TRPM2_RAT
ID TRPM2_RAT Reviewed; 1507 AA.
AC E9PTA2; Q2PH54; Q5G856;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 2;
GN Name=Trpm2 {ECO:0000312|RGD:1311889};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:BAE72117.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16651700; DOI=10.1254/jphs.fp0060128;
RA Kaneko S., Kawakami S., Hara Y., Wakamori M., Itoh E., Minami T.,
RA Takada Y., Kume T., Katsuki H., Mori Y., Akaike A.;
RT "A critical role of TRPM2 in neuronal cell death by hydrogen peroxide.";
RL J. Pharmacol. Sci. 101:66-76(2006).
RN [2] {ECO:0000312|EMBL:AAW65801.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16260005; DOI=10.1016/j.neuropharm.2005.08.021;
RA Hill K., Tigue N.J., Kelsell R.E., Benham C.D., McNulty S., Schaefer M.,
RA Randall A.D.;
RT "Characterisation of recombinant rat TRPM2 and a TRPM2-like conductance in
RT cultured rat striatal neurones.";
RL Neuropharmacology 50:89-97(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11804595; DOI=10.1016/s1097-2765(01)00438-5;
RA Hara Y., Wakamori M., Ishii M., Maeno E., Nishida M., Yoshida T.,
RA Yamada H., Shimizu S., Mori E., Kudoh J., Shimizu N., Kurose H., Okada Y.,
RA Imoto K., Mori Y.;
RT "LTRPC2 Ca2+-permeable channel activated by changes in redox status confers
RT susceptibility to cell death.";
RL Mol. Cell 9:163-173(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16601673; DOI=10.1038/sj.emboj.7601083;
RA Togashi K., Hara Y., Tominaga T., Higashi T., Konishi Y., Mori Y.,
RA Tominaga M.;
RT "TRPM2 activation by cyclic ADP-ribose at body temperature is involved in
RT insulin secretion.";
RL EMBO J. 25:1804-1815(2006).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19454650; DOI=10.1126/scisignal.2000278;
RA Lange I., Yamamoto S., Partida-Sanchez S., Mori Y., Fleig A., Penner R.;
RT "TRPM2 functions as a lysosomal Ca2+-release channel in beta cells.";
RL Sci. Signal. 2:RA23-RA23(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP FUNCTION.
RX PubMed=25562606; DOI=10.1042/bj20140747;
RA Manna P.T., Munsey T.S., Abuarab N., Li F., Asipu A., Howell G., Sedo A.,
RA Yang W., Naylor J., Beech D.J., Jiang L.H., Sivaprasadarao A.;
RT "TRPM2-mediated intracellular Zn2+ release triggers pancreatic beta-cell
RT death.";
RL Biochem. J. 466:537-546(2015).
CC -!- FUNCTION: Nonselective, voltage-independent cation channel that
CC mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic
CC Ca(2+) levels (PubMed:16651700, PubMed:16260005, PubMed:11804595,
CC PubMed:16601673, PubMed:19454650). Functions as ligand-gated ion
CC channel. Binding of ADP-ribose to the cytoplasmic Nudix domain causes a
CC conformation change; the channel is primed but still requires Ca(2+)
CC binding to trigger channel opening. Extracellular calcium passes
CC through the channel and increases channel activity (By similarity).
CC Also contributes to Ca(2+) release from intracellular stores in
CC response to ADP-ribose (PubMed:19454650). Plays a role in numerous
CC processes that involve signaling via intracellular Ca(2+) levels
CC (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in
CC response to reactive oxygen species, leading to increased cytosolic
CC Zn(2+) levels (PubMed:25562606). Activated by moderate heat (35 to 40
CC degrees Celsius) (PubMed:16601673). Activated by intracellular ADP-
CC ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative
CC stress caused by reactive oxygen or nitrogen species (PubMed:16260005,
CC PubMed:16601673, PubMed:25562606). The precise physiological activators
CC are under debate; the true, physiological activators may be ADP-ribose
CC and ADP-ribose-2'-phosphate. Activation by ADP-ribose and beta-NAD is
CC strongly increased by moderate heat (35 to 40 degrees Celsius) (By
CC similarity). Likewise, reactive oxygen species lower the threshold for
CC activation by moderate heat (37 degrees Celsius). Plays a role in
CC mediating behavorial and physiological responses to moderate heat and
CC thereby contributes to body temperature homeostasis. Plays a role in
CC insulin secretion, a process that requires increased cytoplasmic Ca(2+)
CC levels (PubMed:16601673). Required for normal IFNG and cytokine
CC secretion and normal innate immune immunity in response to bacterial
CC infection. Required for normal phagocytosis and cytokine release by
CC macrophages exposed to zymosan (in vitro). Plays a role in dendritic
CC cell differentiation and maturation, and in dendritic cell chemotaxis
CC via its role in regulating cytoplasmic Ca(2+) levels (By similarity).
