ADCY3_MOUSE
ID ADCY3_MOUSE Reviewed; 1145 AA.
AC Q8VHH7; B8JK57;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Adenylate cyclase type 3;
DE EC=4.6.1.1 {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148, ECO:0000269|PubMed:9768837};
DE AltName: Full=ATP pyrophosphate-lyase 3;
DE AltName: Full=Adenylate cyclase type III;
DE Short=AC-III;
DE AltName: Full=Adenylate cyclase, olfactive type;
DE AltName: Full=Adenylyl cyclase 3;
DE Short=AC3 {ECO:0000303|PubMed:9768837};
GN Name=Adcy3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Pasternak S., Neumann P.E.;
RT "Sequence of mouse Adcy3.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-1077, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=9768837; DOI=10.1016/s0896-6273(00)80561-9;
RA Wei J., Zhao A.Z., Chan G.C., Baker L.P., Impey S., Beavo J.A., Storm D.R.;
RT "Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM kinase
RT II in neurons: a mechanism for attenuation of olfactory signals.";
RL Neuron 21:495-504(1998).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11055432; DOI=10.1016/s0896-6273(00)00060-x;
RA Wong S.T., Trinh K., Hacker B., Chan G.C., Lowe G., Gaggar A., Xia Z.,
RA Gold G.H., Storm D.R.;
RT "Disruption of the type III adenylyl cyclase gene leads to peripheral and
RT behavioral anosmia in transgenic mice.";
RL Neuron 27:487-497(2000).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15705663; DOI=10.1210/me.2004-0318;
RA Livera G., Xie F., Garcia M.A., Jaiswal B., Chen J., Law E., Storm D.R.,
RA Conti M.;
RT "Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility
RT and spermatozoon function.";
RL Mol. Endocrinol. 19:1277-1290(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP MUTAGENESIS OF MET-279, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=25329148; DOI=10.1371/journal.pone.0110226;
RA Pitman J.L., Wheeler M.C., Lloyd D.J., Walker J.R., Glynne R.J.,
RA Gekakis N.;
RT "A gain-of-function mutation in adenylate cyclase 3 protects mice from
RT diet-induced obesity.";
RL PLoS ONE 9:E110226-E110226(2014).
RN [9]
RP SUMOYLATION, AND TISSUE SPECIFICITY.
RX PubMed=25908845; DOI=10.1242/jcs.164673;
RA McIntyre J.C., Joiner A.M., Zhang L., Iniguez-Lluhi J., Martens J.R.;
RT "SUMOylation regulates ciliary localization of olfactory signaling
RT proteins.";
RL J. Cell Sci. 128:1934-1945(2015).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling (PubMed:9768837, PubMed:11055432,
CC PubMed:25329148). Participates in signaling cascades triggered by
CC odorant receptors via its function in cAMP biosynthesis
CC (PubMed:9768837, PubMed:11055432). Required for the perception of
CC odorants (PubMed:11055432). Required for normal sperm motility and
CC normal male fertility (PubMed:15705663). Plays a role in regulating
CC insulin levels and body fat accumulation in response to a high fat diet
CC (PubMed:25329148). {ECO:0000269|PubMed:11055432,
CC ECO:0000269|PubMed:15705663, ECO:0000269|PubMed:9768837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148,
CC ECO:0000269|PubMed:9768837};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:P30803};
CC -!- ACTIVITY REGULATION: Activated by forskolin (PubMed:11055432,
CC PubMed:25329148). After forskolin treatment, activity is further
CC increased by calcium/calmodulin. In the absence of forskolin,
CC calcium/calmodulin has little effect on enzyme activity (By
CC similarity). {ECO:0000250|UniProtKB:P21932,
CC ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11055432};
CC Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium
CC {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:9768837}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P21932}. Cytoplasm
CC {ECO:0000250|UniProtKB:O60266}.
CC -!- TISSUE SPECIFICITY: Detected in the acrosomal region of epididymal
CC spermatozoa, the acrosomal region of round spermatids and in elongating
CC spermatids (PubMed:15705663). Detected in cilia in the olfactory
CC epithelium (at protein level) (PubMed:9768837, PubMed:11055432,
CC PubMed:25908845). Detected in olfactory epithelium neurons
CC (PubMed:11055432). Detected in brain, testis, late pachytene
CC spermatocytes, round spermatids and elongating spermatids
CC (PubMed:15705663). {ECO:0000269|PubMed:11055432,
CC ECO:0000269|PubMed:15705663}.
CC -!- DOMAIN: The protein contains two modules with six transmembrane helices
CC each; both are required for catalytic activity. Isolated N-terminal or
CC C-terminal modules have no catalytic activity, but when they are
CC brought together, enzyme activity is restored. The active site is at
CC the interface of the two modules. {ECO:0000250|UniProtKB:P30803}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9768837}.
CC -!- PTM: Rapidly phosphorylated after stimulation by odorants or forskolin.
CC Phosphorylation by CaMK2 at Ser-1077 down-regulates enzyme activity.
CC {ECO:0000269|PubMed:9768837}.
CC -!- PTM: Sumoylated (PubMed:25908845). Sumoylation is required for
CC targeting of olfactory cilia. {ECO:0000250|UniProtKB:P21932,
CC ECO:0000269|PubMed:25908845}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate, but up to 80% of the pups die within 48 h after birth. Survival
CC is improved by paring down the litter size shortly after birth. Mutant
CC mice are initially smaller than wild-type, but achieve normal size
CC within three months. Mutant mice do not display the normal
CC electrophysiological responses to odorants that stimulate production of
CC cAMP or inositoltrisphosphate (IP3). Likewise, behavorial responses to
CC smells are abolished (PubMed:11055432). In spite of normal mating
CC behavior, they do not produce any offspring (PubMed:11055432,
CC PubMed:15705663). Male mice have strongly reduced fertility due to
CC defects in sperm motility, an increased rate of spontaneous acrosome
CC reactions and an impaired ability to penetrate the oocyte zona
CC (PubMed:15705663). {ECO:0000269|PubMed:11055432,
CC ECO:0000269|PubMed:15705663}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF458089; AAL59384.1; -; mRNA.
DR EMBL; CT572999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466623; EDL01374.1; -; Genomic_DNA.
DR CCDS; CCDS25787.1; -.
DR RefSeq; NP_612178.2; NM_138305.3.
DR RefSeq; XP_006514995.1; XM_006514932.2.
DR RefSeq; XP_006514996.1; XM_006514933.2.
DR RefSeq; XP_006514997.1; XM_006514934.3.
DR RefSeq; XP_006514998.1; XM_006514935.3.
DR AlphaFoldDB; Q8VHH7; -.
DR SMR; Q8VHH7; -.
DR BioGRID; 222368; 3.
DR IntAct; Q8VHH7; 1.
DR MINT; Q8VHH7; -.
DR STRING; 10090.ENSMUSP00000122073; -.
DR GlyGen; Q8VHH7; 1 site.
DR iPTMnet; Q8VHH7; -.
DR PhosphoSitePlus; Q8VHH7; -.
DR SwissPalm; Q8VHH7; -.
DR EPD; Q8VHH7; -.
DR MaxQB; Q8VHH7; -.
DR PaxDb; Q8VHH7; -.
DR PRIDE; Q8VHH7; -.
DR ProteomicsDB; 285684; -.
DR Antibodypedia; 4130; 148 antibodies from 26 providers.
DR DNASU; 104111; -.
DR Ensembl; ENSMUST00000020984; ENSMUSP00000020984; ENSMUSG00000020654.
DR Ensembl; ENSMUST00000127756; ENSMUSP00000115406; ENSMUSG00000020654.
DR GeneID; 104111; -.
DR KEGG; mmu:104111; -.
DR UCSC; uc007mxm.2; mouse.
DR CTD; 109; -.
DR MGI; MGI:99675; Adcy3.
DR VEuPathDB; HostDB:ENSMUSG00000020654; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000156549; -.
DR InParanoid; Q8VHH7; -.
DR OMA; MIFIMML; -.
DR OrthoDB; 154265at2759; -.
DR PhylomeDB; Q8VHH7; -.
DR BRENDA; 4.6.1.1; 3474.
DR Reactome; R-MMU-163615; PKA activation.
DR Reactome; R-MMU-170660; Adenylate cyclase activating pathway.
DR Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR BioGRID-ORCS; 104111; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Adcy3; mouse.
DR PRO; PR:Q8VHH7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8VHH7; protein.
DR Bgee; ENSMUSG00000020654; Expressed in gastrula and 242 other tissues.
DR ExpressionAtlas; Q8VHH7; baseline and differential.
DR Genevisible; Q8VHH7; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:ARUK-UCL.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007340; P:acrosome reaction; IMP:UniProtKB.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006171; P:cAMP biosynthetic process; IMP:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; IMP:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008355; P:olfactory learning; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IDA:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR030672; Adcy.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF039050; Ade_cyc; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; cAMP biosynthesis; Cell membrane;
KW Cell projection; Cytoplasm; Glycoprotein; Golgi apparatus; Isopeptide bond;
KW Lyase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Olfaction; Phosphoprotein; Reference proteome; Repeat;
KW Sensory transduction; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1145
FT /note="Adenylate cyclase type 3"
FT /id="PRO_0000195688"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..1145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 504..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 366..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 976
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1063..1065
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1070..1074
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60266"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1077
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:9768837"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000250|UniProtKB:P21932"
FT MUTAGEN 279
FT /note="M->I: In Jll; dominant allele that increases enzyme
FT activity, and decreases fasting insulin levels, fasting
FT leptin levels, weight gain and fat accumulation when mice
FT are kept on a high fat diet."
FT /evidence="ECO:0000269|PubMed:25329148"
FT CONFLICT 152
FT /note="F -> L (in Ref. 1; AAL59384)"
FT /evidence="ECO:0000305"
FT CONFLICT 833..835
FT /note="RLP -> MLL (in Ref. 1; AAL59384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1145 AA; 129085 MW; 09195176F4B3D61F CRC64;
MPRNQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLMV AGFGLVLDII
LFVLCKKGLL PDRVSRKVVP YLLWLLISAQ IFSYLGLNFS RAHAASDTVG WQAFFVFSFF
ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG
IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
YLDEKGIETY LIIASKPEVK KTAQNGLNGS AVPNGAPASS KPSSPALIET KEPNGSAHAS
GSTSEEAEEQ EAQADNPSFP NPRRRLRLQD LADRVVDASE DEHELNQLLN EALLERESAQ
VVKKRNTFLL TMRFMDPEME TRYSVEKEKQ SGAAFSCSCV VLFCTAMVEI LIDPWLMTNY
VTFVVGEVLL LILTICSMAA IFPRSFPKKL VAFSSWIDRT RWARNTWAML AIFILVMANV
VDMLSCLQYY MGPYNMTAGM ELDGGCMENP KYYNYVAVLS LIATIMLVQV SHMVKLTLML
LVTGAVTALN LYAWCPVFDE YDHKRFQEKD SPMVALEKMQ VLATPGLNGT DSRLPLVPSK
YSMTVMMFVM MLSFYYFSRH VEKLARTLFL WKIEVHDQKE RVYEMRRWNE ALVTNMLPEH
VARHFLGSKK RDEELYSQSY DEIGVMFASL PNFADFYTEE SINNGGIECL RFLNEIISDF
DSLLDNPKFR VITKIKTIGS TYMAASGVTP DVNTNGFTSS SKEEKSDKER WQHLADLADF
ALAMKDTLTN INNQSFNNFM LRIGMNKGGV LAGVIGARKP HYDIWGNTVN VASRMESTGV
MGNIQVVEET QVILREYGFR FVRRGPIFVK GKGELLTFFL KGRDRPAAFP NGSSVTLPHQ
VVDNP
