOSE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
RP AND MUTAGENESIS OF LYS-150; TYR-267; GLU-270; ARG-274; ARG-330 AND
RP 1157-GLU--PHE-1470.
RX PubMed=30250252; DOI=10.1038/s41586-018-0558-4;
RA Huang Y., Winkler P.A., Sun W., Lue W., Du J.;
RT "Architecture of the TRPM2 channel and its activation mechanism by ADP-
RT ribose and calcium.";
RL Nature 562:145-149(2018).
RN [3]
RP DOMAIN.
RX PubMed=30467180; DOI=10.1126/science.aav4809;
RA Wang L., Fu T.M., Zhou Y., Xia S., Greka A., Wu H.;
RT "Structures and gating mechanism of human TRPM2.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Nonselective, voltage-independent cation channel that
CC mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels.
CC Functions as ligand-gated ion channel. Binding of ADP-ribose to the
CC cytoplasmic N-terminal region causes a conformation change; the channel
CC is primed but still requires Ca(2+) binding to trigger channel opening.
CC {ECO:0000269|PubMed:30250252}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:30250252}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30250252};
CC Multi-pass membrane protein {ECO:0000269|PubMed:30250252}.
CC -!- DOMAIN: Binds ADP-ribose via the N-terminal cytoplasmic region
CC (PubMed:30250252). Other family members contain a C-terminal Nudix
CC hydrolase domain that binds ADP-ribose and is important for channel
CC gating. In zebrafish, the corresponding region is highly divergent and
CC has only low affinity for ADP-ribose (PubMed:30467180). Still, the
CC region is required for channel activity (PubMed:30250252).
CC {ECO:0000269|PubMed:30250252, ECO:0000269|PubMed:30467180}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM2 sub-subfamily. {ECO:0000305}.
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DR EMBL; CR753902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU855885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FQ311915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FQ377657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6DRJ; EM; 3.30 A; A/B/C/D=1-1470.
DR PDB; 6DRK; EM; 3.80 A; A/B/C/D=1-1470.
DR PDB; 6PKV; EM; 4.30 A; A/B/C/D=32-1470.
DR PDB; 6PKW; EM; 4.50 A; A/B/C/D=32-1470.
DR PDB; 6PKX; EM; 4.20 A; A/B/C/D=32-1470.
DR PDB; 7AOV; X-ray; 2.00 A; A/B=33-415.
DR PDBsum; 6DRJ; -.
DR PDBsum; 6DRK; -.
DR PDBsum; 6PKV; -.
DR PDBsum; 6PKW; -.
DR PDBsum; 6PKX; -.
DR PDBsum; 7AOV; -.
DR AlphaFoldDB; A0A0R4IMY7; -.
DR SMR; A0A0R4IMY7; -.
DR Ensembl; ENSDART00000166906; ENSDARP00000136274; ENSDARG00000101641.
DR ZFIN; ZDB-GENE-061214-4; trpm2.
DR GeneTree; ENSGT00940000156404; -.
DR Reactome; R-DRE-3295583; TRP channels.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR PRO; PR:A0A0R4IMY7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000101641; Expressed in granulocyte and 26 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0072570; F:ADP-D-ribose binding; IDA:ZFIN.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; IDA:ZFIN.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0072571; F:mono-ADP-D-ribose binding; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR029594; TRPM2.
DR InterPro; IPR041491; TRPM_SLOG.
DR PANTHER; PTHR13800:SF2; PTHR13800:SF2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1470
FT /note="Transient receptor potential cation channel
FT subfamily M member 2"
FT /id="PRO_0000446372"
FT TOPO_DOM 1..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 726..738
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 739..808
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 830..836
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 858..876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 898..905
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 927..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 942..968
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 969..977
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 978..1002
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 1003..1034
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1035..1059
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 1060..1087
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 1088..1105
FT /evidence="ECO:0000269|PubMed:30250252"
FT TOPO_DOM 1106..1470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1157..1470
FT /note="Divergent Nudix hydrolase-like domain"
FT /evidence="ECO:0000305|PubMed:30250252"
FT REGION 1215..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 991..993
FT /note="Selectivity filter"
FT /evidence="ECO:0000305|PubMed:30250252"
FT COMPBIAS 1224..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 274
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 305..308
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 330
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 853
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 856
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 879
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:30250252"
FT BINDING 1084
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:30250252"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 1008..1020
FT /evidence="ECO:0000269|PubMed:30250252,
FT ECO:0007744|PDB:6DRJ"
FT MUTAGEN 150
FT /note="K->A: No significant effect on channel activity."
FT /evidence="ECO:0000269|PubMed:30250252"
FT MUTAGEN 267
FT /note="Y->A: Decreased channel activity."
FT /evidence="ECO:0000269|PubMed:30250252"
FT MUTAGEN 270
FT /note="E->A: Decreased channel activity."
FT /evidence="ECO:0000269|PubMed:30250252"
FT MUTAGEN 274
FT /note="R->A: Decreased channel activity. Loss of channel
FT activity; when associated with A-330."
