Reviewed, UniProtKB/Swiss-Prot Q8C0T9 (ADCYA_MOUSE)

Names and origin

Protein names

Recommended name:
    Adenylate cyclase type 10
    EC=4.6.1.1
Alternative name(s):
    Testicular soluble adenylyl cyclase
    Germ cell soluble adenylyl cyclase
      Short name=sAC

Gene names

Name:	Adcy10
Synonyms:	Sac, Sacy

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1614 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (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. Ref.4 Ref.5
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. Ref.3
Tissue specificity	Expressed in testis. Ref.5
Disruption phenotype	Mice are infertile because of a severe sperm-motility defect. Ref.4
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro spermatogenesis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Traceable author statement. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8C0T9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8C0T9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-471: MF → TC
     472-1614: Missing.

Note: Not experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1614	1614	Adenylate cyclase type 10		PRO_0000317102
Regions
	Domain	42 – 179	138	Guanylate cyclase 1
	Domain	293 – 418	126	Guanylate cyclase 2
	Compositional bias	909 – 912	4	Poly-Glu
Sites
	Metal binding	47	1	Magnesium 1 By similarity
	Metal binding	47	1	Magnesium 2 By similarity
	Metal binding	48	1	Magnesium 2; via carbonyl oxygen By similarity
	Metal binding	99	1	Magnesium 1 By similarity
	Metal binding	99	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	810	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	470 – 471	2	MF → TC in isoform 2.		VSP_030871
	Alternative sequence	472 – 1614	1143	Missing in isoform 2.		VSP_030872

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 94828EA35CE5D433	FASTA	1,614	186,407
	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
	Isoform 2. Checksum: E41C5F74AB6FBC0C	FASTA	471	52,961
	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 YPGIVSCDSV TYDGSNLPAY FFKELPKKVM KGVADPGPVY QCLGLNEKVT C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Testis.
[2]	"Identification and functional analysis of splice variants of the germ cell soluble adenylyl cyclase." Jaiswal B.S., Conti M. J. Biol. Chem. 276:31698-31708(2001) [PubMed: 11423534] [Abstract] Cited for: ALTERNATIVE SPLICING.
[3]	"Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains." Zippin J.H., Chen Y., Nahirney P., Kamenetsky M., Wuttke M.S., Fischman D.A., Levin L.R., Buck J. FASEB J. 17:82-84(2003) [PubMed: 12475901] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Mice deficient for soluble adenylyl cyclase are infertile because of a severe sperm-motility defect." 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. Proc. Natl. Acad. Sci. U.S.A. 101:2993-2998(2004) [PubMed: 14976244] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"The 'soluble' adenylyl cyclase in sperm mediates multiple signaling events required for fertilization." 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. Dev. Cell 9:249-259(2005) [PubMed: 16054031] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK029849 mRNA. Translation: BAC26642.1. AK133181 mRNA. Translation: BAE21546.1.
IPI	IPI00224014. IPI00830276.
RefSeq	NP_766617.2.
UniGene	Mm.66952
3D structure databases
SMR	Q8C0T9. Positions 41-198, 288-466.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8C0T9.
Proteomic databases
PRIDE	Q8C0T9.
Genome annotation databases
Ensembl	ENSMUST00000027852; ENSMUSP00000027852; ENSMUSG00000026567; Mus musculus. [Genome view] ENSMUST00000111437; ENSMUSP00000107064; ENSMUSG00000026567; Mus musculus. [Genome view]
GeneID	271639.
KEGG	mmu:271639.
UCSC	uc007djf.1. mouse.
Organism-specific databases
CTD	271639.
MGI	MGI:2660854. Adcy10.
Phylogenomic databases
eggNOG	roNOG06659.
HOGENOM	HBG282712.
HOVERGEN	Q8C0T9.
InParanoid	Q8C0T9.
Enzyme and pathway databases
BRENDA	4.6.1.1. 244.
Gene expression databases
ArrayExpress	Q8C0T9.
Bgee	Q8C0T9.
CleanEx	MM_ADCY10.
Genevestigator	Q8C0T9.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR016577. Adenylate_cylcase_typ10. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
Pfam	PF00211. Guanylate_cyc. 2 hits. [Graphical view]
PIRSF	PIRSF011131. Soluble_adenylyl_cyclase. 1 hit.
SMART	SM00044. CYCc. 1 hit. [Graphical view]
PROSITE	PS00452. GUANYLATE_CYCLASE_1. False negative. PS50125. GUANYLATE_CYCLASE_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	393482.
SOURCE	Search...

Entry information

Entry name

ADCYA_MOUSE

Accession

Primary (citable) accession number: Q8C0T9
Secondary accession number(s): Q3V0F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)