TMP2L_NEMVE
ID TMP2L_NEMVE Reviewed; 1551 AA.
AC A7T1N0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Transient receptor potential cation channel subfamily M member-like 2 {ECO:0000305|PubMed:25620041};
DE Short=nvTRPM2 {ECO:0000303|PubMed:25620041};
GN Name=TRPM2 {ECO:0000303|PubMed:25620041};
GN ORFNames=v1g248535 {ECO:0000312|EMBL:EDO30135.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000312|Proteomes:UP000001593};
RN [1] {ECO:0000312|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000312|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
RN [2] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF 1037-GLU--PHE-1039;
RP GLN-1438 AND 1449-MET--ALA-1463.
RX PubMed=25620041; DOI=10.1038/srep08032;
RA Kuehn F.J., Kuehn C., Lueckhoff A.;
RT "Functional characterisation of a TRPM2 orthologue from the sea anemone
RT Nematostella vectensis in human cells.";
RL Sci. Rep. 5:8032-8032(2015).
RN [3] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF ASN-1365 AND 1442-ALA--GLU-1446.
RX PubMed=27333281; DOI=10.1371/journal.pone.0158060;
RA Kuehn F.J., Kuehn C., Winking M., Hoffmann D.C., Lueckhoff A.;
RT "ADP-Ribose Activates the TRPM2 Channel from the Sea Anemone Nematostella
RT vectensis Independently of the NUDT9H Domain.";
RL PLoS ONE 11:E0158060-E0158060(2016).
RN [4] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-908 AND 1037-GLU--PHE-1039.
RX PubMed=28775320; DOI=10.1038/s41598-017-07652-4;
RA Kuehn F.J.P., Mathis W., Cornelia K., Hoffmann D.C., Lueckhoff A.;
RT "Modulation of activation and inactivation by Ca2+ and 2-APB in the pore of
RT an archetypal TRPM channel from Nematostella vectensis.";
RL Sci. Rep. 7:7245-7245(2017).
RN [5] {ECO:0007744|PDB:6CO7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.07 ANGSTROMS) IN COMPLEX WITH CALCIUM,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, MOTIF, COILED
RP COIL, GLYCOSYLATION AT ASN-1017, AND MUTAGENESIS OF GLN-896; ASN-918;
RP ASP-921; 1040-LEU--GLU-1042; LYS-1047 AND GLU-1110.
RX PubMed=29745897; DOI=10.7554/elife.36409;
RA Zhang Z., Toth B., Szollosi A., Chen J., Csanady L.;
RT "Structure of a TRPM2 channel in complex with Ca2+ explains unique gating
RT regulation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Nonselective, voltage-independent cation channel that
CC mediates Ca(2+) and to a lesser extent Na(+) influx, leading to
CC increased cytoplasmic Ca(2+) levels (PubMed:25620041, PubMed:27333281,
CC PubMed:28775320, PubMed:29745897). Functions as ligand-gated ion
CC channel (PubMed:25620041, PubMed:27333281, PubMed:28775320,
CC PubMed:29745897). Binding of ADP-ribose causes a conformation change;
CC the channel is primed but still requires Ca(2+) binding to trigger
CC channel opening (PubMed:25620041, PubMed:27333281, PubMed:28775320,
CC PubMed:29745897). May have ADP-ribose pyrophosphatase activity which
CC reduces ADP-ribose levels induced by oxidative stress, thus preventing
CC the channel activation by reactive oxygen species (PubMed:25620041,
CC PubMed:27333281). {ECO:0000269|PubMed:25620041,
CC ECO:0000269|PubMed:27333281, ECO:0000269|PubMed:28775320,
CC ECO:0000269|PubMed:29745897}.
CC -!- ACTIVITY REGULATION: Activated by phosphatidylinositol 4,5-bisphosphate
CC (PIP2) (PubMed:29745897). Although PIP2 is essential for the channel
CC activation, its contribution to the level of channel activity is
CC minimal (PubMed:29745897). Also activated by diphosphate ribose-2'-
CC phosphate (PubMed:27333281). Upon binding to ADPR, channel activation
CC requires only a short initial cytosolic Ca(2+) increase, then the
CC activation is sustained by the uptake of extracellular Ca(2+)
CC (PubMed:29745897, PubMed:25620041). Activated by 2-aminoethyl
CC diphenylborinate (2-APB) in a Ca(2+)-dependent manner
CC (PubMed:28775320). 2-APB prevents the inactivation of the channel
CC (PubMed:28775320). {ECO:0000269|PubMed:25620041,
CC ECO:0000269|PubMed:27333281, ECO:0000269|PubMed:28775320,
CC ECO:0000269|PubMed:29745897}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29745897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27333281,
CC ECO:0000305|PubMed:28775320}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29745897}.
