[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). STRAIN=C57BL/6J; TISSUE=Testis; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[2]	ALTERNATIVE SPLICING. DOI=10.1074/jbc.M011698200; PubMed=11423534 [NCBI, ExPASy, EBI, Israel, Japan] Jaiswal B.S., Conti M.; "Identification and functional analysis of splice variants of the germ cell soluble adenylyl cyclase."; J. Biol. Chem. 276:31698-31708(2001).
[3]	SUBCELLULAR LOCATION. DOI=10.1096/fj.02-0598fje; PubMed=12475901 [NCBI, ExPASy, EBI, Israel, Japan] Zippin J.H., Chen Y., Nahirney P., Kamenetsky M., Wuttke M.S., Fischman D.A., Levin L.R., Buck J.; "Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains."; FASEB J. 17:82-84(2003).
[4]	FUNCTION, AND KNOCKOUT. DOI=10.1073/pnas.0400050101; PubMed=14976244 [NCBI, ExPASy, EBI, Israel, Japan] Esposito G., Jaiswal B.S., Xie F., Krajnc-Franken M.A.M., Robben T.J.A.A., Strik A.M., Kuil C., Philipsen R.L.A., van Duin M., Conti M., Gossen J.A.; "Mice deficient for soluble adenylyl cyclase are infertile because of a severe sperm-motility defect."; Proc. Natl. Acad. Sci. U.S.A. 101:2993-2998(2004).
[5]	FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1016/j.devcel.2005.06.007; PubMed=16054031 [NCBI, ExPASy, EBI, Israel, Japan] Hess K.C., Jones B.H., Marquez B., Chen Y., Ord T.S., Kamenetsky M., Miyamoto C., Zippin J.H., Kopf G.S., Suarez S.S., Levin L.R., Williams C.J., Buck J., Moss S.B.; "The 'soluble' adenylyl cyclase in sperm mediates multiple signaling events required for fertilization."; Dev. Cell 9:249-259(2005).

Comments

FUNCTION: Soluble adenylyl cyclase that has a critical role in mammalian spermatogenesis. Produces the cAMP which mediates in part the cAMP-responsive nuclear factors indispensable for maturation of sperm in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization. May be the bicarbonate sensor.
CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
ENZYME REGULATION: Activated by manganese or magnesium ions. In the presence of magnesium ions, the enzyme is activated by bicarbonate while in the presence of manganese ions, the enzyme is inhibited by bicarbonate. In the absence of magnesium and bicarbonate, the enzyme is weakly activated by calcium (By similarity).
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane-associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q8C0T9-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q8C0T9-2
Note: Not experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_030871, VSP_030872.

TISSUE SPECIFICITY: Expressed in testis.
SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
SIMILARITY: Contains 2 guanylate cyclase domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AK029849; BAC26642.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK133181; BAE21546.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_766617.1; -.

UniGene

Mm.66952

3D structure databases

ModBase

Q8C0T9.

PTM databases

PhosphoSite

Q8C0T9; -.

Organism-specific databases

MGI

MGI:2660854; Adcy10.

Gene expression databases

ArrayExpress

Q8C0T9; -.

CleanEx

MM_ADCY10; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (traceable author statement from MGI).
GO:0005856;	Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004016;	Molecular function: adenylate cyclase activity (traceable author statement from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0006171;	Biological process: cAMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0007283;	Biological process: spermatogenesis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001054; A/G_cyclase.
IPR016577; Adenylate_cylcase_typ10.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.1230; A/G_cyclase; 2.

Pfam

PF00211; Guanylate_cyc; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF011131; Soluble_adenylyl_cyclase; 1.

SMART

SM00044; CYCc; 1.
SMART graphical view of domain structure.

PROSITE

PS00452; GUANYLATE_CYCLASE_1; FALSE_NEG.
PS50125; GUANYLATE_CYCLASE_2; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000026567; Mus musculus. [Contig view]

GeneID

271639; -.

KEGG

mmu:271639; -.

Phylogenomic databases

HOGENOM

Q8C0T9; -.

HOVERGEN

Q8C0T9; -.

Other

NextBio

393482; -.

SOURCE

Adcy10; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane; Cytoplasm; Cytoskeleton; Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1614`	`1614`	`Adenylate cyclase type 10.`	`PRO_0000317102`
`DOMAIN`	`42 179`	`138`	`Guanylate cyclase 1.`
`DOMAIN`	`293 418`	`126`	`Guanylate cyclase 2.`
`COMPBIAS`	`909 912`	`4`	`Poly-Glu.`
`METAL`	`47 47`		`Magnesium 1 (By similarity).`
`METAL`	`47 47`		`Magnesium 2 (By similarity).`
`METAL`	`48 48`		`Magnesium 2; via carbonyl oxygen (By similarity).`
`METAL`	`99 99`		`Magnesium 1 (By similarity).`
`METAL`	`99 99`		`Magnesium 2 (By similarity).`
`MOD_RES`	`810 810`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`470 471`		`MF -> TC (in isoform 2).`	`VSP_030871`
`VAR_SEQ`	`472 1614`		`Missing (in isoform 2).`	`VSP_030872`

Sequence information

Length: 1614 AA [This is the length of the unprocessed precursor]

