CAC1I_RAT
ID CAC1I_RAT Reviewed; 2201 AA.
AC Q9Z0Y8; Q9EQ59;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1I;
DE AltName: Full=CaVT.3;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.3;
GN Name=Cacna1i;
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] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10066244; DOI=10.1523/jneurosci.19-06-01912.1999;
RA Lee J.-H., Daud A.N., Cribbs L.L., Lacerda A.E., Pereverzev A.,
RA Kloeckner U., Schneider T., Perez-Reyes E.;
RT "Cloning and expression of a novel member of the low voltage-activated T-
RT type calcium channel family.";
RL J. Neurosci. 19:1912-1921(1999).
RN [2]
RP SEQUENCE REVISION TO 345; 1656 AND 1737.
RA Perez-Reyes E.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP SEQUENCE REVISION.
RA McRory J.E.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, 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: 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. This channel gives rise to T-type calcium
CC currents. T-type calcium channels belong to the 'low-voltage activated
CC (LVA)' group and are strongly blocked by nickel and mibefradil. A
CC particularity of this type of channels is an opening at quite negative
CC potentials, and a voltage-dependent inactivation. T-type channels serve
CC pacemaking functions in both central neurons and cardiac nodal cells
CC and support calcium signaling in secretory cells and vascular smooth
CC muscle. They may also be involved in the modulation of firing patterns
CC of neurons which is important for information processing as well as in
CC cell growth processes. Gates in voltage ranges similar to, but higher
CC than alpha 1G or alpha 1H.
CC -!- SUBUNIT: Interacts with CATSPER1 and CATSPER2, leading to suppress T-
CC type calcium channel activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0Y8-2; Sequence=VSP_018347, VSP_018348, VSP_018349;
CC -!- TISSUE SPECIFICITY: Brain.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1I subfamily. {ECO:0000305}.
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DR EMBL; AF086827; AAD17796.2; -; mRNA.
DR EMBL; AF290214; AAG35188.4; -; mRNA.
DR RefSeq; NP_064469.3; NM_020084.3. [Q9Z0Y8-1]
DR AlphaFoldDB; Q9Z0Y8; -.
DR SMR; Q9Z0Y8; -.
DR STRING; 10116.ENSRNOP00000046091; -.
DR BindingDB; Q9Z0Y8; -.
DR ChEMBL; CHEMBL5459; -.
DR GuidetoPHARMACOLOGY; 537; -.
DR GlyGen; Q9Z0Y8; 5 sites.
DR iPTMnet; Q9Z0Y8; -.
DR PhosphoSitePlus; Q9Z0Y8; -.
DR PaxDb; Q9Z0Y8; -.
DR PRIDE; Q9Z0Y8; -.
DR GeneID; 56827; -.
DR KEGG; rno:56827; -.
DR UCSC; RGD:68944; rat. [Q9Z0Y8-1]
DR CTD; 8911; -.
DR RGD; 68944; Cacna1i.
DR eggNOG; KOG2302; Eukaryota.
DR InParanoid; Q9Z0Y8; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9Z0Y8; -.
DR PRO; PR:Q9Z0Y8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IC:RGD.
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:MGI.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:InterPro.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0030431; P:sleep; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR030162; CACNA1I.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF209; PTHR10037:SF209; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2201
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1I"
FT /id="PRO_0000053958"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..137
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..166
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..189
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..396
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..654
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..679
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..711
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..795
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..820
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..1125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1126..1148
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1167..1187
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1188..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1198..1217
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1218..1231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1232..1253
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1254..1263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1264..1287
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1288..1364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1365..1390
