ADCY1_MOUSE
ID ADCY1_MOUSE Reviewed; 1118 AA.
AC O88444; Q5SS89;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Adenylate cyclase type 1;
DE EC=4.6.1.1 {ECO:0000269|PubMed:9662407};
DE AltName: Full=ATP pyrophosphate-lyase 1;
DE AltName: Full=Adenylate cyclase type I;
DE AltName: Full=Adenylyl cyclase 1;
DE AltName: Full=Ca(2+)/calmodulin-activated adenylyl cyclase;
GN Name=Adcy1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-1050, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9662407; DOI=10.1038/980;
RA Abdel-Majid R.M., Leong W.L., Schalkwyk L.C., Smallman D.S., Wong S.T.,
RA Storm D.R., Fine A., Dobson M.J., Guernsey D.L., Neumann P.E.;
RT "Loss of adenylyl cyclase I activity disrupts patterning of mouse
RT somatosensory cortex.";
RL Nat. Genet. 19:289-291(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7816821; DOI=10.1073/pnas.92.1.220;
RA Wu Z.L., Thomas S.A., Villacres E.C., Xia Z., Simmons M.L., Chavkin C.,
RA Palmiter R.D., Storm D.R.;
RT "Altered behavior and long-term potentiation in type I adenylyl cyclase
RT mutant mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:220-224(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, 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 [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24048828; DOI=10.1523/jneurosci.2039-13.2013;
RA Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R.,
RA Iuvone P.M.;
RT "Circadian rhythm of contrast sensitivity is regulated by a dopamine-
RT neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in
RT retinal ganglion cells.";
RL J. Neurosci. 33:14989-14997(2013).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24482543; DOI=10.1093/hmg/ddu042;
RA Santos-Cortez R.L., Lee K., Giese A.P., Ansar M., Amin-Ud-Din M., Rehn K.,
RA Wang X., Aziz A., Chiu I., Hussain Ali R., Smith J.D., Shendure J.,
RA Bamshad M., Nickerson D.A., Ahmed Z.M., Ahmad W., Riazuddin S., Leal S.M.;
RT "Adenylate cyclase 1 (ADCY1) mutations cause recessive hearing impairment
RT in humans and defects in hair cell function and hearing in zebrafish.";
RL Hum. Mol. Genet. 23:3289-3298(2014).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling. Mediates responses to increased
CC cellular Ca(2+)/calmodulin levels (PubMed:9662407, PubMed:7816821). May
CC be involved in regulatory processes in the central nervous system
CC (PubMed:9662407). May play a role in memory and learning
CC (PubMed:7816821). Plays a role in the regulation of the circadian
CC rhythm of daytime contrast sensitivity probably by modulating the
CC rhythmic synthesis of cyclic AMP in the retina (PubMed:24048828).
CC {ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:7816821,
CC ECO:0000269|PubMed:9662407}.
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:9662407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P19754};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P19754};
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 calcium/calmodulin (PubMed:9662407).
CC Activated by forskolin. Activated by the G protein alpha subunit GNAS.
CC Inhibited by the G protein beta and gamma subunit complex. Inhibited by
CC the ATP analogs adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP.
CC {ECO:0000250|UniProtKB:P19754, ECO:0000269|PubMed:9662407}.
CC -!- SUBUNIT: Interacts with CALM. {ECO:0000250|UniProtKB:P19754}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9662407}; Multi-pass
CC membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P19754}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19754}. Cytoplasm
CC {ECO:0000269|PubMed:24482543}. Membrane raft
CC {ECO:0000250|UniProtKB:P19754}. Note=Expressed in the cytoplasm of
CC supporting cells and hair cells of the cochlea vestibule, as well as to
CC the cochlear hair cell nuclei and stereocilia|.
CC {ECO:0000269|PubMed:24482543}.
CC -!- TISSUE SPECIFICITY: Expressed throughout inner ear development.
CC {ECO:0000269|PubMed:24482543}.
CC -!- INDUCTION: Expression in the retina oscillates in a circadian manner.
CC {ECO:0000269|PubMed:24048828}.
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:0000250|UniProtKB:P19754}.
