ADCY7_MOUSE
ID ADCY7_MOUSE Reviewed; 1099 AA.
AC P51829; Q3U3P2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Adenylate cyclase type 7 {ECO:0000305};
DE EC=4.6.1.1 {ECO:0000305|PubMed:23229509};
DE AltName: Full=ATP pyrophosphate-lyase 7;
DE AltName: Full=Adenylate cyclase type VII;
DE AltName: Full=Adenylyl cyclase 7;
GN Name=Adcy7 {ECO:0000312|MGI:MGI:102891};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Lymphoma;
RX PubMed=7961850; DOI=10.1016/s0021-9258(19)61991-5;
RA Watson P.A., Krupinski J., Kempinski A.M., Frankenfield C.D.;
RT "Molecular cloning and characterization of the type VII isoform of
RT mammalian adenylyl cyclase expressed widely in mouse tissues and in S49
RT mouse lymphoma cells.";
RL J. Biol. Chem. 269:28893-28898(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=18205980; DOI=10.1017/s1461145707008395;
RA Mann L., Heldman E., Shaltiel G., Belmaker R.H., Agam G.;
RT "Lithium preferentially inhibits adenylyl cyclase V and VII isoforms.";
RL Int. J. Neuropsychopharmacol. 11:533-539(2008).
RN [4]
RP FUNCTION.
RX PubMed=18541530; DOI=10.1074/jbc.m803281200;
RA Jiang L.I., Collins J., Davis R., Fraser I.D., Sternweis P.C.;
RT "Regulation of cAMP responses by the G12/13 pathway converges on adenylyl
RT cyclase VII.";
RL J. Biol. Chem. 283:23429-23439(2008).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20505140; DOI=10.4049/jimmunol.0903474;
RA Duan B., Davis R., Sadat E.L., Collins J., Sternweis P.C., Yuan D.,
RA Jiang L.I.;
RT "Distinct roles of adenylyl cyclase VII in regulating the immune responses
RT in mice.";
RL J. Immunol. 185:335-344(2010).
RN [6]
RP FUNCTION.
RX PubMed=23178822; DOI=10.1016/j.molimm.2012.10.027;
RA Jiang L.I., Sternweis P.C., Wang J.E.;
RT "Zymosan activates protein kinase A via adenylyl cyclase VII to modulate
RT innate immune responses during inflammation.";
RL Mol. Immunol. 54:14-22(2013).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23229509; DOI=10.1124/mol.112.082446;
RA Jiang L.I., Wang J.E., Sternweis P.C.;
RT "Regions on adenylyl cyclase VII required for selective regulation by the
RT G13 pathway.";
RL Mol. Pharmacol. 83:587-593(2013).
CC -!- FUNCTION: Catalyzes the formation of cAMP in response to activation of
CC G protein-coupled receptors (Probable). Functions in signaling cascades
CC activated namely by thrombin and sphingosine 1-phosphate and mediates
CC regulation of cAMP synthesis through synergistic action of the
CC stimulatory G alpha protein with GNA13 (PubMed:18541530). Also, during
CC inflammation, mediates zymosan-induced increase intracellular cAMP,
CC leading to protein kinase A pathway activation in order to modulate
CC innate immune responses through heterotrimeric G proteins G(12/13)
CC (PubMed:23178822). Functions in signaling cascades activated namely by
CC dopamine and C5 alpha chain and mediates regulation of cAMP synthesis
CC through synergistic action of the stimulatory G protein with G
CC beta:gamma complex (By similarity). Functions, through cAMP response
CC regulation, to keep inflammation under control during bacterial
CC infection by sensing the presence of serum factors, such as the
CC bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha
CC production. However, it is also required for the optimal functions of B
CC and T cells during adaptive immune responses by regulating cAMP
CC synthesis in both B and T cells (PubMed:20505140).
CC {ECO:0000250|UniProtKB:P51828, ECO:0000269|PubMed:18541530,
CC ECO:0000269|PubMed:20505140, ECO:0000269|PubMed:23178822,
CC ECO:0000305|PubMed:18541530, ECO:0000305|PubMed:23178822,
CC ECO:0000305|PubMed:23229509}.