CC Plays a role in the regulation of the reorganization of the actin
CC cytoskeleton and filopodia formation in response to reactive oxygen
CC species via its function in increasing cytoplasmic Ca(2+) and Zn(2+)
CC levels (By similarity). Confers susceptibility to cell death following
CC oxidative stress (PubMed:16651700, PubMed:11804595, PubMed:19454650,
CC PubMed:25562606). {ECO:0000250|UniProtKB:O94759,
CC ECO:0000250|UniProtKB:Q91YD4, ECO:0000269|PubMed:11804595,
CC ECO:0000269|PubMed:16260005, ECO:0000269|PubMed:16601673,
CC ECO:0000269|PubMed:16651700, ECO:0000269|PubMed:19454650,
CC ECO:0000269|PubMed:25562606, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O94759}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804595,
CC ECO:0000269|PubMed:16260005, ECO:0000269|PubMed:16601673,
CC ECO:0000269|PubMed:16651700, ECO:0000269|PubMed:19454650}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:O94759}. Perikaryon
CC {ECO:0000269|PubMed:16651700}. Cell projection
CC {ECO:0000269|PubMed:16651700}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:16651700}. Lysosome {ECO:0000269|PubMed:19454650}.
CC Note=Detected at the cell membrane and in intracellular vesicles in
CC cortical neurons. Detected on neuronal cell bodies and neurites
CC (PubMed:16651700). Detected on the cell membrane in polymorphonuclear
CC neutrophils. Detected on cytoplasmic vesicles and lysosomes in immature
CC bone marrow dendritic cells (By similarity).
CC {ECO:0000250|UniProtKB:Q91YD4, ECO:0000269|PubMed:16651700}.
CC -!- TISSUE SPECIFICITY: Detected in pancreas beta-cells (PubMed:16601673).
CC Detected in fetal brain cortex neurons (at protein level)
CC (PubMed:16651700). {ECO:0000269|PubMed:16601673,
CC ECO:0000269|PubMed:16651700}.
CC -!- DOMAIN: The cytosolic nudix box binds ADP-ribose and is required for
CC channel activation by ADP-ribose. {ECO:0000250|UniProtKB:O94759}.
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; AB193179; BAE72117.1; -; mRNA.
DR EMBL; AY749166; AAW65801.1; -; mRNA.
DR EMBL; AABR07044580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07044581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07072820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001011559.1; NM_001011559.1.
DR RefSeq; XP_006256311.1; XM_006256249.3.
DR AlphaFoldDB; E9PTA2; -.
DR SMR; E9PTA2; -.
DR STRING; 10116.ENSRNOP00000001631; -.
DR BindingDB; E9PTA2; -.
DR ChEMBL; CHEMBL4295638; -.
DR PaxDb; E9PTA2; -.
DR PeptideAtlas; E9PTA2; -.
DR GeneID; 294329; -.
DR KEGG; rno:294329; -.
DR CTD; 7226; -.
DR RGD; 1311889; Trpm2.
DR VEuPathDB; HostDB:ENSRNOG00000001216; -.
DR eggNOG; KOG3614; Eukaryota.
DR eggNOG; KOG4195; Eukaryota.
DR HOGENOM; CLU_001390_0_2_1; -.
DR InParanoid; E9PTA2; -.
DR OMA; DGTHGHY; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; E9PTA2; -.
DR TreeFam; TF314204; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:E9PTA2; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001216; Expressed in spleen and 15 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0072571; F:mono-ADP-D-ribose binding; ISS:UniProtKB.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071415; P:cellular response to purine-containing compound; ISS:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB.
DR GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0006828; P:manganese ion transport; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IDA:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0033194; P:response to hydroperoxide; ISO:RGD.
