CNGB1_BOVIN
ID CNGB1_BOVIN Reviewed; 1394 AA.
AC Q28181; Q03861; Q28082;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cyclic nucleotide-gated cation channel beta-1;
DE AltName: Full=240 kDa protein of rod photoreceptor CNG-channel;
DE AltName: Full=Cyclic nucleotide-gated cation channel 4;
DE Short=CNG channel 4;
DE Short=CNG-4;
DE Short=CNG4;
DE AltName: Full=Cyclic nucleotide-gated cation channel gamma;
DE AltName: Full=Cyclic nucleotide-gated cation channel modulatory subunit;
DE AltName: Full=Cyclic nucleotide-gated channel beta-1;
DE Short=CNG channel beta-1;
DE AltName: Full=Glutamic acid-rich protein;
DE Short=GARP;
GN Name=CNGB1; Synonyms=CNCG4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNG4A), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7546742; DOI=10.1016/0896-6273(95)90151-5;
RA Koerschen H.G., Illing M., Seifert R., Sesti F., Williams A., Gotzes S.,
RA Colville C., Mueller F., Dose A., Godde M., Molday L., Kaupp U.B.,
RA Molday R.S.;
RT "A 240 kDa protein represents the complete beta subunit of the cyclic
RT nucleotide-gated channel from rod photoreceptor.";
RL Neuron 15:627-636(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNG4C), AND ALTERNATIVE SPLICING
RP (ISOFORMS CNG4D AND CNG4E).
RC TISSUE=Testis;
RX PubMed=8626431; DOI=10.1074/jbc.271.11.6349;
RA Biel M., Zong X., Ludwig A., Sautter A., Hofmann F.;
RT "Molecular cloning and expression of the modulatory subunit of the cyclic
RT nucleotide-gated cation channel.";
RL J. Biol. Chem. 271:6349-6355(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GARP1).
RC TISSUE=Retina;
RX PubMed=2014230; DOI=10.1073/pnas.88.8.3116;
RA Sugimoto Y., Yatsunami K., Tsujimoto M., Khorana H.G., Ichikawa A.;
RT "The amino acid sequence of a glutamic acid-rich protein from bovine retina
RT as deduced from the cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3116-3119(1991).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS GARP1 AND GARP2).
RA Cote R.H.;
RL Unpublished observations (MAY-2009).
RN [5]
RP SUBUNIT.
RX PubMed=21878911; DOI=10.1038/ncomms1466;
RA Shuart N.G., Haitin Y., Camp S.S., Black K.D., Zagotta W.N.;
RT "Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic
RT nucleotide-gated ion channels.";
RL Nat. Commun. 2:457-457(2011).
CC -!- FUNCTION: Subunit of cyclic nucleotide-gated (CNG) channels,
CC nonselective cation channels, which play important roles in both visual
CC and olfactory signal transduction. When associated with CNGA1, it is
CC involved in the regulation of ion flow into the rod photoreceptor outer
CC segment (ROS), in response to light-induced alteration of the levels of
CC intracellular cGMP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory
CC subunits. {ECO:0000269|PubMed:21878911}.
CC -!- INTERACTION:
CC Q28181; F1MWM0: ABCA4; NbExp=3; IntAct=EBI-6979031, EBI-7079806;
CC Q28181; Q28181: CNGB1; NbExp=12; IntAct=EBI-6979031, EBI-6979031;
CC Q28181; P04695: GNAT1; NbExp=4; IntAct=EBI-6979031, EBI-7052221;
CC Q28181; P55203: GUCY2D; NbExp=5; IntAct=EBI-6979031, EBI-6943076;
CC Q28181; Q32LM8: NRM; NbExp=4; IntAct=EBI-6979031, EBI-7079707;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Isoform CNG4D is the most frequent isoform (CNG4D:CNG4C:CNG4E
CC = 20:2:1) in testis.;
CC Name=CNG4A;
CC IsoId=Q28181-6; Sequence=Displayed;
CC Name=CNG4C;
CC IsoId=Q28181-1; Sequence=VSP_037919, VSP_037920, VSP_037913;
CC Name=CNG4D;
CC IsoId=Q28181-2; Sequence=VSP_037919, VSP_037920, VSP_037916;
CC Name=CNG4E;
CC IsoId=Q28181-3; Sequence=VSP_037919, VSP_037920, VSP_037915;
CC Name=GARP1;
CC IsoId=Q28181-4; Sequence=VSP_037912, VSP_037913, VSP_037914,
CC VSP_037917, VSP_037918;
CC Name=GARP2;
CC IsoId=Q28181-5; Sequence=VSP_037910, VSP_037911;
CC -!- TISSUE SPECIFICITY: Retina, testis, kidney, heart and brain.