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:0000305|PubMed:23229509};
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 the G protein alpha subunit.
CC Activated by the G protein beta and gamma subunit complex. Activated by
CC GNA13 and GNA12. Ethanol and phorbol 12,13-dibutanoate significantly
CC potentiate adenylate cyclase activity generated in response to the
CC activation of the prostanoid receptor by the agonist prostaglandin
CC E1(1-) in a PKC-dependent manner (By similarity). Inhibited by lithium
CC (PubMed:18205980). {ECO:0000250|UniProtKB:P51828,
CC ECO:0000269|PubMed:18205980}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundant in heart, spleen and lung.
CC {ECO:0000269|PubMed:7961850}.
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 guanylate cyclase domains have no catalytic activity, but
CC when they are brought together, enzyme activity is restored. The active
CC site is at the interface of the two domains. Both contribute substrate-
CC binding residues, but the catalytic metal ions are bound exclusively
CC via the N-terminal guanylate cyclase domain.
CC {ECO:0000250|UniProtKB:P26769}.
CC -!- PTM: Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:P51828}.
CC -!- DISRUPTION PHENOTYPE: Knockout Adcy7 homozygous mice die during
CC embryogenesis (more than 93%). To obtain adult animals with Adcy7-
CC deficient immune systems, the hematopoietic stem cells obtained from
CC the rare adult Adcy7 homozygous mice are transplanted into lethally
CC irradiated wild-type animals. All chimeric mice survived the transplant
CC procedure and appeared healthy. Adcy7-deficient mice appear to be
CC hypersensitive to lipopolysaccharide-induced endotoxic shock and
CC display a higher mortality rate. {ECO:0000269|PubMed:20505140}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; U12919; AAA57554.1; -; mRNA.
DR EMBL; AK154652; BAE32743.1; -; mRNA.
DR CCDS; CCDS22509.1; -.
DR PIR; A55405; A55405.
DR RefSeq; NP_001032812.2; NM_001037723.3.
DR RefSeq; NP_001032813.1; NM_001037724.4.
DR RefSeq; NP_001103226.1; NM_001109756.1.
DR RefSeq; NP_031432.2; NM_007406.2.
DR AlphaFoldDB; P51829; -.
DR SMR; P51829; -.
DR BioGRID; 197976; 3.
DR STRING; 10090.ENSMUSP00000130594; -.
DR GlyGen; P51829; 1 site.
DR iPTMnet; P51829; -.
DR PhosphoSitePlus; P51829; -.
DR SwissPalm; P51829; -.
DR EPD; P51829; -.
DR MaxQB; P51829; -.
DR PaxDb; P51829; -.
DR PeptideAtlas; P51829; -.
DR PRIDE; P51829; -.
DR ProteomicsDB; 285764; -.
DR Antibodypedia; 28237; 169 antibodies from 28 providers.
DR DNASU; 11513; -.
DR Ensembl; ENSMUST00000098521; ENSMUSP00000096122; ENSMUSG00000031659.
DR Ensembl; ENSMUST00000168545; ENSMUSP00000129252; ENSMUSG00000031659.
DR Ensembl; ENSMUST00000169037; ENSMUSP00000130594; ENSMUSG00000031659.
DR Ensembl; ENSMUST00000171456; ENSMUSP00000132528; ENSMUSG00000031659.
DR GeneID; 11513; -.
DR KEGG; mmu:11513; -.
DR UCSC; uc009mrh.2; mouse.
DR CTD; 113; -.
DR MGI; MGI:102891; Adcy7.
DR VEuPathDB; HostDB:ENSMUSG00000031659; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000159096; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR InParanoid; P51829; -.
DR OMA; PRSKQCL; -.
DR OrthoDB; 363718at2759; -.
DR PhylomeDB; P51829; -.
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; 11513; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Adcy7; mouse.
DR PRO; PR:P51829; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P51829; protein.
DR Bgee; ENSMUSG00000031659; Expressed in peripheral lymph node and 244 other tissues.
DR ExpressionAtlas; P51829; baseline and differential.
DR Genevisible; P51829; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP 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; ISO:MGI.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISO:MGI.
