CAC1G_RAT
ID CAC1G_RAT Reviewed; 2254 AA.
AC O54898; Q548R1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1G;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.1;
GN Name=Cacna1g;
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 [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9495342; DOI=10.1038/36110;
RA Perez-Reyes E., Cribbs L.L., Daud A., Lacerda A.E., Barclay J.,
RA Williamson M.P., Fox M., Rees M., Lee J.-H.;
RT "Molecular characterization of a neuronal low-voltage-activated T-type
RT calcium channel.";
RL Nature 391:896-900(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11073957; DOI=10.1074/jbc.m008215200;
RA McRory J.E., Santi C.M., Hamming K.S.C., Mezeyova J., Sutton K.G.,
RA Baillie D.L., Stea A., Snutch T.P.;
RT "Molecular and functional characterization of a family of rat brain T-type
RT calcium channels.";
RL J. Biol. Chem. 276:3999-4011(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-716; SER-1118;
RP SER-1124 AND SER-1125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1G gives rise to T-type
CC calcium currents. T-type calcium channels belong to the 'low-voltage
CC activated (LVA)' group and are strongly blocked by nickel and
CC mibefradil. A particularity of this type of channels is an opening at
CC quite negative potentials and a voltage-dependent inactivation. T-type
CC channels serve pacemaking functions in both central neurons and cardiac
CC nodal cells and support calcium signaling in secretory cells and
CC vascular smooth muscle. They may also be involved in the modulation of
CC firing patterns of neurons which is important for information
CC processing as well as in cell growth processes.
CC {ECO:0000269|PubMed:11073957, ECO:0000269|PubMed:9495342}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43497};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43497}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Moderate expression in
CC heart; low expression in placenta, kidney and lung.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: In response to raising of intracellular calcium, the T-type
CC channels are activated by CaM-kinase II.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1G subfamily. {ECO:0000305}.
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DR EMBL; AF027984; AAC67372.1; -; mRNA.
DR EMBL; AF290212; AAG35186.2; -; mRNA.
DR PIR; T09053; T09053.
DR AlphaFoldDB; O54898; -.
DR SMR; O54898; -.
DR BioGRID; 248334; 1.
DR STRING; 10116.ENSRNOP00000061436; -.
DR BindingDB; O54898; -.
DR ChEMBL; CHEMBL4257; -.
DR DrugCentral; O54898; -.
DR GuidetoPHARMACOLOGY; 535; -.
DR GlyGen; O54898; 8 sites.
DR iPTMnet; O54898; -.
DR PhosphoSitePlus; O54898; -.
DR PaxDb; O54898; -.
DR PRIDE; O54898; -.
DR RGD; 68942; Cacna1g.
DR eggNOG; KOG2302; Eukaryota.
DR InParanoid; O54898; -.
DR PhylomeDB; O54898; -.
DR PRO; PR:O54898; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:BHF-UCL.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0014824; P:artery smooth muscle contraction; IMP:RGD.
DR GO; GO:0086016; P:AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086027; P:AV node cell to bundle of His cell signaling; ISS:BHF-UCL.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0010045; P:response to nickel cation; ISO:RGD.
DR GO; GO:0086015; P:SA node cell action potential; ISS:BHF-UCL.
DR GO; GO:0086018; P:SA node cell to atrial cardiac muscle cell signaling; ISS:BHF-UCL.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR030154; VDCC_T_a1G.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR PANTHER; PTHR10037:SF137; PTHR10037:SF137; 2.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Cytoplasm;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2254
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1G"
FT /id="PRO_0000053953"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 102..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..141
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..170
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 171..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..193
FT /note="Helical; Name=S4 of repeat I"
FT TOPO_DOM 194..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..395
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 396..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..778
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..800
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..825
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..857
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 858..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..940
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 941..965