CC -!- MISCELLANEOUS: [Isoform GARP1]: In the rod cells, the Cngb1 locus
CC encodes the cyclic nucleotide-gated cation channel beta-1 subunit and
CC several glutamic-acid-rich proteins (GARPs). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform GARP2]: In the rod cells, the Cngb1 locus
CC encodes the cyclic nucleotide-gated cation channel beta-1 subunit and
CC several glutamic-acid-rich proteins (GARPs). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGB1 subfamily. {ECO:0000305}.
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DR EMBL; X89626; CAA61769.1; -; mRNA.
DR EMBL; X94707; CAA64367.1; -; mRNA.
DR EMBL; M61185; AAA30536.1; -; mRNA.
DR PIR; A40437; A40437.
DR RefSeq; NP_001129112.1; NM_001135640.1. [Q28181-4]
DR RefSeq; NP_001129113.1; NM_001135641.1. [Q28181-5]
DR RefSeq; NP_851362.1; NM_181019.2. [Q28181-6]
DR PDB; 7O4H; EM; 3.40 A; D=1-1394.
DR PDBsum; 7O4H; -.
DR AlphaFoldDB; Q28181; -.
DR SMR; Q28181; -.
DR DIP; DIP-47448N; -.
DR IntAct; Q28181; 9.
DR MINT; Q28181; -.
DR STRING; 9913.ENSBTAP00000032365; -.
DR PaxDb; Q28181; -.
DR PRIDE; Q28181; -.
DR GeneID; 281702; -.
DR KEGG; bta:281702; -.
DR CTD; 1258; -.
DR eggNOG; KOG0499; Eukaryota.
DR eggNOG; KOG1808; Eukaryota.
DR InParanoid; Q28181; -.
DR OrthoDB; 1073751at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0001895; P:retina homeostasis; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR DisProt; DP00768; -. [Q28181-4]
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032944; CNGB1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF16; PTHR45638:SF16; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cAMP; cAMP-binding;
KW Direct protein sequencing; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Olfaction;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..1394
FT /note="Cyclic nucleotide-gated cation channel beta-1"
FT /id="PRO_0000005555"
FT TOPO_DOM 1..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..789
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..822
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..867
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 868..904
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 905..927
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 928..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..991
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 992..1075
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1076..1096
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1097..1394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 682..692
FT /note="IQ-like"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1084..1222
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 1144
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT BINDING 1156
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..456
FT /note="Missing (in isoform CNG4C, isoform CNG4E and isoform
FT CNG4D)"
FT /evidence="ECO:0000303|PubMed:8626431"
FT /id="VSP_037919"
FT VAR_SEQ 292..299
FT /note="ISILPGEQ -> RVVAAGSL (in isoform GARP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037910"
FT VAR_SEQ 300..1394
FT /note="Missing (in isoform GARP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037911"
FT VAR_SEQ 341
FT /note="K -> E (in isoform GARP1)"
FT /evidence="ECO:0000303|PubMed:2014230"
FT /id="VSP_037912"
FT VAR_SEQ 457..465
FT /note="EEDEEEEQD -> MRAGQKGRC (in isoform CNG4C, isoform
FT CNG4E and isoform CNG4D)"
FT /evidence="ECO:0000303|PubMed:8626431"
FT /id="VSP_037920"
FT VAR_SEQ 482
FT /note="R -> Q (in isoform GARP1 and isoform CNG4C)"
FT /evidence="ECO:0000303|PubMed:2014230,
FT ECO:0000303|PubMed:8626431"
FT /id="VSP_037913"
FT VAR_SEQ 499
FT /note="A -> T (in isoform GARP1)"
FT /evidence="ECO:0000303|PubMed:2014230"
FT /id="VSP_037914"
FT VAR_SEQ 515..532
FT /note="Missing (in isoform CNG4E)"
FT /evidence="ECO:0000305"
FT /id="VSP_037915"
FT VAR_SEQ 522..530
FT /note="Missing (in isoform CNG4D)"
FT /evidence="ECO:0000305"
FT /id="VSP_037916"
FT VAR_SEQ 572..590
FT /note="VPATEEHPELQVEDADADS -> GSFQMSPFEALQECEALKR (in