FT /evidence="ECO:0000269|PubMed:30250252"
FT MUTAGEN 330
FT /note="R->A: Decreased channel activity. Loss of channel
FT activity; when associated with A-274."
FT /evidence="ECO:0000269|PubMed:30250252"
FT MUTAGEN 1157..1470
FT /note="Missing: Loss of channel activity."
FT /evidence="ECO:0000269|PubMed:30250252"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 469..477
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 491..497
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 503..511
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 532..543
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 591..599
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 607..611
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 619..633
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 639..643
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 644..667
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 677..680
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 688..694
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 704..715
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 724..732
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 734..738
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 739..741
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 745..757
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 759..761
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 796..802
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 805..828
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 838..858
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 866..873
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 878..895
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 901..926
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 933..967
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 975..982
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 984..989
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 994..997
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1033..1048
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1050..1067
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1073..1087
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1096..1109
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1114..1116
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1118..1120
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1126..1152
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1155..1174
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1271..1274
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1316..1333
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1338..1346
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 1347..1349
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1351..1353
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1365..1373
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1379..1383
FT /evidence="ECO:0007829|PDB:6DRJ"
FT TURN 1384..1386
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1391..1396
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1403..1415
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1424..1428
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1434..1444
FT /evidence="ECO:0007829|PDB:6DRJ"
FT STRAND 1449..1451
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1453..1466
FT /evidence="ECO:0007829|PDB:6DRJ"
FT HELIX 1467..1469
FT /evidence="ECO:0007829|PDB:6DRJ"
SQ SEQUENCE 1470 AA; 167987 MW; 96E3253B800F205B CRC64;
MDEAALEPTL VQTLAVSTAK GGRYLSLSPS FQRCSLASWI KENIKKKECC FYVEDGREGI
CKCGYPKVQH CDEAIKPEDY MGEQWDKHRH VRETPTDAFG DISFGGLGQK TGKYVRVSSD
TSCENLYQLM TEQWKLRSPN LLISVTGGAK NFYIKTHLKD KFRRGLIKVA QTTGAWILTG
GTHAGVMKHV GMAVRDYTLS SGSMEGQIVV IGVAPWGVIH NRSTLIHPEG RFPAYYSLDE
QGQGRLSCLD INHTHFLLVD DGTQGHYGVE IELRARLEKL ISKLSLGNRE SGVTIPVVCV
VLDGGPGTLN TIYNSMLNHT PCVVLEGSGR LADVIAHVAS VPVSKVTMAL INRLLKRFFM
QEYKNFTELQ IIEWTKKIQD ILRMPHLLTV FRIDEDKNYD VDVAILQALL KASRSDEHAG
RHCWERQLEL AVAWNRVDIA ESEIFTEESQ WTSSDLHPAM FSALVGDKPE FVRLLLENGV
CVREFLEREE TLCELYSHLP SCFFLRKLAK RVQGGKMRRG QEPLPGSRKV CLSHVSEEVR
HLLGSFTQPL YIASRYKPTK DDVRLKVPSK GALDLPCSGE EWSADTVWDP GRDLFLWAVV
QNNRELAEIG WEQCRDCIAA ALAASKILRK LAQESGEDDS EEATEMLELA NHYEKQAIGV
FSECHSWDAQ RAQKLLIRIS PSWGRSTCLW LALEAHDKSF IAHSGVQALL TQIWCGELSV
DNPHWKVLLC MIFFPLIYTG FLTFRRDEDI QRQAERTEQQ KLAMESVFAG QSDGKIKRHL
RGFSQKSELK PLNCSSRLMS FLKSPQVKFY WNIASYFGFL WLFAVVLMID FQTSPSWREL
LLYVWLTSLV CEEIRQLYHD FDGSGFRRKA KMYIKDLWNI LDVLSIVLFI AGLICRLQAS
DTVFYIGKVI LCIDFIIFCL RLMAIFSISR TLGPKIIIVR RMMLDLFFFM FLLSIWVVAY
GVAKQGILIE NEERLNWIIR GAVYEPYITI FGNFPTNIDN TLFDISSCSV NASDPLKPKC
PMLNADNTPV FPEWLTIMML CVYLLFANIL LLNLLIAIFN YTFQEVQDNT DTIWKFQRYE
LIKEYHSRPA LPPPFILLSH LILFIRGVFL RDLPQRHKNF RQELEQTEEE ELLSWEAYMK
DNYLASTRQD ESQSVEHRIH DTAEKVGAMS ELLEREQEMV SATMAKRLAR LEEQVSESAK
ALRWIIDALK SQGCKSKVQP PLMRSKSSDR DDGDSSGQET DDEEAPHMFA RQLQYPDSTV
RRFPVPEEKV SWEVNFSPYQ PPVYNQQDSS ESDTSALDKH RNPGGRTGIR GKGALNTLGP
NHILHPIFTR WRDAEHKVLE FLAVWEDAEK RWALLGGPAQ PDEPLAQVLE RILGKKLNEK
TKTLLKAGEE VYKGYVDDSR NTDNAWVETS IITLHCDKNT PLMADLNHMV ESSLSSHQPL
QWREVSSDAC RCSYQREALR QIAHHHNTYF
