ADCYA_MOUSE
ID ADCYA_MOUSE Reviewed; 1614 AA.
AC Q8C0T9; B2RRJ9; Q3V0F8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Adenylate cyclase type 10;
DE EC=4.6.1.1;
DE AltName: Full=Germ cell soluble adenylyl cyclase;
DE Short=sAC;
DE AltName: Full=Testicular soluble adenylyl cyclase;
GN Name=Adcy10; Synonyms=Sac, Sacy;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ALTERNATIVE SPLICING.
RX PubMed=11423534; DOI=10.1074/jbc.m011698200;
RA Jaiswal B.S., Conti M.;
RT "Identification and functional analysis of splice variants of the germ cell
RT soluble adenylyl cyclase.";
RL J. Biol. Chem. 276:31698-31708(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12475901; DOI=10.1096/fj.02-0598fje;
RA Zippin J.H., Chen Y., Nahirney P., Kamenetsky M., Wuttke M.S.,
RA Fischman D.A., Levin L.R., Buck J.;
RT "Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct
RT signaling microdomains.";
RL FASEB J. 17:82-84(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14976244; DOI=10.1073/pnas.0400050101;
RA Esposito G., Jaiswal B.S., Xie F., Krajnc-Franken M.A.M., Robben T.J.A.A.,
RA Strik A.M., Kuil C., Philipsen R.L.A., van Duin M., Conti M., Gossen J.A.;
RT "Mice deficient for soluble adenylyl cyclase are infertile because of a
RT severe sperm-motility defect.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2993-2998(2004).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16054031; DOI=10.1016/j.devcel.2005.06.007;
RA Hess K.C., Jones B.H., Marquez B., Chen Y., Ord T.S., Kamenetsky M.,
RA Miyamoto C., Zippin J.H., Kopf G.S., Suarez S.S., Levin L.R.,
RA Williams C.J., Buck J., Moss S.B.;
RT "The 'soluble' adenylyl cyclase in sperm mediates multiple signaling events
RT required for fertilization.";
RL Dev. Cell 9:249-259(2005).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP. May
CC function as sensor that mediates responses to changes in cellular
CC bicarbonate and CO(2) levels (By similarity). Has a critical role in
CC mammalian spermatogenesis by producing the cAMP which regulates cAMP-
CC responsive nuclear factors indispensable for sperm maturation in the
CC epididymis. Induces capacitation, the maturational process that sperm
CC undergo prior to fertilization (PubMed:14976244, PubMed:16054031).
CC Involved in ciliary beat regulation (By similarity).
CC {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244,
CC ECO:0000269|PubMed:16054031}.
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:0000250|UniProtKB:Q96PN6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:Q96PN6};
CC -!- ACTIVITY REGULATION: Activated by manganese or magnesium ions. In the
CC presence of magnesium ions, the enzyme is activated by bicarbonate.
CC Calcium mildly increases the enzyme activity, also in the presence of
CC magnesium ions. {ECO:0000250|UniProtKB:Q96PN6}.
CC -!- INTERACTION:
CC Q8C0T9; Q6UJY2: Slc9c1; NbExp=2; IntAct=EBI-15639026, EBI-15639080;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PN6};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}.
CC Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm
CC {ECO:0000269|PubMed:12475901}. Mitochondrion
CC {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular
CC compartments containing cAMP targets. Found as a plasma membrane-
CC associated protein, protein concentrated in the perinuclear region and
CC protein colocalized with actin or tubulin.
CC {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0T9-2; Sequence=VSP_030871, VSP_030872;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16054031}.
CC -!- DOMAIN: The N-terminal guanylate cyclase domains are required for
CC enzyme activity. Fragments containing the first 470 amino acid residues
CC are fully active. {ECO:0000250|UniProtKB:Q96PN6}.
CC -!- DISRUPTION PHENOTYPE: Mice are infertile because of a severe sperm-
CC motility defect. {ECO:0000269|PubMed:14976244}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AK029849; BAC26642.1; -; mRNA.
DR EMBL; AK133181; BAE21546.1; -; mRNA.
DR EMBL; BC138448; AAI38449.1; -; mRNA.
DR CCDS; CCDS35756.1; -. [Q8C0T9-1]
DR RefSeq; NP_766617.2; NM_173029.3. [Q8C0T9-1]
DR RefSeq; XP_006496930.1; XM_006496867.1. [Q8C0T9-1]
DR RefSeq; XP_017176545.1; XM_017321056.1. [Q8C0T9-1]
DR AlphaFoldDB; Q8C0T9; -.
DR SMR; Q8C0T9; -.
DR BioGRID; 234845; 3.
DR DIP; DIP-60950N; -.
DR IntAct; Q8C0T9; 1.
DR STRING; 10090.ENSMUSP00000027852; -.
DR iPTMnet; Q8C0T9; -.
DR PhosphoSitePlus; Q8C0T9; -.
DR PaxDb; Q8C0T9; -.
DR PRIDE; Q8C0T9; -.
DR ProteomicsDB; 285765; -. [Q8C0T9-1]
DR ProteomicsDB; 285766; -. [Q8C0T9-2]
DR Antibodypedia; 3017; 147 antibodies from 23 providers.
DR DNASU; 271639; -.
DR Ensembl; ENSMUST00000027852; ENSMUSP00000027852; ENSMUSG00000026567. [Q8C0T9-1]
DR Ensembl; ENSMUST00000148550; ENSMUSP00000137959; ENSMUSG00000026567. [Q8C0T9-2]
DR GeneID; 271639; -.
DR KEGG; mmu:271639; -.
DR UCSC; uc007djf.1; mouse. [Q8C0T9-1]
DR CTD; 55811; -.