DR GO; GO:0014074; P:response to purine-containing compound; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
DR GO; GO:0071577; P:zinc ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cytoplasmic vesicle; Disulfide bond; Ion channel;
KW Ion transport; Lysosome; Membrane; Metal-binding; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1507
FT /note="Transient receptor potential cation channel
FT subfamily M member 2"
FT /id="PRO_0000438192"
FT TOPO_DOM 1..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 752..768
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 769..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 815..825
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 847..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 887..894
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 916..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 949..968
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 969..983
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 984..1020
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1021..1042
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 1043..1077
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 1078..1096
FT /evidence="ECO:0000250|UniProtKB:O94759"
FT TOPO_DOM 1097..1507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 1351..1502
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1387..1408
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 841
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IMY7"
FT BINDING 844
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IMY7"
FT BINDING 867
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IMY7"
FT BINDING 1071
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IMY7"
FT DISULFID 994..1006
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IMY7"
FT CONFLICT 783
FT /note="L -> P (in Ref. 2; AAW65801 and 1; BAE72117)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210
FT /note="L -> LA (in Ref. 2; AAW65801)"
FT /evidence="ECO:0000305"
FT CONFLICT 1374
FT /note="V -> M (in Ref. 2; AAW65801 and 1; BAE72117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1507 AA; 172259 MW; 3E54E154A0166F99 CRC64;
MEPLDQRRTD SDQEEGFGVQ SRRATDLGMV PNLRRSNSSL CKSRRLLCSF SSEKQENLSS
WIPENIKKKE CVYFVESSKL SDAGKVVCEC GYTHEQHIEV AIKPHTFQGK EWDPKKHVHE
MPTDAFGDIV FTGLSQKVGK YVRLSQDTSS IVIYQLMTQH WGLDVPSLLI SVTGGAKNFN
MKLRLKSIFR RGLVKVAQTT GAWIITGGSH TGVMKQVGEA VRDFSLSSSC KEGDVITIGI
ATWGTIHNRE ALIHPMGGFP AEYMLDEEGQ GNLTCLDSNH SHFILVDDGT HGQYGVEIPL
RTKLEKFISE QTKERGGVAI KIPIVCVVLE GGPGTLHTIY NAITNGTPCV IVEGSGRVAD
VIAQVAALPV SEITISLIQQ KLSVFFQEMF ETFTENQIVE WTKKIQDIVR RRQLLTVFRE
GKDGQQDVDV AILQALLKAS RSQDHFGHEN WDHQLKLAVA WNRVDIARSE IFTDEWQWKP
SDLHPMMTAA LISNKPEFVR LFLENGVRLK EFVTWDTLLC LYENLEPSCL FHSKLQKVLA
EEHERLAYAS ETPRLQMHHV AQVLRELLGD STQLLYPRPR YTDRPRLSLP MPHIKLNVQG
VSLRSLYKRS TGHVTFTIDP VRDLLIWAII QNHRELAGII WAQSQDCTAA ALACSKILKE
LSKEEEDTDS SEEMLALADE FEHRAIGVFT ECYRKDEERA QKLLVRVSEA WGKTTCLQLA
LEAKDMKFVS HGGIQAFLTK VWWGQLCVDN GLWRIILCML AFPLLFTGFI SFREKRLQAL
CRLARVRAFF NAPVVIFYLN ILSYFAFLCL FAYVLMVDFQ PSPSWCEYLI YLWLFSLVCE
ETRQLFYDPD GCGLMKMASL YFSDFWNKLD VGAILLFIAG LTCRLIPATL YPGRIILSLD
FIMFCLRLMH IFTISKTLGP KIIIVKRMMK DVFFFLFLLA VWVVSFGVAK QAILIHNESR
VDWIFRGVIY HSYLTIFGQI PTYIDGVNFS MDQCSPNGTD PYKPKCPESD WTGQAPAFPE
WLTVTLLCLY LLFANILLLN LLIAMFNYTF QEVQEHTDQI WKFQRHDLIE EYHGRPPAPP
PLILLSHLQL LIKRIVLKIP AKRHKQLKNK LEKNEEAALL SWELYLKENY LQNQQYQHKQ
RPEQKIQDIS EKVDTMVDLL DMDRVKRSGS TEQRLASLEE QVTQMGRSLH WIVTTLKDSG
FGSGAGALTL AQRAFDEPDA ELSIRKKGEE GGDGYHVSAR HLLYPDARIM RFPVPNEKVP
WEAEFLIYDP PFYTAEKKDA TLTDPVGDTA EPLSKINYNV VDGLMDRCSF HGTYVVQYGF
PLNPMGRTGL RGRGSLSWFG PNHTLQPVVT RWKRNQGGGI CRKSVRKMLE VLVVKLPQSE
HWALPGGSRE PGKMLPRKLK QVLQQEYWVT FETLLRQGTE VYKGYVDDPR NTDNAWIETV
AVSIHFQDQN DVELKRLEEN LQTHDPKESA RGLEMSTEWQ VVDRRIPLYV NHKKILQKVA
SLFGAHF