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1391..1445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1446..1466
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1467..1480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1481..1502
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1503..1509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1510..1528
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1529..1542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1543..1566
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1567..1580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1581..1601
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1602..1664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1665..1692
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1693..1835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 64..399
FT /note="I"
FT REPEAT 584..823
FT /note="II"
FT REPEAT 1116..1393
FT /note="III"
FT REPEAT 1431..1692
FT /note="IV"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2126..2201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 355
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 779
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1339
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1637
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1732..1772
FT /note="WPLAPVLARGCPLVLLGATGARIGRGRCWRRHRESPVPSTR -> CPCPCPG
FT PRLPTSSPGAPGRGSGGAGAGGDTESHLCRHC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10066244"
FT /id="VSP_018347"
FT VAR_SEQ 1827..1837
FT /note="VQLAETEAFSL -> TGLHPSCWGMT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10066244"
FT /id="VSP_018348"
FT VAR_SEQ 1838..2201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10066244"
FT /id="VSP_018349"
FT CONFLICT 555
FT /note="P -> L (in Ref. 1; AAD17796)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="E -> K (in Ref. 1; AAD17796)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="Y -> C (in Ref. 1; AAD17796)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="C -> R (in Ref. 1; AAD17796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2201 AA; 243693 MW; 5791A4FDD7B882FE CRC64;
MADSNLPPSS AAAPAPEPGI TEQPGPRSPP PSPPGLEEPL EGTNPDVPHP DLAPVAFFCL
RQTTSPRNWC IKMVCNPWFE CVSMLVILLN CVTLGMYQPC DDMECLSDRC KILQVFDDFI
FIFFAMEMVL KMVALGIFGK KCYLGDTWNR LDFFIVMAGM VEYSLDLQNI NLSAIRTVRV
LRPLKAINRV PSMRILVNLL LDTLPMLGNV LLLCFFVFFI FGIIGVQLWA GLLRNRCFLE
ENFTIQGDVA LPPYYQPEED DEMPFICSLT GDNGIMGCHE IPPLKEQGRE CCLSKDDVYD
FGAGRQDLNA SGLCVNWNRY YNVCRTGNAN PHKGAINFDN IGYAWIVIFQ VITLEGWVEI
MYYVMDAHSF YNFIYFILLI IVGSFFMINL CLVVIATQFS ETKQREHRLM LEQRQRYLSS
STVASYAEPG DCYEEIFQYV CHILRKAKRR ALGLYQALQN RRQAMGPGTP APAKPGPHAK
EPSHCKLCPR HSPLDPTPHT LVQPISAILA SDPSSCPHCQ HEAGRRPSGL GSTDSGQEGS
GSGGSAEAEA NGDGPQSSED GVSSDLGKEE EQEDGAARLC GDVWRETREK LRGIVDSKYF
NRGIMMAILV NTVSMGIEHH EQPEELTNIL EICNVVFTSM FALEMILKLA AFGLFDYLRN
PYNIFDSIIV IISIWEIVGQ ADGGLSVLRT FRLLRVLKLV RFMPALRRQL VVLMKTMDNV
ATFCMLLMLF IFIFSILGMH IFGCKFSLRT DTGDTVPDRK NFDSLLWAIV TVFQILTQED
WNVVLYNGMA STTPWASLYF VALMTFGNYV LFNLLVAILV EGFQAEGDAN RSYSDEDQSS
SNLEEFDKLP EGLDNSRDLK LCPIPMTPNG HLDPSLPLGA HLGPAGTMGT APRLSLQPDP
VLVALDSRKS SVMSLGRMSY DQRSLSSSRS SYYGPWGRSG TWASRRSSWN SLKHKPPSAE
HESLLSGEGG GSCVRACEGA REEAPTRTAP LHAPHAHHAH HGPHLAHRHR HHRRTLSLDT
RDSVDLGELV PVVGAHSRAA WRGAGQAPGH EDCNGRMPNI AKDVFTKMDD CRDRGEDEEE
IDYTLCFRVR KMIDVYKPDW CEVREDWSVY LFSPENKFRI LCQTIIAHKL FDYVVLAFIF
LNCITIALER PQIEAGSTER IFLTVSNYIF TAIFVGEMTL KVVSLGLYFG EQAYLRSSWN
VLDGFLVFVS IIDIVVSVAS AGGAKILGVL RVLRLLRTLR PLRVISRAPG LKLVVETLIS
SLKPIGNIVL ICCAFFIIFG ILGVQLFKGK FYHCLGVDTR NITNRSDCVA ANYRWVHHKY
NFDNLGQALM SLFVLASKDG WVNIMYNGLD AVAVDQQPVT NHNPWMLLYF ISFLLIVSFF
VLNMFVGVVV ENFHKCRQHQ EAEEARRREE KRLRRLEKKR RKAQRLPYYA TYCPTRLLIH
SMCTSHYLDI FITFIICLNV VTMSLEHYNQ PTSLETALKY CNYMFTTVFV LEAVLKLVAF
GLRRFFKDRW NQLDLAIVLL SVMGITLEEI EINAALPINP TIIRIMRVLR IARVLKLLKM
ATGMRALLDT VVQALPQVGN LGLLFMLLFF IYAALGVELF GKLVCNDENP CEGMSRHATF
ENFGMAFLTL FQVSTGDNWN GIMKDTLRDC THDERSCLSS LQFVSPLYFV SFVLTAQFVL
INVVVAVLMK HLDDSNKEAQ EDAEMDAEIE LEMAHGLGPC PGPCPGPCPC PWPLAPVLAR
GCPLVLLGAT GARIGRGRCW RRHRESPVPS TRYSPAQETL WLDSVSLIIK DSLEGELTII
DNLSGSVFHH YASPDGCGKC HHDKQEVQLA ETEAFSLNSD RSSSILLGDD LSLEDPTACP
PGRKDSKGEL DPPEPMRVGD LGECFFPLSS TAVSPDPENF LCEMEEIPFN PVQSWLKHDS
SQAPPSPFSP DGSSPLLQMP AEFFHPAVSA SQKGPEKGTG TGTLPKIALQ GSWASLRSPS
VNCTLLRQAT GSDTSLDASP SSSAGSLQTT LEDSLTLSDS PRRALGPPVQ VPGPRASLSP
ATRRRLSLRG RGLFSLRGLR AHQRSHSSGG STSPGCTHHD SMDPSDEEGR GGAGGGGAGS
EHSETLSSLS LTSLFCLPPT LPPPGLTPAR KFNSTSSLAA GPGRPGSTVS ARGLVRSPSW
AADRSKDPPG QAQLVSGLGS SAPGPQPPPG ESTDAASKRK R
