UniProtKB - Q96PN6 (ADCYA_HUMAN)

>sp|Q96PN6|ADCYA_HUMAN Adenylate cyclase type 10 OS=Homo sapiens OX=9606 GN=ADCY10 PE=1 SV=3
MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSS
AMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVI
KCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQN
MAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYY
PSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLM
FEDQDKAEEIGPAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELT
HALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMY
YPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNR
KEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRI
IAISLNKISFHQTFYTIQMFMANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIF
HVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKL
IRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISK
ELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLN
MVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTF
TTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLK
PSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEED
AHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAF
FPENRSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGE
NDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEV
CFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKK
RLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSL
YHHLAGYKGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGS
RALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLGRLWELSVTQEHIFSKAFFYF
VCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFY
KFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLV
AQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESW
YSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFLMRANTVDNHF

Entry version 157 (12 Aug 2020)
Sequence version 3 (05 Oct 2010)
Previous versions | rss

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Protein

Adenylate cyclase type 10

Gene

ADCY10

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the formation of the signaling molecule cAMP (PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695, PubMed:24567411). May function as sensor that mediates responses to changes in cellular bicarbonate and CO₂ levels (PubMed:15659711, PubMed:17591988). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (PubMed:17591988).By similarity5 Publications

Catalytic activityⁱ

ATP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
3',5'-cyclic AMP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
5 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Kinetic properties of 'soluble' adenylyl cyclase. Synergism between calcium and bicarbonate."
  Litvin T.N., Kamenetsky M., Zarifyan A., Buck J., Levin L.R.
  J. Biol. Chem. 278:15922-15926(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, VARIANT VAL-697.
- Ref.11
  "Cloning and characterization of the human soluble adenylyl cyclase."
  Geng W., Wang Z., Zhang J., Reed B.Y., Pak C.Y.C., Moe O.W.
  Am. J. Physiol. 288:C1305-C1316(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION.
- Ref.13
  "Crystal structure of human soluble adenylate cyclase reveals a distinct, highly flexible allosteric bicarbonate binding pocket."
  Saalau-Bethell S.M., Berdini V., Cleasby A., Congreve M., Coyle J.E., Lock V., Murray C.W., O'Brien M.A., Rich S.J., Sambrook T., Vinkovic M., Yon J.R., Jhoti H.
  ChemMedChem 9:823-832(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH HYDROGENCARBONATE; CALCIUM AND ATP ANALOG, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DOMAIN.
- Ref.14
  "Structural analysis of human soluble adenylyl cyclase and crystal structures of its nucleotide complexes-implications for cyclase catalysis and evolution."
  Kleinboelting S., van den Heuvel J., Steegborn C.
  FEBS J. 281:4151-4164(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-469 IN COMPLEXES WITH MAGNESIUM; CALCIUM; ATP AND ATP ANALOGS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN.
- Ref.15
  "Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate."
  Kleinboelting S., Diaz A., Moniot S., van den Heuvel J., Weyand M., Levin L.R., Buck J., Steegborn C.
  Proc. Natl. Acad. Sci. U.S.A. 111:3727-3732(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH CALCIUM; HYDROGENCARBONATE AND ATP ANALOGS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF LYS-95 AND ARG-176, DOMAIN.
EC:
4.6.1.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
5 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Kinetic properties of 'soluble' adenylyl cyclase. Synergism between calcium and bicarbonate."
  Litvin T.N., Kamenetsky M., Zarifyan A., Buck J., Levin L.R.
  J. Biol. Chem. 278:15922-15926(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, VARIANT VAL-697.
- Ref.11
  "Cloning and characterization of the human soluble adenylyl cyclase."
  Geng W., Wang Z., Zhang J., Reed B.Y., Pak C.Y.C., Moe O.W.
  Am. J. Physiol. 288:C1305-C1316(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION.
- Ref.13
  "Crystal structure of human soluble adenylate cyclase reveals a distinct, highly flexible allosteric bicarbonate binding pocket."
  Saalau-Bethell S.M., Berdini V., Cleasby A., Congreve M., Coyle J.E., Lock V., Murray C.W., O'Brien M.A., Rich S.J., Sambrook T., Vinkovic M., Yon J.R., Jhoti H.
  ChemMedChem 9:823-832(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH HYDROGENCARBONATE; CALCIUM AND ATP ANALOG, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DOMAIN.
- Ref.14
  "Structural analysis of human soluble adenylyl cyclase and crystal structures of its nucleotide complexes-implications for cyclase catalysis and evolution."
  Kleinboelting S., van den Heuvel J., Steegborn C.
  FEBS J. 281:4151-4164(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-469 IN COMPLEXES WITH MAGNESIUM; CALCIUM; ATP AND ATP ANALOGS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN.
- Ref.15
  "Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate."
  Kleinboelting S., Diaz A., Moniot S., van den Heuvel J., Weyand M., Levin L.R., Buck J., Steegborn C.
  Proc. Natl. Acad. Sci. U.S.A. 111:3727-3732(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-469 IN COMPLEX WITH CALCIUM; HYDROGENCARBONATE AND ATP ANALOGS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF LYS-95 AND ARG-176, DOMAIN.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
=
3',5'-cyclic AMP
zoom
+
diphosphate
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Cofactorⁱ

