TRPM4_RAT
ID TRPM4_RAT Reviewed; 1208 AA.
AC Q9ESQ5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 4;
DE AltName: Full=Calcium-activated non-selective cation channel 1;
DE AltName: Full=Long transient receptor potential channel 4;
DE Short=LTrpC-4;
DE Short=LTrpC4;
DE AltName: Full=MLS2s;
DE AltName: Full=Melastatin-like 2;
GN Name=Trpm4; Synonyms=Ltrpc4;
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;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19945433; DOI=10.1016/j.bbrc.2009.11.142;
RA Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N., Hong S.G.,
RA Park J.Y.;
RT "Cloning and characterization of rat transient receptor potential-
RT melastatin 4 (TRPM4).";
RL Biochem. Biophys. Res. Commun. 391:806-811(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 717-1208.
RC TISSUE=Brain;
RA Ohki G., Ishibashi K., Suzuki M.;
RT "Cloning of novel Ca-permeable channels.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION.
RX PubMed=15030426; DOI=10.1046/j.1540-8167.2004.03477.x;
RA Guinamard R., Chatelier A., Lenfant J., Bois P.;
RT "Activation of the Ca(2+)-activated nonselective cation channel by
RT diacylglycerol analogues in rat cardiomyocytes.";
RL J. Cardiovasc. Electrophysiol. 15:342-348(2004).
RN [5]
RP FUNCTION.
RX PubMed=16966582; DOI=10.1161/01.hyp.0000237864.65019.a5;
RA Guinamard R., Demion M., Magaud C., Potreau D., Bois P.;
RT "Functional expression of the TRPM4 cationic current in ventricular
RT cardiomyocytes from spontaneously hypertensive rats.";
RL Hypertension 48:587-594(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Calcium-activated non selective (CAN) cation channel that
CC mediates membrane depolarization. While it is activated by increase in
CC intracellular Ca(2+), it is impermeable to it. Mediates transport of
CC monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to
CC depolarize the membrane. It thereby plays a central role in
CC cadiomyocytes, neurons from entorhinal cortex, dorsal root and
CC vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells,
CC cochlea hair cells etc. Participates in T-cell activation by modulating
CC Ca(2+) oscillations after T lymphocyte activation, which is required
CC for NFAT-dependent IL2 production. Involved in myogenic constriction of
CC cerebral arteries. Controls insulin secretion in pancreatic beta-cells.
CC May also be involved in pacemaking or could cause irregular electrical
CC activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1)
CC and T-helper 2 (Th2) cell motility and cytokine production through
CC differential regulation of calcium signaling and NFATC1 localization.
CC Enhances cell proliferation through up-regulation of the beta-catenin
CC signaling pathway. Essential for the migration but not the maturation
CC of dendritic cells (By similarity). Plays a role in keratinocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q7TN37,
CC ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:16966582,
CC ECO:0000269|PubMed:19945433}.
CC -!- ACTIVITY REGULATION: Gating is voltage-dependent and repressed by
CC decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity. ATP is
CC able to restore Ca(2+) sensitivity after desensitization.
CC Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances
CC activity, by increasing the channel's Ca(2+) sensitivity and shifting
CC its voltage dependence of activation towards negative potentials.
CC Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole
CC derivative (BTP2) (By similarity). {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:19945433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TD43}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:19945433}. Golgi apparatus
CC {ECO:0000269|PubMed:19945433}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:19945433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TD43}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:19945433}. Golgi apparatus
CC {ECO:0000269|PubMed:19945433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist.;
CC Name=1; Synonyms=TRPM4b;
CC IsoId=Q9ESQ5-1; Sequence=Displayed;
CC Name=2; Synonyms=TRPM4a;
CC IsoId=Q9ESQ5-2; Sequence=VSP_040337;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the testis with a
CC moderate expression in the brain, spleen and thymus. Isoform 2 is only
CC expressed in the brain and spleen. {ECO:0000269|PubMed:19945433}.
CC -!- PTM: Phosphorylation by PKC leads to increase the sensitivity to
CC Ca(2+). {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- PTM: Sumoylated. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- MISCELLANEOUS: [Isoform 2]: Probably non-functional. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM4 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15808.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AABR03000917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03004552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040807; BAB15808.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001129701.1; NM_001136229.1. [Q9ESQ5-1]
DR AlphaFoldDB; Q9ESQ5; -.