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 966..1251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1252..1274
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1275..1292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1293..1313
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1314..1323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1324..1343
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1344..1357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1358..1379
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1380..1389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1390..1413
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1414..1490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1491..1516
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1517..1578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1579..1599
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1600..1613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1614..1635
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1636..1642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1643..1661
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1662..1675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1676..1699
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1700..1713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1714..1734
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1735..1794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1795..1822
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1823..2254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..398
FT /note="I"
FT REPEAT 730..968
FT /note="II"
FT REPEAT 1242..1519
FT /note="III"
FT REPEAT 1564..1822
FT /note="IV"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2153..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2217..2248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 354
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 924
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1465
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1770
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2254 AA; 250407 MW; 697BBE06360CF0F6 CRC64;
MDEEEDGAGA EESGQPRSFT QLNDLSGAGG RQGPGSTEKD PGSADSEAEG LPYPALAPVV
FFYLSQDSRP RSWCLRTVCN PWFERVSMLV ILLNCVTLGM FRPCEDIACD SQRCRILQAF
DDFIFAFFAV EMVVKMVALG IFGKKCYLGD TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR
TVRVLRPLRA INRVPSMRIL VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR
CFLPENFSLP LSVDLEPYYQ TENEDESPFI CSQPRENGMR SCRSVPTLRG EGGGGPPCSL
DYETYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
STLASFSEPG SCYEELLKYL VYILRKAARR LAQVSRAIGV RAGLLSSPVA RSGQEPQPSG
SCTRSHRRLS VHHLVHHHHH HHHHYHLGNG TLRVPRASPE IQDRDANGSR RLMLPPPSTP
TPSGGPPRGA ESVHSFYHAD CHLEPVRCQA PPPRCPSEAS GRTVGSGKVY PTVHTSPPPE
ILKDKALVEV APSPGPPTLT SFNIPPGPFS SMHKLLETQS TGACHSSCKI SSPCSKADSG
ACGPDSCPYC ARTGAGEPES ADHVMPDSDS EAVYEFTQDA QHSDLRDPHS RRRQRSLGPD
AEPSSVLAFW RLICDTFRKI VDSKYFGRGI MIAILVNTLS MGIEYHEQPE ELTNALEISN
IVFTSLFALE MLLKLLVYGP FGYIKNPYNI FDGVIVVISV WEIVGQQGGG LSVLRTFRLM
RVLKLVRFLP ALQRQLVVLM KTMDNVATFC MLLMLFIFIF SILGMHLFGC KFASERDGDT
LPDRKNFDSL LWAIVTVFQI LTQEDWNKVL YNGMASTSSW AALYFIALMT FGNYVLFNLL
VAILVEGFQA EGDATKSESE PDFFSPSVDG DGDRKKRLAL VALGEHAELR KSLLPPLIIH
TAATPMSHPK SSSTGVGEAL GSGSRRTSSS GSAEPGAAHH EMKCPPSARS SPHSPWSAAS
SWTSRRSSRN SLGRAPSLKR RSPSGERRSL LSGEGQESQD EEESSEEDRA SPAGSDHRHR
GSLEREAKSS FDLPDTLQVP GLHRTASGRS SASEHQDCNG KSASGRLART LRTDDPQLDG
DDDNDEGNLS KGERIQAWVR SRLPACCRER DSWSAYIFPP QSRFRLLCHR IITHKMFDHV
VLVIIFLNCI TIAMERPKID PHSAERIFLT LSNYIFTAVF LAEMTVKVVA LGWCFGEQAY
LRSSWNVLDG LLVLISVIDI LVSMVSDSGT KILGMLRVLR LLRTLRPLRV ISRAQGLKLV
VETLMSSLKP IGNIVVICCA FFIIFGILGV QLFKGKFFVC QGEDTRNITN KSDCAEASYR
WVRHKYNFDN LGQALMSLFV LASKDGWVDI MYDGLDAVGV DQQPIMNHNP WMLLYFISFL
LIVAFFVLNM FVGVVVENFH KCRQHQEEEE ARRREEKRLR RLEKKRRSKE KQMAEAQCKP
YYSDYSRFRL LVHHLCTSHY LDLFITGVIG LNVVTMAMEH YQQPQILDEA LKICNYIFTV
IFVFESVFKL VAFGFRRFFQ DRWNQLDLAI VLLSIMGITL EEIEVNLSLP INPTIIRIMR
VLRIARVLKL LKMAVGMRAL LHTVMQALPQ VGNLGLLFML LFFIFAALGV ELFGDLECDE
THPCEGLGRH ATFRNFGMAF LTLFRVSTGD NWNGIMKDTL RDCDQESTCY NTVISPIYFV
SFVLTAQFVL VNVVIAVLMK HLEESNKEAK EEAELEAELE LEMKTLSPQP HSPLGSPFLW
PGVEGVNSTD SPKPGAPHTT AHIGAASGFS LEHPTMVPHP EEVPVPLGPD LLTVRKSGVS
RTHSLPNDSY MCRNGSTAER SLGHRGWGLP KAQSGSILSV HSQPADTSCI LQLPKDVHYL
LQPHGAPTWG AIPKLPPPGR SPLAQRPLRR QAAIRTDSLD VQGLGSREDL LSEVSGPSCP
LTRSSSFWGG SSIQVQQRSG IQSKVSKHIR LPAPCPGLEP SWAKDPPETR SSLELDTELS
WISGDLLPSS QEEPLFPRDL KKCYSVETQS CRRRPGFWLD EQRRHSIAVS CLDSGSQPRL
CPSPSSLGGQ PLGGPGSRPK KKLSPPSISI DPPESQGSRP PCSPGVCLRR RAPASDSKDP
SVSSPLDSTA ASPSPKKDTL SLSGLSSDPT DMDP