CC -!- DOMAIN: The Nudix hydrolase domain is dispensable for ADP-ribose-
CC dependent channel activation. May be involved in the regulation of ADP-
CC ribose intracellular levels. Essential to prevent response to oxidative
CC stress. {ECO:0000269|PubMed:27333281}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM2 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Unlike in human TRPM2, residues in the Nudix box (AEFGE) that
CC are important for ADP-ribose pyrophosphatase activity are conserved
CC suggesting that N.vectensis TRPM2 may have ADP-ribose pyrophosphatase
CC activity. {ECO:0000305|PubMed:27333281}.
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DR EMBL; DS470128; EDO30135.1; -; Genomic_DNA.
DR RefSeq; XP_001622235.1; XM_001622185.1.
DR PDB; 6CO7; EM; 3.07 A; A/B/C/D=1-1551.
DR PDBsum; 6CO7; -.
DR AlphaFoldDB; A7T1N0; -.
DR SMR; A7T1N0; -.
DR STRING; 45351.EDO30135; -.
DR iPTMnet; A7T1N0; -.
DR EnsemblMetazoa; EDO30135; EDO30135; NEMVEDRAFT_v1g248535.
DR GeneID; 5500864; -.
DR KEGG; nve:5500864; -.
DR eggNOG; KOG3614; Eukaryota.
DR eggNOG; KOG4195; Eukaryota.
DR HOGENOM; CLU_001390_0_3_1; -.
DR InParanoid; A7T1N0; -.
DR OMA; WMENSIA; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; A7T1N0; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IMP:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR041491; TRPM_SLOG.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Coiled coil; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1551
FT /note="Transient receptor potential cation channel
FT subfamily M member-like 2"
FT /id="PRO_0000446910"
FT TOPO_DOM 1..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 715..730
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 731..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 859..877
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 878..898
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 899..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 938..947
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 969..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 1002..1018
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1019..1034
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 1035..1059
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29745897"
FT TOPO_DOM 1081..1116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 1117..1135
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 1136..1551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 1394..1546
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 744..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1184..1209
FT /evidence="ECO:0000269|PubMed:29745897"
FT MOTIF 1035..1037
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:29745897"
FT MOTIF 1040..1042
FT /note="Prevents fast channel inactivation"
FT /evidence="ECO:0000269|PubMed:29745897"
FT MOTIF 1428..1449
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 893
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:29745897,
FT ECO:0007744|PDB:6CO7"
FT BINDING 896
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:29745897,
FT ECO:0007744|PDB:6CO7"
FT BINDING 918
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:29745897,
FT ECO:0007744|PDB:6CO7"
FT BINDING 921
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:29745897,
FT ECO:0007744|PDB:6CO7"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29745897,
FT ECO:0007744|PDB:6CO7"
FT MUTAGEN 896
FT /note="Q->A: Severe loss of Ca(2+) sensitivity and
FT increased sensitivity to phosphatidylinositol 4,5-
FT bisphosphate-mediated activation."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 908
FT /note="K->N: Severe reduction in ADP-ribose-mediated
FT channel activation."
FT /evidence="ECO:0000269|PubMed:28775320"
FT MUTAGEN 918
FT /note="N->A: Severe loss of Ca(2+) sensitivity and
FT increased sensitivity to phosphatidylinositol 4,5-
FT bisphosphate-mediated activation."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 921
FT /note="D->A: Severe loss of Ca(2+) sensitivity and
FT increased sensitivity to phosphatidylinositol 4,5-
FT bisphosphate-mediated activation."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 1037..1039
FT /note="ELF->QLP: Mild decrease in channel activation."
FT /evidence="ECO:0000269|PubMed:25620041,
FT ECO:0000269|PubMed:28775320"
FT MUTAGEN 1040..1042
FT /note="LDE->GY: Induces fast inactivation of the channel."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 1047
FT /note="K->A,E: Does not affect channel activity."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 1110
FT /note="E->A: Mild loss of Ca(2+) sensitivity and increased
FT sensitivity to phosphatidylinositol 4,5-bisphosphate-
FT mediated activation."
FT /evidence="ECO:0000269|PubMed:29745897"
FT MUTAGEN 1149..1463
FT /note="Missing: Induces transient spontaneous channel
FT activity. Does not affect channel activity by ADP-ribose.
FT Acquires sensitivity to oxidative stress. In response to
FT oxidative stress, induces intracellular Ca(2+) oscillations
FT instead of a sustained Ca(2+) increase."
FT /evidence="ECO:0000269|PubMed:25620041"
FT MUTAGEN 1365
FT /note="N->D: Does not affect channel activity. Acquires
FT sensitivity to oxidative stress."
FT /evidence="ECO:0000269|PubMed:27333281"
FT MUTAGEN 1438
FT /note="Q->R: Does not affect channel activity by ADP-
FT ribose. Acquires sensitivity to oxidative stress."
FT /evidence="ECO:0000269|PubMed:25620041"
FT MUTAGEN 1442..1446
FT /note="AEFGE->RILRQ: Does not affect channel activity by
FT ADP-ribose. Acquires sensitivity to oxidative stress."