DR MGI; MGI:2660854; Adcy10.
DR VEuPathDB; HostDB:ENSMUSG00000026567; -.
DR eggNOG; ENOG502QPPT; Eukaryota.
DR GeneTree; ENSGT00390000001322; -.
DR HOGENOM; CLU_047661_0_0_1; -.
DR InParanoid; Q8C0T9; -.
DR OMA; TVDIRLN; -.
DR OrthoDB; 37924at2759; -.
DR PhylomeDB; Q8C0T9; -.
DR TreeFam; TF329284; -.
DR BRENDA; 4.6.1.1; 3474.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR BioGRID-ORCS; 271639; 0 hits in 60 CRISPR screens.
DR PRO; PR:Q8C0T9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C0T9; protein.
DR Bgee; ENSMUSG00000026567; Expressed in spermatid and 26 other tissues.
DR ExpressionAtlas; Q8C0T9; baseline and differential.
DR Genevisible; Q8C0T9; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0045178; C:basal part of cell; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0071890; F:bicarbonate binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; ISS:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR016577; Adenylate_cyclase_typ10.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF011131; Soluble_adenylyl_cyclase; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Lyase; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1614
FT /note="Adenylate cyclase type 10"
FT /id="PRO_0000317102"
FT DOMAIN 42..179
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 293..418
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 47..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 95
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 167
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 176
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 337
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT VAR_SEQ 470..471
FT /note="MF -> TC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030871"
FT VAR_SEQ 472..1614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030872"
FT CONFLICT 304
FT /note="Q -> H (in Ref. 1; BAC26642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="I -> V (in Ref. 1; BAC26642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1614 AA; 186412 MW; AE56433825277126 CRC64;
MSARRQELQD RAIVKIAAHL PDLIVYGDFS PERPSVKCFD GVLMFVDISG FTAMTEKFST
AMYMDRGAEQ LVEILNYYIS AIVEKVLIFG GDILKFAGDA LLALWKVERK QLKNIITVVI
KCSLEIHGLF EAKEAEEGLD IRVKIGLAAG HITMLVFGDE TRNYFLVIGQ AVDDVRLAQN
MAQMNDVILS PNCWQLCDRS MIEIERIPDQ RAVKVSFLKP PPTFNFDEFF TKCMGFMDYY
PSGDHKNFLR LACMLESDPE LELSLQKYVM EIILKQIDDK QLRGYLSELR PVTIVFVNLM
FKEQDKVEVI GSAIQAACVH ITSVLKVFRG QINKVFMFDK GCSFLCVFGF PGEKAPDEIT
HALESAVDIF DFCSQVHKIR TVSIGVASGI VFCGIVGHTV RHEYTVIGQK VNIAARMMMY
YPGIVSCDSV TYDGSNLPAY FFKELPKKVM KGVADPGPVY QCLGLNEKVM FGMAYLICNR
YEGYPLLGRV REIDYFMSTM KDFLMTNCSR VLMYEGLPGY GKSQVLMEIE YLASQHENHR
AVAIALTKIS FHQNFYTIQI LMANVLGLDT CKHYKERQTN LQNRVKTLLD EKFHCLLNDI
FHVQFPVSRE MSRMSKIRKQ KQLEALFMKI LAQTVREERI IFIIDEAQFV DGTSWAFIEK
LIRSMPIFIV MSLAPFSEVP CAAANAIMKN RNTTYITLGT MQPQEIRDKV CVDLSVSSIP
RELDSYLVEG SCGIPYYCEE LLKNLDHHRV LLFQQAETEQ KTNVTWNNMF KHSVRPTDDM
QLFTSISEGQ KEVCYLVSGV RLNNLSPPAS LKEISLVQLD SMSLSHQMLV RCAAIIGLTF
TTELLFEILP CWNMKMMIKA LATLVESNVF NCFRSSKDLQ LALKQNVPTF EVHYRSLALK
LKEGLTYGEE EELREMEGEV VECRILRFCR PIMQKTAYEL WLKDQKKVLH LKCARFLEES
AHRCNHCRNV DFIPYHHFIV DIRLNTLDMD TVKRMVTSQG FKIDEEEAIF SKSELPRKYK
FPENLSITEI REKILHFFDN VILKMKSSPN DIIPLESCQC KELLQIVILP LAQHFVALEE
NNKALYYFLE LASAYLILGD NYNAYMYLGE GERLLKSLTN EDSWSQTFEY ATFYSLKAEV
CFNMGQMVLA KKMLRKALKL LNRMFPCNLL TLTFQMHVEK NRLSHFMNQH TQEGSVPGKK
LAQLYLQASC FSLLWRIYSL NFFFHYKYYG HLAAMMEMNT SLETQNDFQI IKAYLDFSLY
HHLAGYQGVW FKYEILVMEQ LLNLPLKGEA IEIMAYTADT LGHIKFLMGH LDLAIELGSR
AHRMWSLLRN PNKYQMVLCR LSKPLFLKSR YKHLVQVLGW LWDLSVTEED IFSKAFFYFV
CLDIMLYSGF IYRTFEECLE FIHHNEDNRI LKFQSGLLLG LYSCIAVWYA RLQEWDNFNK
FSDRAKHLVT RRTPTVLYYE GISRYMEGQV LHLQKQIEEQ AENAQDSGVE ILKALETLVA
QNTTGPVFYP RLYHLMAYVC ILMGDGHSCD FFLNTALELS ETHGNLLEKC WLSMSKEWWY
SASELTGDQW LQTVLSLPSW DKIVSGKGGQ RKRSWSWFCP PNFSMVSWSQ PQCA