CC -!- DISRUPTION PHENOTYPE: Mice appear grossly normal and healthy, but have
CC decreased levels of calmodulin-sensitive adenylyl cyclase activity in
CC the brain (PubMed:7816821). They show impaired spatial memory
CC (PubMed:7816821). Mice show a significant reduction in daytime contrast
CC sensitivity (PubMed:24048828). {ECO:0000269|PubMed:24048828,
CC ECO:0000269|PubMed:7816821}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AL669838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF053980; AAC29478.1; -; mRNA.
DR CCDS; CCDS24426.1; -.
DR RefSeq; NP_033752.1; NM_009622.1.
DR AlphaFoldDB; O88444; -.
DR SMR; O88444; -.
DR BioGRID; 240661; 1.
DR STRING; 10090.ENSMUSP00000020706; -.
DR GlyGen; O88444; 1 site.
DR iPTMnet; O88444; -.
DR PhosphoSitePlus; O88444; -.
DR SwissPalm; O88444; -.
DR MaxQB; O88444; -.
DR PaxDb; O88444; -.
DR PeptideAtlas; O88444; -.
DR PRIDE; O88444; -.
DR ProteomicsDB; 285683; -.
DR Antibodypedia; 4335; 251 antibodies from 29 providers.
DR Ensembl; ENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431.
DR GeneID; 432530; -.
DR KEGG; mmu:432530; -.
DR UCSC; uc007hzf.1; mouse.
DR CTD; 107; -.
DR MGI; MGI:99677; Adcy1.
DR VEuPathDB; HostDB:ENSMUSG00000020431; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000154872; -.
DR HOGENOM; CLU_001072_2_1_1; -.
DR InParanoid; O88444; -.
DR OMA; ERRMCPY; -.
DR OrthoDB; 594476at2759; -.
DR PhylomeDB; O88444; -.
DR TreeFam; TF313845; -.
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; 432530; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adcy1; mouse.
DR PRO; PR:O88444; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88444; protein.
DR Bgee; ENSMUSG00000020431; Expressed in cerebellum lobe and 211 other tissues.
DR Genevisible; O88444; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IMP:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0004016; F:adenylate cyclase activity; IGI:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0150076; P:neuroinflammatory response; IMP:UniProtKB.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; Biological rhythms; Calmodulin-binding; cAMP biosynthesis;
KW Cell membrane; Cytoplasm; Glycoprotein; Lyase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1118
FT /note="Adenylate cyclase type 1"
FT /id="PRO_0000195683"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..519
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT REGION 1023..1046
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT REGION 1079..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 307..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 307
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 307
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 308
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 349..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 351
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 351
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 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 919
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 996..998
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1003..1007
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1043
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 147..155
FT /note="SSAGGAMGS -> ALQEAQWAR (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="T -> A (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="L -> M (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="T -> K (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="R -> K (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="F -> I (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="S -> T (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="S -> T (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="R -> L (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="Q -> R (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="G -> V (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="A -> S (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="V -> L (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="G -> C (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 720..721
FT /note="AL -> GP (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 774..776
FT /note="VGG -> AMGA (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 867..869
FT /note="GVM -> AVL (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="R -> K (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="R -> C (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="T -> I (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="C -> S (in Ref. 2; AAC29478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1118 AA; 123373 MW; CEFAFF3940B22277 CRC64;
MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG YTLRLEQAAT
LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL FLALFVVTNV RSLQVSQLQQ
VGQLALFFSL TFALLCCPFA LGGPARSSAG GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS
LLAIGFGLVV AASHLLVTAA LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK
AFLQARNCIE DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN
VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG DCYYCVSGLT
QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT GRVLCGVLGL RKWQYDVWSN
DVTLANVMEA AGLPGKVHIT KTTLACLNGD YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR
RKIFPGLILS DIKPAKRMKF KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT
ASEKLRNRSS FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY
HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC TLYLHITRVQ
CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS QSNSSLVVLA AGGRRTVLPA
LPCESAHHAL LCCLVGTLPL AIFLRVSSLP KMILLSGLTT SYILVLELSG YTKVGGGALS
GRSYEPIMAI LLFSCTLALH ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL
PAHVAQHFLM SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII
ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL ADFAIDMFDV
LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN TVNVASRMDS TGVQGRIQVT
EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG
GQARRPPLCP AAGPPVRPGL PPAPTSQYLS STAAGKEA