Mg²⁺1 Publication4 Publications, Mn²⁺3 PublicationsNote: Binds 2 magnesium ions per subunit (PubMed:25040695). Is also active with manganese (in vitro) (PubMed:12609998, PubMed:15659711, PubMed:24616449).1 Publication3 Publications

Activity regulationⁱ

Activated by manganese or magnesium ions (PubMed:12609998, PubMed:24616449). In the presence of magnesium ions, the enzyme is activated by bicarbonate (PubMed:12609998, PubMed:15659711, PubMed:24567411). In the presence of manganese ions, the enzyme is inhibited by bicarbonate (PubMed:15659711). In the absence of magnesium and bicarbonate, the enzyme is weakly activated by calcium (PubMed:15659711). Calcium mildly increases the enzyme activity, also in the presence of magnesium ions (PubMed:15659711, PubMed:25040695).5 Publications

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	47	Magnesium 1PROSITE-ProRule annotation2 Publications1 Publication	1
Metal bindingⁱ	47	Magnesium 2PROSITE-ProRule annotation	1
Metal bindingⁱ	48	Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation	1
Binding siteⁱ	95	BicarbonateCombined sources2 Publications	1
Metal bindingⁱ	99	Magnesium 1PROSITE-ProRule annotation2 Publications1 Publication	1
Metal bindingⁱ	99	Magnesium 2PROSITE-ProRule annotation	1
Binding siteⁱ	99	ATPCombined sources2 Publications1 Publication	1
Binding siteⁱ	144	ATPCombined sources2 Publications1 Publication	1
Binding siteⁱ	167	Bicarbonate; via amide nitrogen and carbonyl oxygenCombined sources2 Publications	1
Binding siteⁱ	176	BicarbonateCombined sources2 Publications	1
Binding siteⁱ	337	Bicarbonate; via amide nitrogenCombined sources2 Publications	1
Binding siteⁱ	406	ATP; via carbonyl oxygenCombined sources2 Publications1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	47 – 52	ATPCombined sources2 Publications1 Publication		6
Nucleotide bindingⁱ	412 – 416	ATP3 Publications		5

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	cAMP biosynthesis
Ligand	ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	4.6.1.1, 2681
PathwayCommonsⁱ	Q96PN6
Reactomeⁱ	R-HSA-5610787, Hedgehog 'off' state
SIGNORⁱ	Q96PN6

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Adenylate cyclase type 10 (EC:4.6.1.15 Publications) Alternative name(s): AH-related protein Adenylate cyclase homolog Germ cell soluble adenylyl cyclase1 Publication Short name: hsAC Short name: sAC2 Publications Testicular soluble adenylyl cyclase
Gene namesⁱ	Name:ADCY10 Synonyms:SAC
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000143199.17
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:21285, ADCY10
MIMⁱ	605205, gene
neXtProtⁱ	NX_Q96PN6

Keywords - Cellular componentⁱ

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Hypercalciuria absorptive 2 (HCA2)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA common type of hypercalciuria, a condition characterized by excessive urinary calcium excretion. Absorptive hypercalciuria is due to gastrointestinal hyperabsorption of calcium and is a frequent cause of calcium oxalate nephrolithiasis.