Molecular weight: 186407 Da [This is the MW of the unprocessed precursor]

CRC64: 94828EA35CE5D433 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSARRQELQD RAIVKIAAHL PDLIVYGDFS PERPSVKCFD GVLMFVDISG FTAMTEKFST 

        70         80         90        100        110        120 
AMYMDRGAEQ LVEILNYYIS AIVEKVLIFG GDILKFAGDA LLALWKVERK QLKNIITVVI 

       130        140        150        160        170        180 
KCSLEIHGLF EAKEAEEGLD IRVKIGLAAG HITMLVFGDE TRNYFLVIGQ AVDDVRLAQN 

       190        200        210        220        230        240 
MAQMNDVILS PNCWQLCDRS MIEIERIPDQ RAVKVSFLKP PPTFNFDEFF TKCMGFMDYY 

       250        260        270        280        290        300 
PSGDHKNFLR LACMLESDPE LELSLQKYVM EIILKQIDDK QLRGYLSELR PVTIVFVNLM 

       310        320        330        340        350        360 
FKEHDKVEVI GSAIQAACVH ITSVLKVFRG QINKVFMFDK GCSFLCVFGF PGEKAPDEIT 

       370        380        390        400        410        420 
HALESAVDIF DFCSQVHKIR TVSIGVASGI VFCGIVGHTV RHEYTVIGQK VNIAARMMMY 

       430        440        450        460        470        480 
YPGIVSCDSV TYDGSNLPAY FFKELPKKVM KGVADPGPVY QCLGLNEKVM FGMAYLICNR 

       490        500        510        520        530        540 
YEGYPLLGRV REIDYFMSTM KDFLMTNCSR VLMYEGLPGY GKSQVLMEIE YLASQHENHR 

       550        560        570        580        590        600 
AVAIALTKIS FHQNFYTIQI LMANVLGLDT CKHYKERQTN LQNRVKTLLD EKFHCLLNDI 

       610        620        630        640        650        660 
FHVQFPVSRE MSRMSKIRKQ KQLEALFMKI LAQTVREERI IFIIDEAQFV DGTSWAFIEK 

       670        680        690        700        710        720 
LIRSMPIFIV MSLAPFSEVP CAAANAIMKN RNTTYITLGT MQPQEIRDKV CVDLSVSSIP 

       730        740        750        760        770        780 
RELDSYLVEG SCGIPYYCEE LLKNLDHHRV LLFQQAETEQ KTNVTWNNMF KHSVRPTDDM 

       790        800        810        820        830        840 
QLFTSISEGQ KEVCYLVSGV RLNNLSPPAS LKEISLVQLD SMSLSHQMLV RCAAIIGLTF 

       850        860        870        880        890        900 
TTELLFEILP CWNMKMMIKA LATLVESNVF NCFRSSKDLQ LALKQNVPTF EVHYRSLALK 

       910        920        930        940        950        960 
LKEGLTYGEE EELREMEGEV VECRILRFCR PIMQKTAYEL WLKDQKKVLH LKCARFLEES 

       970        980        990       1000       1010       1020 
AHRCNHCRNV DFIPYHHFIV DIRLNTLDMD TVKRMVTSQG FKIDEEEAVF SKSELPRKYK 

      1030       1040       1050       1060       1070       1080 
FPENLSITEI REKILHFFDN VILKMKSSPN DIIPLESCQC KELLQIVILP LAQHFVALEE 

      1090       1100       1110       1120       1130       1140 
NNKALYYFLE LASAYLILGD NYNAYMYLGE GERLLKSLTN EDSWSQTFEY ATFYSLKAEV 

      1150       1160       1170       1180       1190       1200 
CFNMGQMVLA KKMLRKALKL LNRMFPCNLL TLTFQMHVEK NRLSHFMNQH TQEGSVPGKK 

      1210       1220       1230       1240       1250       1260 
LAQLYLQASC FSLLWRIYSL NFFFHYKYYG HLAAMMEMNT SLETQNDFQI IKAYLDFSLY 

      1270       1280       1290       1300       1310       1320 
HHLAGYQGVW FKYEILVMEQ LLNLPLKGEA IEIMAYTADT LGHIKFLMGH LDLAIELGSR 

      1330       1340       1350       1360       1370       1380 
AHRMWSLLRN PNKYQMVLCR LSKPLFLKSR YKHLVQVLGW LWDLSVTEED IFSKAFFYFV 

      1390       1400       1410       1420       1430       1440 
CLDIMLYSGF IYRTFEECLE FIHHNEDNRI LKFQSGLLLG LYSCIAVWYA RLQEWDNFNK 

      1450       1460       1470       1480       1490       1500 
FSDRAKHLVT RRTPTVLYYE GISRYMEGQV LHLQKQIEEQ AENAQDSGVE ILKALETLVA 

      1510       1520       1530       1540       1550       1560 
QNTTGPVFYP RLYHLMAYVC ILMGDGHSCD FFLNTALELS ETHGNLLEKC WLSMSKEWWY 

      1570       1580       1590       1600       1610 
SASELTGDQW LQTVLSLPSW DKIVSGKGGQ RKRSWSWFCP PNFSMVSWSQ PQCA

Q8C0T9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools