ADCYA_HUMAN
ID ADCYA_HUMAN Reviewed; 1610 AA.
AC Q96PN6; B4DZF0; F5GWS5; O95558; Q5R329; Q5R330; Q8WXV4; Q9NNX0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Adenylate cyclase type 10;
DE EC=4.6.1.1 {ECO:0000269|PubMed:12609998, ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449, ECO:0000269|PubMed:25040695};
DE AltName: Full=AH-related protein;
DE AltName: Full=Adenylate cyclase homolog;
DE AltName: Full=Germ cell soluble adenylyl cyclase {ECO:0000303|PubMed:11423534};
DE Short=hsAC;
DE Short=sAC {ECO:0000303|PubMed:12609998, ECO:0000303|PubMed:25040695};
DE AltName: Full=Testicular soluble adenylyl cyclase;
GN Name=ADCY10; Synonyms=SAC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-697.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INVOLVEMENT IN
RP HCA2, AND VARIANT VAL-697.
RC TISSUE=Intestine;
RX PubMed=11932268; DOI=10.1210/jcem.87.4.8300;
RA Reed B.Y., Gitomer W.L., Heller H.J., Hsu M.C., Lemke M., Padalino P.,
RA Pak C.Y.C.;
RT "Identification and characterization of a gene with base substitutions
RT associated with the absorptive hypercalciuria phenotype and low spinal bone
RT density.";
RL J. Clin. Endocrinol. Metab. 87:1476-1485(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND VARIANT VAL-697.
RX PubMed=12609998; DOI=10.1074/jbc.m212475200;
RA Litvin T.N., Kamenetsky M., Zarifyan A., Buck J., Levin L.R.;
RT "Kinetic properties of 'soluble' adenylyl cyclase. Synergism between
RT calcium and bicarbonate.";
RL J. Biol. Chem. 278:15922-15926(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Khole V.V., Westbrook V.A., Mandal A., Herr J.C., Visconti P.E.;
RT "Cloning of a human testicular soluble adenylyl cyclase.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [10]
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 [11]
RP CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15659711; DOI=10.1152/ajpcell.00584.2004;
RA Geng W., Wang Z., Zhang J., Reed B.Y., Pak C.Y.C., Moe O.W.;
RT "Cloning and characterization of the human soluble adenylyl cyclase.";
RL Am. J. Physiol. 288:C1305-C1316(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17591988; DOI=10.1085/jgp.200709784;
RA Schmid A., Sutto Z., Nlend M.-C., Horvath G., Schmid N., Buck J.,
RA Levin L.R., Conner G.E., Fregien N., Salathe M.;
RT "Soluble adenylyl cyclase is localized to cilia and contributes to ciliary
RT beat frequency regulation via production of cAMP.";
RL J. Gen. Physiol. 130:99-109(2007).
RN [13] {ECO:0007744|PDB:4OYA, ECO:0007744|PDB:4OYB, ECO:0007744|PDB:4OYI}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH
RP HYDROGENCARBONATE; CALCIUM AND ATP ANALOG, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, AND DOMAIN.
RX PubMed=24616449; DOI=10.1002/cmdc.201300480;
RA Saalau-Bethell S.M., Berdini V., Cleasby A., Congreve M., Coyle J.E.,
RA Lock V., Murray C.W., O'Brien M.A., Rich S.J., Sambrook T., Vinkovic M.,
RA Yon J.R., Jhoti H.;
RT "Crystal structure of human soluble adenylate cyclase reveals a distinct,
RT highly flexible allosteric bicarbonate binding pocket.";
RL ChemMedChem 9:823-832(2014).
RN [14] {ECO:0007744|PDB:4UST, ECO:0007744|PDB:4USU, ECO:0007744|PDB:4USV}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-469 IN COMPLEXES WITH
RP MAGNESIUM; CALCIUM; ATP AND ATP ANALOGS, FUNCTION, COFACTOR, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=25040695; DOI=10.1111/febs.12913;
RA Kleinboelting S., van den Heuvel J., Steegborn C.;
RT "Structural analysis of human soluble adenylyl cyclase and crystal
RT structures of its nucleotide complexes-implications for cyclase catalysis
RT and evolution.";
RL FEBS J. 281:4151-4164(2014).
