CAC1A_RABIT
ID CAC1A_RABIT Reviewed; 2424 AA.
AC P27884; P27883;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE AltName: Full=Brain calcium channel I;
DE Short=BI;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN Name=CACNA1A; Synonyms=CACH4, CACN3, CACNL1A4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=1849233; DOI=10.1038/350398a0;
RA Mori Y., Friedrich T., Kim M.-S., Mikami A., Nakai J., Ruth P., Bosse E.,
RA Hofmann F., Flockerzi V., Furuichi T., Mikoshiba K., Imoto K., Tanabe T.,
RA Numa S.;
RT "Primary structure and functional expression from complementary DNA of a
RT brain calcium channel.";
RL Nature 350:398-402(1991).
RN [2]
RP BETA-SUBUNIT BINDING DOMAIN, AND MUTAGENESIS OF GLU-386; LEU-389; TYR-392
RP AND GLU-400.
RX PubMed=7509046; DOI=10.1038/368067a0;
RA Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.;
RT "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT cytoplasmic linker of the alpha 1-subunit.";
RL Nature 368:67-70(1994).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLU-188 AND GLU-1658.
RX PubMed=11055992; DOI=10.1085/jgp.116.5.637;
RA Winterfield J.R., Swartz K.J.;
RT "A hot spot for the interaction of gating modifier toxins with voltage-
RT dependent ion channels.";
RL J. Gen. Physiol. 116:637-644(2000).
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-1A gives rise to P and/or Q-
CC type calcium currents. P/Q-type calcium channels belong to the 'high-
CC voltage activated' (HVA) group and are specifically blocked by the
CC spider omega-agatoxin-IVA (AC P54282) (By similarity). They are however
CC insensitive to dihydropyridines (DHP). {ECO:0000250|UniProtKB:P54282,
CC ECO:0000269|PubMed:11055992}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity. Interacts with CABP1 (By similarity).
CC Interacts with the spider omega-agatoxin-IVA (AC P30288). {ECO:0000250,
CC ECO:0000250|UniProtKB:O00555, ECO:0000250|UniProtKB:P54282}.
CC -!- INTERACTION:
CC P27884; P62158: CALM3; Xeno; NbExp=3; IntAct=EBI-15685548, EBI-397435;
CC P27884; P55040: GEM; Xeno; NbExp=2; IntAct=EBI-15685548, EBI-744104;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00555};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=BI-2; Synonyms=1A-2;
CC IsoId=P27884-1; Sequence=Displayed;
CC Name=BI-1; Synonyms=1A-1;
CC IsoId=P27884-2; Sequence=VSP_000879, VSP_000880;
CC Name=CBP101; Synonyms=CBP109;
CC IsoId=P27884-3; Sequence=VSP_000878;
CC Name=CBP103;
CC IsoId=P27884-4; Sequence=VSP_000877;
CC Name=CBP107;
CC IsoId=P27884-5; Sequence=VSP_000876;
CC -!- TISSUE SPECIFICITY: Brain specific. Purkinje cells contain
CC predominantly P-type VSCC, the Q-type being a prominent calcium current
CC in cerebellar granule cells.
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 -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
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DR EMBL; X57477; CAA40715.1; -; mRNA.
DR EMBL; X57689; CAA40872.1; -; mRNA.
DR EMBL; X57476; CAA40714.1; -; mRNA.
DR EMBL; X57688; CAA40871.1; -; mRNA.
DR PIR; I46477; I46477.
DR PIR; I46480; I46480.
DR RefSeq; NP_001095163.1; NM_001101693.1. [P27884-2]
DR PDB; 3DVM; X-ray; 2.60 A; B=1963-1982.
DR PDBsum; 3DVM; -.
DR AlphaFoldDB; P27884; -.
DR BMRB; P27884; -.
DR SMR; P27884; -.
DR BioGRID; 1172286; 4.
DR DIP; DIP-29591N; -.
DR IntAct; P27884; 3.
DR STRING; 9986.ENSOCUP00000010319; -.
DR PRIDE; P27884; -.
DR GeneID; 100009265; -.
DR KEGG; ocu:100009265; -.
DR CTD; 773; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P27884; -.
DR OrthoDB; 172471at2759; -.