Related information in OMIM

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	95	K → A: Nearly abolishes bicarbonate-mediated increase of enzyme activity. Abolishes bicarbonate-mediated increase of enzyme activity; when associated with A-176. 1 Publication		1
Mutagenesisⁱ	176	R → A: Reduces bicarbonate-mediated increase of enzyme activity. Abolishes bicarbonate-mediated increase of enzyme activity; when associated with A-95. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	55811
MalaCards human disease database More...MalaCardsⁱ	ADCY10
MIMⁱ	143870, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000143199
Orphanetⁱ	2197, Idiopathic hypercalciuria
PharmGKBⁱ	PA162375618

Miscellaneous databases

Pharosⁱ	Q96PN6, Tchem

Pharosⁱ

Q96PN6, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL5854
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	3068

Polymorphism and mutation databases

BioMutaⁱ	ADCY10
DMDMⁱ	308153637

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000317101	1 – 1610	Adenylate cyclase type 10Add BLAST		1610

Post-translational modificationⁱ

Cleavage may occur to generate the active 48 kDa form.Curated

Proteomic databases

EPDⁱ	Q96PN6
MassIVEⁱ	Q96PN6
PaxDbⁱ	Q96PN6
PeptideAtlas More...PeptideAtlasⁱ	Q96PN6
PRIDEⁱ	Q96PN6
ProteomicsDBⁱ	24204 77715 [Q96PN6-1] 77716 [Q96PN6-2] 77717 [Q96PN6-3]

PTM databases

iPTMnetⁱ	Q96PN6
PhosphoSitePlusⁱ	Q96PN6
SwissPalmⁱ	Q96PN6

Expressionⁱ

Tissue specificityⁱ

Detected in airway epithelial cells and testis (at protein level) (PubMed:17591988). Weakly expressed in multiple tissues. Expressed in brain, heart, kidney, liver, lung, pancreas, peripheral blood leukocytes, placenta, skeletal muscle, stomach, thymus, airway epithelial cells, duodenum, jejunum and ileum. Very low level of expression in bone.3 Publications

Gene expression databases

Bgeeⁱ	ENSG00000143199, Expressed in testis and 97 other tissues
ExpressionAtlasⁱ	Q96PN6, baseline and differential
Genevisibleⁱ	Q96PN6, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000143199, Group enriched (liver, testis)

HPAⁱ

ENSG00000143199, Group enriched (liver, testis)

Interactionⁱ

GO - Molecular functionⁱ

ATPase binding Source: Ensembl

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	120921, 1 interactor
IntActⁱ	Q96PN6, 1 interactor
STRINGⁱ	9606.ENSP00000356825

Chemistry databases

BindingDBⁱ

Q96PN6

Miscellaneous databases

RNActⁱ	Q96PN6, protein

RNActⁱ

Q96PN6, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	12 – 17	Combined sources	6
Helixⁱ	22 – 25	Combined sources	4
Beta strandⁱ	33 – 47	Combined sources	15
Helixⁱ	49 – 52	Combined sources	4
Helixⁱ	55 – 59	Combined sources	5
Helixⁱ	61 – 63	Combined sources	3
Helixⁱ	67 – 88	Combined sources	22
Beta strandⁱ	92 – 96	Combined sources	5
Beta strandⁱ	98 – 106	Combined sources	9
Helixⁱ	109 – 111	Combined sources	3
Helixⁱ	112 – 129	Combined sources	18
Turnⁱ	130 – 132	Combined sources	3
Beta strandⁱ	135 – 138	Combined sources	4
Beta strandⁱ	144 – 158	Combined sources	15
Beta strandⁱ	163 – 169	Combined sources	7
Helixⁱ	170 – 181	Combined sources	12
Beta strandⁱ	187 – 189	Combined sources	3
Helixⁱ	191 – 196	Combined sources	6
Helixⁱ	199 – 201	Combined sources	3
Beta strandⁱ	202 – 207	Combined sources	6
Beta strandⁱ	210 – 218	Combined sources	9
Helixⁱ	226 – 234	Combined sources	9
Helixⁱ	243 – 245	Combined sources	3
Helixⁱ	251 – 254	Combined sources	4
Helixⁱ	259 – 266	Combined sources	8
Helixⁱ	271 – 277	Combined sources	7
Turnⁱ	283 – 286	Combined sources	4
Beta strandⁱ	288 – 302	Combined sources	15
Helixⁱ	307 – 327	Combined sources	21
Beta strandⁱ	331 – 337	Combined sources	7
Beta strandⁱ	339 – 349	Combined sources	11
Turnⁱ	351 – 353	Combined sources	3
Helixⁱ	358 – 374	Combined sources	17
Beta strandⁱ	379 – 398	Combined sources	20
Beta strandⁱ	401 – 408	Combined sources	8
Helixⁱ	409 – 420	Combined sources	12
Beta strandⁱ	424 – 427	Combined sources	4
Helixⁱ	429 – 435	Combined sources	7
Helixⁱ	439 – 441	Combined sources	3
Beta strandⁱ	442 – 444	Combined sources	3
Beta strandⁱ	460 – 462	Combined sources	3
Beta strandⁱ	465 – 467	Combined sources	3