RN [15] {ECO:0007744|PDB:4CLF, ECO:0007744|PDB:4CLK, ECO:0007744|PDB:4CLL}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH CALCIUM;
RP HYDROGENCARBONATE AND ATP ANALOGS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION,
RP ACTIVITY REGULATION, MUTAGENESIS OF LYS-95 AND ARG-176, AND DOMAIN.
RX PubMed=24567411; DOI=10.1073/pnas.1322778111;
RA Kleinboelting S., Diaz A., Moniot S., van den Heuvel J., Weyand M.,
RA Levin L.R., Buck J., Steegborn C.;
RT "Crystal structures of human soluble adenylyl cyclase reveal mechanisms of
RT catalysis and of its activation through bicarbonate.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3727-3732(2014).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
CC (PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695,
CC PubMed:24567411). May function as sensor that mediates responses to
CC changes in cellular bicarbonate and CO(2) levels (PubMed:15659711,
CC PubMed:17591988). Has a critical role in mammalian spermatogenesis by
CC producing the cAMP which regulates cAMP-responsive nuclear factors
CC indispensable for sperm maturation in the epididymis. Induces
CC capacitation, the maturational process that sperm undergo prior to
CC fertilization (By similarity). Involved in ciliary beat regulation
CC (PubMed:17591988). {ECO:0000250|UniProtKB:Q8C0T9,
CC ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988,
CC ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449,
CC ECO:0000269|PubMed:25040695}.
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:12609998, ECO:0000269|PubMed:15659711,
CC ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449,
CC ECO:0000269|PubMed:25040695};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12609998, ECO:0000269|PubMed:15659711,
CC ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:25040695,
CC ECO:0000305|PubMed:24616449};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12609998, ECO:0000269|PubMed:15659711,
CC ECO:0000269|PubMed:24616449};
CC Note=Binds 2 magnesium ions per subunit (PubMed:25040695). Is also
CC active with manganese (in vitro) (PubMed:12609998, PubMed:15659711,
CC PubMed:24616449). {ECO:0000269|PubMed:12609998,
CC ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:24616449,
CC ECO:0000305|PubMed:25040695};
CC -!- ACTIVITY REGULATION: Activated by manganese or magnesium ions
CC (PubMed:12609998, PubMed:24616449). In the presence of magnesium ions,
CC the enzyme is activated by bicarbonate (PubMed:12609998,
CC PubMed:15659711, PubMed:24567411). In the presence of manganese ions,
CC the enzyme is inhibited by bicarbonate (PubMed:15659711). In the
CC absence of magnesium and bicarbonate, the enzyme is weakly activated by
CC calcium (PubMed:15659711). Calcium mildly increases the enzyme
CC activity, also in the presence of magnesium ions (PubMed:15659711,
CC PubMed:25040695). {ECO:0000269|PubMed:12609998,
CC ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:24567411,
CC ECO:0000269|PubMed:24616449, ECO:0000269|PubMed:25040695}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for ATP-Mn(2+) {ECO:0000269|PubMed:12609998};
CC KM=2.41 mM for Mg(2+) {ECO:0000269|PubMed:12609998};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15659711};
CC Peripheral membrane protein {ECO:0000269|PubMed:15659711}; Cytoplasmic
CC side {ECO:0000269|PubMed:15659711}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:12475901,
CC ECO:0000269|PubMed:15659711}. Nucleus {ECO:0000269|PubMed:12475901,
CC ECO:0000269|PubMed:15659711}. Cell projection, cilium
CC {ECO:0000269|PubMed:17591988}. Cytoplasm {ECO:0000269|PubMed:12475901}.
CC Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to
CC subcellular compartments containing cAMP targets. Found as a plasma
CC membrane-associated protein, protein concentrated in the perinuclear
CC region and protein colocalized with actin or tubulin.
CC {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96PN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PN6-2; Sequence=VSP_030867;
CC Name=3;
CC IsoId=Q96PN6-3; Sequence=VSP_030866, VSP_030868, VSP_030869,
CC VSP_030870;
CC Name=4;
CC IsoId=Q96PN6-4; Sequence=VSP_046329;
CC -!- TISSUE SPECIFICITY: Detected in airway epithelial cells and testis (at
CC protein level) (PubMed:17591988). Weakly expressed in multiple tissues.
CC Expressed in brain, heart, kidney, liver, lung, pancreas, peripheral
CC blood leukocytes, placenta, skeletal muscle, stomach, thymus, airway
CC epithelial cells, duodenum, jejunum and ileum. Very low level of
CC expression in bone. {ECO:0000269|PubMed:11932268,
CC ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988}.
CC -!- DOMAIN: The N-terminal guanylate cyclase domains are required for
CC enzyme activity. Fragments or isoforms containing the first 470 amino
CC acid residues are fully active. {ECO:0000269|PubMed:24567411,
CC ECO:0000269|PubMed:24616449, ECO:0000269|PubMed:25040695}.
CC -!- PTM: Cleavage may occur to generate the active 48 kDa form.
CC {ECO:0000305}.
CC -!- DISEASE: Hypercalciuria absorptive 2 (HCA2) [MIM:143870]: A common type
CC of hypercalciuria, a condition characterized by excessive urinary
CC calcium excretion. Absorptive hypercalciuria is due to gastrointestinal
CC hyperabsorption of calcium and is a frequent cause of calcium oxalate
CC nephrolithiasis. {ECO:0000269|PubMed:11932268}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF271058; AAF74296.1; -; mRNA.
DR EMBL; AF331033; AAL57036.1; -; mRNA.
DR EMBL; AF176813; AAF65931.1; -; mRNA.
DR EMBL; AF299350; AAK96045.1; -; mRNA.
DR EMBL; AL035122; CAA22684.1; -; mRNA.
DR EMBL; AK302884; BAG64062.1; -; mRNA.
DR EMBL; Z97876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90804.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90807.1; -; Genomic_DNA.
DR EMBL; BC117366; AAI17367.1; -; mRNA.
DR EMBL; BC117372; AAI17373.1; -; mRNA.
DR CCDS; CCDS1265.1; -. [Q96PN6-1]
DR CCDS; CCDS53426.1; -. [Q96PN6-4]
DR CCDS; CCDS72977.1; -. [Q96PN6-2]
DR RefSeq; NP_001161221.1; NM_001167749.2. [Q96PN6-4]
DR RefSeq; NP_001284701.1; NM_001297772.1. [Q96PN6-2]
DR RefSeq; NP_060887.2; NM_018417.5. [Q96PN6-1]
DR RefSeq; XP_011508062.1; XM_011509760.2. [Q96PN6-1]
DR PDB; 4CLF; X-ray; 1.70 A; A=1-469.
DR PDB; 4CLK; X-ray; 2.20 A; A=1-469.
DR PDB; 4CLL; X-ray; 1.70 A; A=1-469.
DR PDB; 4CLP; X-ray; 1.90 A; A=1-469.
DR PDB; 4CLS; X-ray; 1.85 A; A=1-469.
DR PDB; 4CLT; X-ray; 1.95 A; A=1-469.
DR PDB; 4CLU; X-ray; 1.90 A; A=1-469.
DR PDB; 4CLW; X-ray; 2.15 A; A=1-469.
DR PDB; 4CLY; X-ray; 2.05 A; A=1-469.
DR PDB; 4CLZ; X-ray; 1.90 A; A=1-469.
DR PDB; 4CM0; X-ray; 3.20 A; A=1-469.
DR PDB; 4CM2; X-ray; 1.80 A; A=1-469.
DR PDB; 4OYA; X-ray; 2.03 A; A=1-469.
DR PDB; 4OYB; X-ray; 1.70 A; A=1-469.
DR PDB; 4OYI; X-ray; 1.70 A; A=1-469.
DR PDB; 4OYM; X-ray; 1.70 A; A=1-469.
DR PDB; 4OYO; X-ray; 1.75 A; A=1-469.
DR PDB; 4OYP; X-ray; 2.28 A; A=1-469.
DR PDB; 4OYW; X-ray; 1.70 A; A=1-469.
DR PDB; 4OYX; X-ray; 1.89 A; A=1-469.
DR PDB; 4OYZ; X-ray; 1.74 A; A=1-469.
DR PDB; 4OZ2; X-ray; 2.10 A; A=1-469.
DR PDB; 4OZ3; X-ray; 1.70 A; A=1-469.
DR PDB; 4UST; X-ray; 1.90 A; A=1-469.
DR PDB; 4USU; X-ray; 1.95 A; A=1-469.
DR PDB; 4USV; X-ray; 2.00 A; A=1-469.
DR PDB; 4USW; X-ray; 2.05 A; A=1-469.
DR PDB; 5D0R; X-ray; 2.24 A; A=1-469.
DR PDB; 5IV3; X-ray; 1.86 A; A=1-469.