DR SMR; Q9ESQ5; -.
DR STRING; 10116.ENSRNOP00000041387; -.
DR iPTMnet; Q9ESQ5; -.
DR PhosphoSitePlus; Q9ESQ5; -.
DR PaxDb; Q9ESQ5; -.
DR PRIDE; Q9ESQ5; -.
DR ABCD; Q9ESQ5; 1 sequenced antibody.
DR GeneID; 171143; -.
DR KEGG; rno:171143; -.
DR UCSC; RGD:620244; rat. [Q9ESQ5-1]
DR CTD; 54795; -.
DR RGD; 620244; Trpm4.
DR eggNOG; KOG3614; Eukaryota.
DR HOGENOM; CLU_001390_0_3_1; -.
DR InParanoid; Q9ESQ5; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q9ESQ5; -.
DR TreeFam; TF314204; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q9ESQ5; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q9ESQ5; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR GO; GO:0089717; C:spanning component of membrane; ISO:RGD.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0071318; P:cellular response to ATP; ISO:RGD.
DR GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:RGD.
DR GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:RGD.
DR GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:RGD.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:RGD.
DR GO; GO:1903949; P:positive regulation of atrial cardiac muscle cell action potential; IMP:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:1904199; P:positive regulation of regulation of vascular associated smooth muscle cell membrane depolarization; IMP:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0002724; P:regulation of T cell cytokine production; ISS:UniProtKB.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR029581; TRPM4.
DR InterPro; IPR041491; TRPM_SLOG.
DR PANTHER; PTHR13800:SF6; PTHR13800:SF6; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; ATP-binding; Calcium;
KW Calmodulin-binding; Cell membrane; Coiled coil; Disulfide bond;
KW Endoplasmic reticulum; Golgi apparatus; Immunity; Ion channel;
KW Ion transport; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1208
FT /note="Transient receptor potential cation channel
FT subfamily M member 4"
FT /id="PRO_0000259531"
FT TOPO_DOM 1..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 798..808
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 830..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 879..880
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 881..904
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 905..924
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 925..945
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 946..957
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT INTRAMEM 958..978
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 979..1013
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT TOPO_DOM 1035..1208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT REGION 1070..1170
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 1130..1135
FT /note="Mediates modulation by decavanadate and PIP2-
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT REGION 1189..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1128..1180
FT /evidence="ECO:0000255"
FT MOTIF 969..971
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT COMPBIAS 1193..1208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT BINDING 822
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 825
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 859
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 862
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT MOD_RES 1139
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT MOD_RES 1146
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT DISULFID 987..1005
FT /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT VAR_SEQ 1..186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19945433"
FT /id="VSP_040337"
SQ SEQUENCE 1208 AA; 135341 MW; 324CEC9A6B9F7EA6 CRC64;
MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV EDAFGAAVVT
EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP ATVYSLVTRS WGFRAPNLVV
SVLGGSEGPV LQTWLQDLLR RGLVRAAQST GAWIVTGGLH TGIGRHVGVA VRDHQTASTG
GSKVVAMGVA PWGVVRNRDM LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT
YGRMGGENRF RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL
LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA QVERIMTRKE
LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL AVAWNRVDIA QSELFRGDIQ
WRSFHLEASL MDALLNDRPE FVRLLISHGL SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ
ASHASSSKSP PANGAAELRP PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL
MDWANMQQDA SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL
EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA TCLQLAMQAD
ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL IYTNLILFRK SEEEPTQKDL
DFDMDSSMNG AGPLGPAEPS AKVALERRRR RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN
VVSYLLFLLL FAHVLLVDFQ PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG
PGKAPLRHRL HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL
LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD RSLPSILRRV
FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP VAGSCVSQYA NWLVVLLLIV
FLLVANILLL NLLIAMFSYT FNKVHGNSDL YWKAQRYSLI REFHSRPALA PPLIIISHLR
LLFKWLRRCH RTNLPASPVF EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE
RLKRTSQKVD TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP
PSPTGSKD