DR EvolutionaryTrace; P27884; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005448; CACNA1A.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01632; PQVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2424
FT /note="Voltage-dependent P/Q-type calcium channel subunit
FT alpha-1A"
FT /id="PRO_0000053918"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..117
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..155
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..185
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..209
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..248
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..360
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..506
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..541
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..568
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..578
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..597
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..636
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..689
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..714
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..1253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1254..1272
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1273..1288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1289..1308
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1309..1320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1321..1339
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1340..1350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1369
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1370..1388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1389..1408
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1409..1495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1496..1520
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1521..1575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1576..1604
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1605..1609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1610..1629
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1630..1637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1638..1656
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1657..1665
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1666..1684
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1685..1703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1704..1723
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1724..1795
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1796..1820
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1821..2424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 85..363
FT /note="I"
FT REPEAT 473..717
FT /note="II"
FT REPEAT 1240..1523
FT /note="III"
FT REPEAT 1560..1823
FT /note="IV"
FT REGION 383..400
FT /note="Binding to the beta subunit"
FT REGION 819..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1997..2424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2143..2162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2213..2231
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2302
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2369..2389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT SITE 1658
FT /note="Binds to omega-Aga-IVA"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1993
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 2054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54282"
FT MOD_RES 2072
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 2084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54282"
FT MOD_RES 2086
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54282"
FT MOD_RES 2127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 2148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54282"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 772..1120
FT /note="Missing (in isoform CBP103)"
FT /evidence="ECO:0000305"
FT /id="VSP_000877"
FT VAR_SEQ 772..1051
FT /note="Missing (in isoform CBP107)"
FT /evidence="ECO:0000305"
FT /id="VSP_000876"
FT VAR_SEQ 1857..1884
FT /note="LYRDMYAMLRHMPPPLGLGKNCPARVAY -> HYKDMYSLLRVISPPLGLGK
FT KCPHRVAC (in isoform CBP101)"
FT /evidence="ECO:0000305"
FT /id="VSP_000878"
FT VAR_SEQ 2230..2273
FT /note="RGPGRVSPGVSARRRRRGPVARVRPARAPALAHARARARAPARL -> PAAA
FT DKERYGPQDRPDHGHGRARARDQRWSRSPSEGREHTTHRQ (in isoform BI-1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000879"
FT VAR_SEQ 2274..2424
FT /note="Missing (in isoform BI-1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000880"
FT VARIANT 419
FT /note="Missing (in isoform CBP315)"
FT VARIANT 877
FT /note="A -> T (in isoform CBS)"
FT VARIANT 1104
FT /note="S -> N (in isoform CBS)"
FT MUTAGEN 188
FT /note="E->K: No change in inhibition by omega-Aga-IVA."
FT /evidence="ECO:0000269|PubMed:11055992"
FT MUTAGEN 386
FT /note="E->S: Reduced beta-subunit interaction."
FT /evidence="ECO:0000269|PubMed:7509046"
FT MUTAGEN 389
FT /note="L->H: Reduced beta-subunit interaction."
FT /evidence="ECO:0000269|PubMed:7509046"
FT MUTAGEN 392
FT /note="Y->S: Reduced beta-subunit interaction."
FT /evidence="ECO:0000269|PubMed:7509046"
FT MUTAGEN 400
FT /note="E->A: No effect on beta-subunit interaction."
FT /evidence="ECO:0000269|PubMed:7509046"
FT MUTAGEN 1658
FT /note="E->K: Loss of inhibition by omega-Aga-IVA."
FT /evidence="ECO:0000269|PubMed:11055992"
FT HELIX 1963..1979
FT /evidence="ECO:0007829|PDB:3DVM"
SQ SEQUENCE 2424 AA; 273231 MW; F7CC4D0AB4B45604 CRC64;
MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD VEQRHPFDGA
LRRATIKKSK TDLLHPEEAE DQLADIASVG SPFARASIKS AKLENSSFFH KKERRMRFYI
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
QELTKDEQEE EEAVNQKLAL QKAKEVAEVS PLSAANMSIA MKEQQKNQKP AKSVWEQRTS
EMRKQNLLAS REALYSEMDP EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR
VAEPTVDQRL GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY
GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG SPRTGTADGE
PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE GPDGGGGGGG ERRRRHRHGP
PPAYDPDARR DDRERRHRRR KDTQGSGVPV SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK
NSRLATAEPV SPHENLSHAG LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN
PSNPGPPKTP ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN
PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL
MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD
LWNILDFIVV SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV
NSLKNVFNIL IVYMLFMFIF AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA
RDREWKKYEF HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY
VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN
KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS VAYDNALKVF NIVFTSLFSL
ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL
LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF
QITEHNNFRT FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF
VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP AAWGRMLYRD
MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV HFNSTLMALI RTALDIKIAK
GGADKQQMDA ELRKEMMAIW PNLSQKTLDL LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA
KKLQAMREEQ NRTPLMFQRM EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT
QRAQEMFQKT GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS
MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE RVPPEENQRH
HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP SREREQERGR PKDRKHRPHH
HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA RVRPARAPAL AHARARARAP ARLLPELRLR
RARRPRPRQR RRPRRRRGGG GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL
PGPRTGQAPR ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR
RGGRRWTASA GKGGGGPRAS APSP