DR PDB; 5IV4; X-ray; 1.79 A; A=1-469.
DR PDB; 7OVD; X-ray; 2.20 A; A=1-469.
DR PDBsum; 4CLF; -.
DR PDBsum; 4CLK; -.
DR PDBsum; 4CLL; -.
DR PDBsum; 4CLP; -.
DR PDBsum; 4CLS; -.
DR PDBsum; 4CLT; -.
DR PDBsum; 4CLU; -.
DR PDBsum; 4CLW; -.
DR PDBsum; 4CLY; -.
DR PDBsum; 4CLZ; -.
DR PDBsum; 4CM0; -.
DR PDBsum; 4CM2; -.
DR PDBsum; 4OYA; -.
DR PDBsum; 4OYB; -.
DR PDBsum; 4OYI; -.
DR PDBsum; 4OYM; -.
DR PDBsum; 4OYO; -.
DR PDBsum; 4OYP; -.
DR PDBsum; 4OYW; -.
DR PDBsum; 4OYX; -.
DR PDBsum; 4OYZ; -.
DR PDBsum; 4OZ2; -.
DR PDBsum; 4OZ3; -.
DR PDBsum; 4UST; -.
DR PDBsum; 4USU; -.
DR PDBsum; 4USV; -.
DR PDBsum; 4USW; -.
DR PDBsum; 5D0R; -.
DR PDBsum; 5IV3; -.
DR PDBsum; 5IV4; -.
DR PDBsum; 7OVD; -.
DR AlphaFoldDB; Q96PN6; -.
DR SMR; Q96PN6; -.
DR BioGRID; 120921; 3.
DR IntAct; Q96PN6; 1.
DR STRING; 9606.ENSP00000356825; -.
DR BindingDB; Q96PN6; -.
DR ChEMBL; CHEMBL5854; -.
DR GuidetoPHARMACOLOGY; 3068; -.
DR iPTMnet; Q96PN6; -.
DR PhosphoSitePlus; Q96PN6; -.
DR SwissPalm; Q96PN6; -.
DR BioMuta; ADCY10; -.
DR DMDM; 308153637; -.
DR EPD; Q96PN6; -.
DR MassIVE; Q96PN6; -.
DR PaxDb; Q96PN6; -.
DR PeptideAtlas; Q96PN6; -.
DR PRIDE; Q96PN6; -.
DR ProteomicsDB; 24204; -.
DR ProteomicsDB; 77715; -. [Q96PN6-1]
DR ProteomicsDB; 77716; -. [Q96PN6-2]
DR ProteomicsDB; 77717; -. [Q96PN6-3]
DR Antibodypedia; 3017; 147 antibodies from 23 providers.
DR DNASU; 55811; -.
DR Ensembl; ENST00000367848.1; ENSP00000356822.1; ENSG00000143199.18. [Q96PN6-2]
DR Ensembl; ENST00000367851.9; ENSP00000356825.4; ENSG00000143199.18. [Q96PN6-1]
DR Ensembl; ENST00000545172.5; ENSP00000441992.1; ENSG00000143199.18. [Q96PN6-4]
DR GeneID; 55811; -.
DR KEGG; hsa:55811; -.
DR MANE-Select; ENST00000367851.9; ENSP00000356825.4; NM_018417.6; NP_060887.2.
DR UCSC; uc001ger.4; human. [Q96PN6-1]
DR CTD; 55811; -.
DR DisGeNET; 55811; -.
DR GeneCards; ADCY10; -.
DR HGNC; HGNC:21285; ADCY10.
DR HPA; ENSG00000143199; Group enriched (liver, testis).
DR MalaCards; ADCY10; -.
DR MIM; 143870; phenotype.
DR MIM; 605205; gene.
DR neXtProt; NX_Q96PN6; -.
DR OpenTargets; ENSG00000143199; -.
DR Orphanet; 2197; Idiopathic hypercalciuria.
DR PharmGKB; PA162375618; -.
DR VEuPathDB; HostDB:ENSG00000143199; -.
DR eggNOG; ENOG502QPPT; Eukaryota.
DR GeneTree; ENSGT00390000001322; -.
DR HOGENOM; CLU_004055_1_0_1; -.
DR InParanoid; Q96PN6; -.
DR OMA; TVDIRLN; -.
DR PhylomeDB; Q96PN6; -.
DR TreeFam; TF329284; -.