Show more details

3D structure databases

SMRⁱ	Q96PN6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	42 – 179	Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST		138
Domainⁱ	293 – 418	Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST		126

Domainⁱ

The N-terminal guanylate cyclase domains are required for enzyme activity. Fragments or isoforms containing the first 470 amino acid residues are fully active.3 Publications

Sequence similaritiesⁱ

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	ENOG502QPPT, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000001322
HOGENOMⁱ	CLU_004055_1_0_1
InParanoidⁱ	Q96PN6
KEGG Orthology (KO) More...KOⁱ	K11265
OMAⁱ	TVDIRLN
PhylomeDBⁱ	Q96PN6
TreeFamⁱ	TF329284

Family and domain databases

Gene3Dⁱ	3.30.70.1230, 2 hits
InterProⁱ	View protein in InterPro IPR001054, A/G_cyclase IPR016577, Adenylate_cyclase_typ10 IPR029787, Nucleotide_cyclase IPR027417, P-loop_NTPase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00211, Guanylate_cyc, 2 hits
PIRSFⁱ	PIRSF011131, Soluble_adenylyl_cyclase, 1 hit
SUPFAMⁱ	SSF52540, SSF52540, 1 hit SSF55073, SSF55073, 2 hits
PROSITEⁱ	View protein in PROSITE PS50125, GUANYLATE_CYCLASE_2, 2 hits

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q96PN6-1) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MNTPKEEFQD WPIVRIAAHL PDLIVYGHFS PERPFMDYFD GVLMFVDISG 
        60         70         80         90        100
FTAMTEKFSS AMYMDRGAEQ LVEILNYHIS AIVEKVLIFG GDILKFAGDA 
       110        120        130        140        150
LLALWRVERK QLKNIITVVI KCSLEIHGLF ETQEWEEGLD IRVKIGLAAG 
       160        170        180        190        200
HISMLVFGDE THSHFLVIGQ AVDDVRLAQN MAQMNDVILS PNCWQLCDRS 
       210        220        230        240        250
MIEIESVPDQ RAVKVNFLKP PPNFNFDEFF TKCTTFMHYY PSGEHKNLLR 
       260        270        280        290        300
LACTLKPDPE LEMSLQKYVM ESILKQIDNK QLQGYLSELR PVTIVFVNLM 
       310        320        330        340        350
FEDQDKAEEI GPAIQDAYMH ITSVLKIFQG QINKVFMFDK GCSFLCVFGF 
       360        370        380        390        400
PGEKVPDELT HALECAMDIF DFCSQVHKIQ TVSIGVASGI VFCGIVGHTV 
       410        420        430        440        450
RHEYTVIGQK VNLAARMMMY YPGIVTCDSV TYNGSNLPAY FFKELPKKVM 
       460        470        480        490        500
KGVADSGPLY QYWGRTEKVM FGMACLICNR KEDYPLLGRN KEINYFMYTM 
       510        520        530        540        550
KKFLISNSSQ VLMYEGLPGY GKSQILMKIE YLAQGKNHRI IAISLNKISF 
       560        570        580        590        600
HQTFYTIQMF MANVLGLDTC KHYKERQTNL RNKVMTLLDE KFYCLLNDIF 
       610        620        630        640        650
HVQFPISREI SRMSTLKKQK QLEILFMKIL KLIVKEERII FIIDEAQFVD 
       660        670        680        690        700
STSWRFMEKL IRTLPIFIIM SLCPFVNIPC AAARAVIKNR NTTYIVIGAV 
       710        720        730        740        750
QPNDISNKIC LDLNVSCISK ELDSYLGEGS CGIPFYCEEL LKNLEHHEVL 
       760        770        780        790        800
VFQQTESEEK TNRTWNNLFK YSIKLTEKLN MVTLHSDKES EEVCHLTSGV 
       810        820        830        840        850
RLKNLSPPTS LKEISLIQLD SMRLSHQMLV RCAAIIGLTF TTELLFEILP 
       860        870        880        890        900
CWNMKMMIKT LATLVESNIF YCFRNGKELQ KALKQNDPSF EVHYRSLSLK 
       910        920        930        940        950
PSEGMDHGEE EQLRELENEV IECHRIRFCN PMMQKTAYEL WLKDQRKAMH 
       960        970        980        990       1000
LKCARFLEED AHRCDHCRGR DFIPYHHFTV NIRLNALDMD AIKKMAMSHG 
      1010       1020       1030       1040       1050
FKTEEKLILS NSEIPETSAF FPENRSPEEI REKILNFFDH VLTKMKTSDE 
      1060       1070       1080       1090       1100
DIIPLESCQC EEILEIVILP LAHHFLALGE NDKALYYFLE IASAYLIFCD 
      1110       1120       1130       1140       1150
NYMAYMYLNE GQKLLKTLKK DKSWSQTFES ATFYSLKGEV CFNMGQIVLA 
      1160       1170       1180       1190       1200
KKMLRKALKL LNRIFPYNLI SLFLHIHVEK NRHFHYVNRQ AQESPPPGKK 
      1210       1220       1230       1240       1250
RLAQLYRQTV CLSLLWRIYS YSYLFHCKYY AHLAVMMQMN TALETQNCFQ 
      1260       1270       1280       1290       1300
IIKAYLDYSL YHHLAGYKGV WFKYEVMAME HIFNLPLKGE GIEIVAYVAE 
      1310       1320       1330       1340       1350
TLVFNKLIMG HLDLAIELGS RALQMWALLQ NPNRHYQSLC RLSRCLLLNS 
      1360       1370       1380       1390       1400
RYPQLIQVLG RLWELSVTQE HIFSKAFFYF VCLDILLYSG FVYRTFEECL 
      1410       1420       1430       1440       1450
EFIHQYENNR ILKFHSGLLL GLYSSVAIWY ARLQEWDNFY KFSNRAKNLL 
      1460       1470       1480       1490       1500
PRRTMTLTYY DGISRYMEGQ VLHLQKQIKE QSENAQASGE ELLKNLENLV 
      1510       1520       1530       1540       1550
AQNTTGPVFC PRLYHLMAYV CILMGDGQKC GLFLNTALRL SETQGNILEK 
      1560       1570       1580       1590       1600
CWLNMNKESW YSTSELKEDQ WLQTILSLPS WEKIVAGRVN IQDLQKNKFL 
      1610
MRANTVDNHF