FT isoform GARP1)"
FT /evidence="ECO:0000303|PubMed:2014230"
FT /id="VSP_037917"
FT VAR_SEQ 591..1394
FT /note="Missing (in isoform GARP1)"
FT /evidence="ECO:0000303|PubMed:2014230"
FT /id="VSP_037918"
FT CONFLICT 1283
FT /note="S -> A (in Ref. 2; CAA64367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="R -> A (in Ref. 2; CAA64367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336
FT /note="D -> E (in Ref. 2; CAA64367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1338
FT /note="A -> AA (in Ref. 2; CAA64367)"
FT /evidence="ECO:0000305"
FT HELIX 774..790
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 798..803
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 804..808
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 885..896
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 902..930
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 942..955
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 971..1000
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1003..1018
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1019..1021
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1025..1039
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 1040..1042
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1048..1053
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1056..1058
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1059..1066
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1082..1090
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1114..1118
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1121..1123
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1127..1129
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1134..1136
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1145..1147
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1148..1151
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1152..1154
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1160..1164
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1168..1170
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1174..1182
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 1184..1186
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1187..1202
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 1207..1211
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1212..1215
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 1218..1224
FT /evidence="ECO:0007829|PDB:7O4H"
SQ SEQUENCE 1394 AA; 155065 MW; EE6DA559BE3744A7 CRC64;
MLGWVQRVLP QPPGTPQKTK QEEEGTEPEP ELEPKPETAP EETELEEVSL PPEEPCVGKE
VAAVTLGPQG TQETALTPPT SLQAQVSVAP EAHSSPRGWV LTWLRKGVEK VVPQPAHSSR
PSQNIAAGLE SPDQQAGAQI LGQCGTGGSD EPSEPSRAED PGPGPWLLRW FEQNLEKMLP
QPPKISEGWR DEPTDAALGP EPPGPALEIK PMLQAQESPS LPAPGPPEPE EEPIPEPQPT
IQASSLPPPQ DSARLMAWIL HRLEMALPQP VIRGKGGEQE SDAPVTCDVQ TISILPGEQE
ESHLILEEVD PHWEEDEHQE GSTSTSPRTS EAAPADEEKG KVVEQTPREL PRIQEEKEDE
EEEKEDGEEE EEEGREKEEE EGEEKEEEEG REKEEEEGEK KEEEGREKEE EEGGEKEDEE
GREKEEEEGR GKEEEEGGEK EEEEGRGKEE VEGREEEEDE EEEQDHSVLL DSYLVPQSEE
DRSEESETQD QSEVGGAQAQ GEVGGAQALS EESETQDQSE VGGAQDQSEV GGAQAQGEVG
GAQEQDGVGG AQDQSTSHQE LQEEALADSS GVPATEEHPE LQVEDADADS RPLIAEENPP
SPVQLPLSPA KSDTLAVPGS ATGSLRKRLP SQDDEAEELK MLSPAASPVV AWSDPTSPQG
TDDQDRATST ASQNSAIIND RLQELVKLFK ERTEKVKEKL IDPDVTSDEE SPKPSPAKKA
PEPAPEVKPA EAGQVEEEHY CEMLCCKFKR RPWKKYQFPQ SIDPLTNLMY ILWLFFVVLA
WNWNCWLIPV RWAFPYQTPD NIHLWLLMDY LCDLIYLLDI TVFQMRLQFV RGGDIITDKK
EMRNNYVKSQ RFKMDMLCLL PLDLLYLKFG VNPLLRLPRC LKYMAFFEFN NRLESILSKA
YVYRVIRTTA YLLYSLHLNS CLYYWASAYE GLGSTHWVYD GVGNSYIRCY YWAVKTLITI
GGLPDPRTLF EIVFQGLNYF TGVFAFSVMI GQMRDVVGAA TAGQTYYRSC MDSTVKYMNF
YKIPRSVQNR VKTWYEYTWH SQGMLDESEL MVQLPDKMRL DLAIDVNYSI VSKVALFQGC
DRQMIFDMLK RLRSVVYLPN DYVCKKGEIG REMYIIQAGQ VQVLGGPDGK SVLVTLKAGS
VFGEISLLAV GGGNRRTANV VAHGFTNLFI LDKKDLNEIL VHYPESQKLL RKKARRMLRN
NNKPKEKSVL ILPPRAGTPK LFNAALAAAG KMGAKGGRGG RLALLRARLK ELAALEAAAR
QQQLLEQAKS SEDAAVGEEG SASPEQPPRP EPPAPEAPAP EPTAPEPLAP EAPAPEAPAP
SSPPPASQER PEGDKDAARP EEHPVRIHVT LGPDPSEQIL LVEVPEKQEE KEKKEEETEE
KEEGEEARKE KEEE