DR BRENDA; 4.6.1.1; 2681.
DR PathwayCommons; Q96PN6; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR SABIO-RK; Q96PN6; -.
DR SignaLink; Q96PN6; -.
DR SIGNOR; Q96PN6; -.
DR BioGRID-ORCS; 55811; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; ADCY10; human.
DR GeneWiki; ADCY10; -.
DR GenomeRNAi; 55811; -.
DR Pharos; Q96PN6; Tchem.
DR PRO; PR:Q96PN6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96PN6; protein.
DR Bgee; ENSG00000143199; Expressed in sperm and 99 other tissues.
DR ExpressionAtlas; Q96PN6; baseline and differential.
DR Genevisible; Q96PN6; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0071890; F:bicarbonate binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; IDA:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
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 Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF011131; Soluble_adenylyl_cyclase; 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 3D-structure; Alternative splicing; ATP-binding; cAMP biosynthesis;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Lyase; Magnesium;
KW Manganese; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1610
FT /note="Adenylate cyclase type 10"
FT /id="PRO_0000317101"
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:0000269|PubMed:25040695,
FT ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449,
FT ECO:0007744|PDB:4USW"
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 ECO:0000269|PubMed:25040695, ECO:0000305|PubMed:24567411,
FT ECO:0000305|PubMed:24616449"
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:0000269|PubMed:24567411,
FT ECO:0000269|PubMed:24616449, ECO:0007744|PDB:4CLL,
FT ECO:0007744|PDB:4OYZ"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25040695,
FT ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449,
FT ECO:0007744|PDB:4USW"
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 ECO:0000269|PubMed:25040695, ECO:0000305|PubMed:24567411,
FT ECO:0000305|PubMed:24616449"
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:0000269|PubMed:25040695,
FT ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449,
FT ECO:0007744|PDB:4USW"
FT BINDING 167
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:24567411,
FT ECO:0000269|PubMed:24616449, ECO:0007744|PDB:4CLL,
FT ECO:0007744|PDB:4OYZ"
FT BINDING 176
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:24567411,
FT ECO:0000269|PubMed:24616449, ECO:0007744|PDB:4CLL,
FT ECO:0007744|PDB:4OYZ"
FT BINDING 337
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:24567411,
FT ECO:0000269|PubMed:24616449, ECO:0007744|PDB:4CLL,
FT ECO:0007744|PDB:4OYZ"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25040695,
FT ECO:0000305|PubMed:24567411, ECO:0000305|PubMed:24616449,
FT ECO:0007744|PDB:4USW"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24567411,
FT ECO:0000305|PubMed:24616449, ECO:0000305|PubMed:25040695"
FT VAR_SEQ 1..1099
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030866"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046329"
FT VAR_SEQ 1..97
FT /note="MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFT
FT AMTEKFSSAMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFA -> MSLSE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11932268"
FT /id="VSP_030867"
FT VAR_SEQ 1100..1103
FT /note="DNYM -> MLFK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030868"
FT VAR_SEQ 1430..1471
FT /note="YARLQEWDNFYKFSNRAKNLLPRRTMTLTYYDGISRYMEGQV -> ECEAGV
FT GRRLHTSRDPGMPDFRNGTTFTNFPIELKIFCQEEP (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030869"
FT VAR_SEQ 1472..1610
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030870"
FT VARIANT 234
FT /note="T -> M (in dbSNP:rs16859886)"
FT /id="VAR_038476"
FT VARIANT 697
FT /note="I -> V (in dbSNP:rs2071921)"
FT /evidence="ECO:0000269|PubMed:11423534,
FT ECO:0000269|PubMed:11932268, ECO:0000269|PubMed:12609998"
FT /id="VAR_038477"
FT MUTAGEN 95
FT /note="K->A: Nearly abolishes bicarbonate-mediated increase
FT of enzyme activity. Abolishes bicarbonate-mediated increase
FT of enzyme activity; when associated with A-176."
FT /evidence="ECO:0000269|PubMed:24567411"
FT MUTAGEN 176
FT /note="R->A: Reduces bicarbonate-mediated increase of
FT enzyme activity. Abolishes bicarbonate-mediated increase of
FT enzyme activity; when associated with A-95."