Length:1,610

Mass (Da):187,149

Last modified:October 5, 2010 - v3

Checksum:ⁱE0E205747120EFE0

Isoform 2 (identifier: Q96PN6-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-97: MNTPKEEFQD...IFGGDILKFA → MSLSE

« Hide

        10         20         30         40         50
MSLSEGDALL ALWRVERKQL KNIITVVIKC SLEIHGLFET QEWEEGLDIR 
        60         70         80         90        100
VKIGLAAGHI SMLVFGDETH SHFLVIGQAV DDVRLAQNMA QMNDVILSPN 
       110        120        130        140        150
CWQLCDRSMI EIESVPDQRA VKVNFLKPPP NFNFDEFFTK CTTFMHYYPS 
       160        170        180        190        200
GEHKNLLRLA CTLKPDPELE MSLQKYVMES ILKQIDNKQL QGYLSELRPV 
       210        220        230        240        250
TIVFVNLMFE DQDKAEEIGP AIQDAYMHIT SVLKIFQGQI NKVFMFDKGC 
       260        270        280        290        300
SFLCVFGFPG EKVPDELTHA LECAMDIFDF CSQVHKIQTV SIGVASGIVF 
       310        320        330        340        350
CGIVGHTVRH EYTVIGQKVN LAARMMMYYP GIVTCDSVTY NGSNLPAYFF 
       360        370        380        390        400
KELPKKVMKG VADSGPLYQY WGRTEKVMFG MACLICNRKE DYPLLGRNKE 
       410        420        430        440        450
INYFMYTMKK FLISNSSQVL MYEGLPGYGK SQILMKIEYL AQGKNHRIIA 
       460        470        480        490        500
ISLNKISFHQ TFYTIQMFMA NVLGLDTCKH YKERQTNLRN KVMTLLDEKF 
       510        520        530        540        550
YCLLNDIFHV QFPISREISR MSTLKKQKQL EILFMKILKL IVKEERIIFI 
       560        570        580        590        600
IDEAQFVDST SWRFMEKLIR TLPIFIIMSL CPFVNIPCAA ARAVIKNRNT 
       610        620        630        640        650
TYIVIGAVQP NDISNKICLD LNVSCISKEL DSYLGEGSCG IPFYCEELLK 
       660        670        680        690        700
NLEHHEVLVF QQTESEEKTN RTWNNLFKYS IKLTEKLNMV TLHSDKESEE 
       710        720        730        740        750
VCHLTSGVRL KNLSPPTSLK EISLIQLDSM RLSHQMLVRC AAIIGLTFTT 
       760        770        780        790        800
ELLFEILPCW NMKMMIKTLA TLVESNIFYC FRNGKELQKA LKQNDPSFEV 
       810        820        830        840        850
HYRSLSLKPS EGMDHGEEEQ LRELENEVIE CHRIRFCNPM MQKTAYELWL 
       860        870        880        890        900
KDQRKAMHLK CARFLEEDAH RCDHCRGRDF IPYHHFTVNI RLNALDMDAI 
       910        920        930        940        950
KKMAMSHGFK TEEKLILSNS EIPETSAFFP ENRSPEEIRE KILNFFDHVL 
       960        970        980        990       1000
TKMKTSDEDI IPLESCQCEE ILEIVILPLA HHFLALGEND KALYYFLEIA 
      1010       1020       1030       1040       1050