DR GO; GO:0071361; P:cellular response to ethanol; ISS:UniProtKB.
DR GO; GO:0071285; P:cellular response to lithium ion; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0002819; P:regulation of adaptive immune response; 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; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; DUF1053; 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; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1099
FT /note="Adenylate cyclase type 7"
FT /id="PRO_0000195704"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..1099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..484
FT /note="Mediates regulation of adenylate cyclase activity by
FT C5 alpha-induced G- beta and gamma pathway"
FT /evidence="ECO:0000250|UniProtKB:P51828"
FT REGION 493..501
FT /note="Mediates regulation of adenylate cyclase activity by
FT sphingosine 1-phosphate-induced G alpha 13 pathway"
FT /evidence="ECO:0000250|UniProtKB:P51828"
FT REGION 504..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..585
FT /note="Modulates adenylate cyclase activity by modulating
FT the binding of G(s)alpha to the high-affinity G(s)alpha
FT binding site in 7C1a/7C2"
FT /evidence="ECO:0000250|UniProtKB:P51828"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 286
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 286
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 287
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 328..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 330
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 330
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 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 950
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1029..1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1036..1040
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1076
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 150
FT /note="A -> V (in Ref. 1; AAA57554)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="C -> Y (in Ref. 1; AAA57554)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="R -> Q (in Ref. 1; AAA57554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1099 AA; 122708 MW; 0EE189EA9070FF73 CRC64;
MPAKGRYFLN EGDEGPDQAA LYEKYRLTSL HGPLLLLLLL VAAATCIALI SIAFSHEDLR
RHQVVLGTAF LMLTLFVALY VLVYVECLVQ RWLRALALLT WACLMVLGSV LMWDSLENEA
HAWEQVPFFL FVVFVVYALL PLSRRAAIVA GVTSTVSHLL VFGAVTRAFQ TSMSSTQLGL
QLLANAVILL GGNFTGAFHK HQLQDASRDL FIYTVKCIQI RRKLRVEKRQ QENLLLSVLP
AHISMGMKLA IIERLKEGGD RHYMPDNNFH SLYVKRHQNV SILYADIVGF TRLASDCSPK
ELVVVLNELF GKFDQIAKAN ECMRIKILGD CYYCVSGLPV SLPTHARNCV KMGLDICEAI
KQVREATGVD ISMRVGIHSG NVLCGVIGLR KWQYDVWSHD VSLANRMEAA GVPGRVHITE
ATLNHLDKAY EVEDGHGEQR DPYLKEMNIR TYLVIDPRSQ QPPPPSHHLS KPKGDATLKM
RASVRVTRYL ESWGAARPFA HLNHRESVSS SETPISNGRR QKAIPLRRHR APDRSASPKG
RLEDDCDDEM LSAIEGLSST RPCCSKSDDF HTFGPIFLEK GFEREYRLVP IPRARYDFAC
ASLVFVCILL VHLLVMPRMA TLGVSFGLVA CLLGLVLSFC FATEFSRCFP SRSTLQAISE
SVETQPLVRL VLVVLTVGSL LTVAIINMPL TLNPGPEQPG DNKTSPLAAQ NRVGTPCELL
PYYTCSCILG FIACSVFLRM SLELKAMLLT VALVAYLLLF NLSPCWHVSG NSTETNGTQR
TRLLLSDAQS MPSHTLAPGA RETAPSPSYL ERDLKIMVNF YLILFYATLI LLSRQIDYYC
RLDCLWKKKF KKEHEEFETM ENVNRLLLEN VLPAHVAAHF IGDKAAEDWY HQSYDCVCVM
FASVPDFKVF YTECDVNKEG LECLRLLNEI IADFDELLLK PKFSGVEKIK TIGSTYMAAA
GLSAPSGHEN QDLERKHVHI GVLVEFSMAL MSKLDGINRH SFNSFRLRVG INHGPVIAGV
IGARKPQYDI WGNTVNVASR MESTGELGKI QVTEETCTIL QGLGYSCECR GLINVKGKGE
LRTYFVCTDT AKFQGLGLN