FT /evidence="ECO:0000269|PubMed:24567411"
FT CONFLICT 942
FT /note="L -> P (in Ref. 6; BAG64062)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359
FT /note="L -> P (in Ref. 4; AAK96045)"
FT /evidence="ECO:0000305"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 33..47
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 67..88
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:4CLF"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4OYB"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4OYB"
FT STRAND 144..158
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:4CLF"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 288..302
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 307..327
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:4CLF"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4OYW"
FT HELIX 358..374
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 379..398
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:4CLF"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:4CLF"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:4OYZ"
SQ SEQUENCE 1610 AA; 187149 MW; E0E205747120EFE0 CRC64;
MNTPKEEFQD WPIVRIAAHL PDLIVYGHFS PERPFMDYFD GVLMFVDISG FTAMTEKFSS
AMYMDRGAEQ LVEILNYHIS AIVEKVLIFG GDILKFAGDA LLALWRVERK QLKNIITVVI
KCSLEIHGLF ETQEWEEGLD IRVKIGLAAG HISMLVFGDE THSHFLVIGQ AVDDVRLAQN
MAQMNDVILS PNCWQLCDRS MIEIESVPDQ RAVKVNFLKP PPNFNFDEFF TKCTTFMHYY
PSGEHKNLLR LACTLKPDPE LEMSLQKYVM ESILKQIDNK QLQGYLSELR PVTIVFVNLM
FEDQDKAEEI GPAIQDAYMH ITSVLKIFQG QINKVFMFDK GCSFLCVFGF PGEKVPDELT
HALECAMDIF DFCSQVHKIQ TVSIGVASGI VFCGIVGHTV RHEYTVIGQK VNLAARMMMY
YPGIVTCDSV TYNGSNLPAY FFKELPKKVM KGVADSGPLY QYWGRTEKVM FGMACLICNR
KEDYPLLGRN KEINYFMYTM KKFLISNSSQ VLMYEGLPGY GKSQILMKIE YLAQGKNHRI
IAISLNKISF HQTFYTIQMF MANVLGLDTC KHYKERQTNL RNKVMTLLDE KFYCLLNDIF
HVQFPISREI SRMSTLKKQK QLEILFMKIL KLIVKEERII FIIDEAQFVD STSWRFMEKL
IRTLPIFIIM SLCPFVNIPC AAARAVIKNR NTTYIVIGAV QPNDISNKIC LDLNVSCISK
ELDSYLGEGS CGIPFYCEEL LKNLEHHEVL VFQQTESEEK TNRTWNNLFK YSIKLTEKLN
MVTLHSDKES EEVCHLTSGV RLKNLSPPTS LKEISLIQLD SMRLSHQMLV RCAAIIGLTF
TTELLFEILP CWNMKMMIKT LATLVESNIF YCFRNGKELQ KALKQNDPSF EVHYRSLSLK
PSEGMDHGEE EQLRELENEV IECHRIRFCN PMMQKTAYEL WLKDQRKAMH LKCARFLEED
AHRCDHCRGR DFIPYHHFTV NIRLNALDMD AIKKMAMSHG FKTEEKLILS NSEIPETSAF
FPENRSPEEI REKILNFFDH VLTKMKTSDE DIIPLESCQC EEILEIVILP LAHHFLALGE
NDKALYYFLE IASAYLIFCD NYMAYMYLNE GQKLLKTLKK DKSWSQTFES ATFYSLKGEV
CFNMGQIVLA KKMLRKALKL LNRIFPYNLI SLFLHIHVEK NRHFHYVNRQ AQESPPPGKK
RLAQLYRQTV CLSLLWRIYS YSYLFHCKYY AHLAVMMQMN TALETQNCFQ IIKAYLDYSL
YHHLAGYKGV WFKYEVMAME HIFNLPLKGE GIEIVAYVAE TLVFNKLIMG HLDLAIELGS
RALQMWALLQ NPNRHYQSLC RLSRCLLLNS RYPQLIQVLG RLWELSVTQE HIFSKAFFYF
VCLDILLYSG FVYRTFEECL EFIHQYENNR ILKFHSGLLL GLYSSVAIWY ARLQEWDNFY
KFSNRAKNLL PRRTMTLTYY DGISRYMEGQ VLHLQKQIKE QSENAQASGE ELLKNLENLV
AQNTTGPVFC PRLYHLMAYV CILMGDGQKC GLFLNTALRL SETQGNILEK CWLNMNKESW
YSTSELKEDQ WLQTILSLPS WEKIVAGRVN IQDLQKNKFL MRANTVDNHF