FT /evidence="ECO:0000269|PubMed:27333281"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 466..473
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 501..510
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 519..528
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 579..589
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 593..601
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 606..626
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 634..658
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 660..667
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 672..676
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 679..685
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 695..705
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 715..723
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 725..730
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 735..749
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 814..819
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 828..835
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 837..860
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 871..873
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 877..898
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 901..904
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 905..912
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 917..935
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 940..959
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 962..965
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 971..1007
FT /evidence="ECO:0007829|PDB:6CO7"
FT STRAND 1010..1014
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1019..1034
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1040..1043
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 1048..1051
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1058..1074
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1077..1113
FT /evidence="ECO:0007829|PDB:6CO7"
FT TURN 1119..1121
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1122..1135
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1155..1181
FT /evidence="ECO:0007829|PDB:6CO7"
FT HELIX 1184..1209
FT /evidence="ECO:0007829|PDB:6CO7"
SQ SEQUENCE 1551 AA; 175439 MW; 31E4B2755128372C CRC64;
MGKDSFTPLY DGGDSSHVHL NKFGSNQLSQ SKKSWIARNF SRRECIRFVP KSHDVSRCKC
GRPRERHSQQ ALESGQGSEE WNVASCTTKH PTNAYGEIDF EGYGGQKRAP YLRMSHDTDA
NLVITLMLKR WNLEIPNLVI SVTGGAKSFV LKPRLREMFR RGLIKAAKTT GAWIITGGTN
TGVMKHVGEA VKEQQLMFGS DTQVNVIGIA TWGIVDKQSD LISEKNGKYP ALYSMEPTPG
HQGAMLDPNH SHFFLVDDGT EGKYGVEIGM RSRIEEAIMK VKTDSRSEAG SIGVPVVLLV
LEGGPNTVAT MYELIKKKVP AVVIDGSGRA ASVVGFAYNH TIKRNVDGQT INVIDPQYED
EVRAKVVEVF GAKGADKTYS MIKDVLEDEK MISVYSLDGE ISQDIDLAIL KALLKANRSS
PVAQLNLALA WNRIDLAKSD IFTEEQQWTT ETLSAAMLTA LLDDKAEFAE LFLQNGLSMR
EFLSLDILCK LYAEVPGNTT IKPLLQKEMG KRQVKTIDMD VVGEVIEELM GDMFESYYRK
DGHYFGELAS YAEGLVLKNR KSSKDLLANI NRIDPLPTPY LDVFLWAVLC NRRELARVLW
EAGREPMAAA LMASRLLKRM ASRAQEDNTI TDISSDLYDH ARLFEERAVG VLDECFNENE
TLSQTLLVRE LDHYSRMTAL ELAVSAESQD FIAHTSCQVL LTRLWMGTMA MNTRWWKVLV
CLYLPVLIFP IIYFVPDEQH ERQAAEREHQ KSLNQKSSKV KSHKEKNDAP VVPVYRSKEE
KAVSNDEEAR VGTENEEEDF QLEDYIPEIR EDDSMEVIMR NKKLGFCDRI MHFYSAPFSK
FVGNVVGYLA FIFLYAYVVL FNFPRFDPAK TLGGIHPTEI VLYFWVFTIL IEEIRQLAAK
PPKYIKDKVS VYFSDTWNFV DIFSLTVFII AIILRFFTNS RIFTASRIIL SLDIIFFIVR
SLQIFSVNRL LGPKLVMIQK MMQDLAQFII ILAVFTIAYG IALHAVMFPS PGIYARNNTW
VTITSVVQYP YWQMYGELFL DEIQGEKPKE FGEVDPDGRW LSPLLLAIYM VFTNILLLNL
LIAIFNYTFE RVQEDSDKVW KFQRYDLVQE YHSRPVFAPP LVLLGHILIF IRWVWRMCRC
GHPPRGSTMK IGLSPAEMEQ MDNWEFQAAE MYIHQQQQKN SGTLEERVRA LGDRVDCINS
QLNRVLDSMS GTRAHALTDG NGLEGGHDSE GRLARMEVEL SSNSESLQKI LALLQQQPPV
KGQAAVPIQL TLLHYKARSS PYPGSTAKRF AVQDNMVDWQ VPFPDYKPVN YTAPVVLANP
VWADKDLMAM SPRPELPYNQ MDHTCNVNRV SYNGTYVVKD GLPLNPMGRT GMQGRGLLGR
FGPNHAADPV VTRWKRTSAG VMLQGGKKVL EFVAIQRKDN NQWAIPGGMV EPGQLVTQAL
KAEFGEEAMA KLNVSQEEKE RIAKQIERLF QQGQEIYKGY VDDPRNTDNA WMETVAVNFH
DDKGDLFGDI TLQAGDDAAA VRWQRVSGNI PLYASHVSIL EKVAKMRDAA F