SAYLIFCDNY MAYMYLNEGQ KLLKTLKKDK SWSQTFESAT FYSLKGEVCF 
      1060       1070       1080       1090       1100
NMGQIVLAKK MLRKALKLLN RIFPYNLISL FLHIHVEKNR HFHYVNRQAQ 
      1110       1120       1130       1140       1150
ESPPPGKKRL AQLYRQTVCL SLLWRIYSYS YLFHCKYYAH LAVMMQMNTA 
      1160       1170       1180       1190       1200
LETQNCFQII KAYLDYSLYH HLAGYKGVWF KYEVMAMEHI FNLPLKGEGI 
      1210       1220       1230       1240       1250
EIVAYVAETL VFNKLIMGHL DLAIELGSRA LQMWALLQNP NRHYQSLCRL 
      1260       1270       1280       1290       1300
SRCLLLNSRY PQLIQVLGRL WELSVTQEHI FSKAFFYFVC LDILLYSGFV 
      1310       1320       1330       1340       1350
YRTFEECLEF IHQYENNRIL KFHSGLLLGL YSSVAIWYAR LQEWDNFYKF 
      1360       1370       1380       1390       1400
SNRAKNLLPR RTMTLTYYDG ISRYMEGQVL HLQKQIKEQS ENAQASGEEL 
      1410       1420       1430       1440       1450
LKNLENLVAQ NTTGPVFCPR LYHLMAYVCI LMGDGQKCGL FLNTALRLSE 
      1460       1470       1480       1490       1500
TQGNILEKCW LNMNKESWYS TSELKEDQWL QTILSLPSWE KIVAGRVNIQ 
      1510 
DLQKNKFLMR ANTVDNHF

Show »

Length:1,518

Mass (Da):176,591

Checksum:ⁱA533D2474085BF7E

Isoform 3 (identifier: Q96PN6-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1099: Missing.
     1100-1103: DNYM → MLFK
     1430-1471: YARLQEWDNF...GISRYMEGQV → ECEAGVGRRL...ELKIFCQEEP
     1472-1610: Missing.

« Hide

        10         20         30         40         50
MLFKAYMYLN EGQKLLKTLK KDKSWSQTFE SATFYSLKGE VCFNMGQIVL 
        60         70         80         90        100
AKKMLRKALK LLNRIFPYNL ISLFLHIHVE KNRHFHYVNR QAQESPPPGK 
       110        120        130        140        150
KRLAQLYRQT VCLSLLWRIY SYSYLFHCKY YAHLAVMMQM NTALETQNCF 
       160        170        180        190        200
QIIKAYLDYS LYHHLAGYKG VWFKYEVMAM EHIFNLPLKG EGIEIVAYVA 
       210        220        230        240        250
ETLVFNKLIM GHLDLAIELG SRALQMWALL QNPNRHYQSL CRLSRCLLLN 
       260        270        280        290        300
SRYPQLIQVL GRLWELSVTQ EHIFSKAFFY FVCLDILLYS GFVYRTFEEC 
       310        320        330        340        350
LEFIHQYENN RILKFHSGLL LGLYSSVAIW ECEAGVGRRL HTSRDPGMPD 
       360        370 
FRNGTTFTNF PIELKIFCQE EP

Show »

Length:372

Mass (Da):43,900

Checksum:ⁱE645DCFBE8E415A6

Isoform 4 (identifier: Q96PN6-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-153: Missing.

« Hide

        10         20         30         40         50
MLVFGDETHS HFLVIGQAVD DVRLAQNMAQ MNDVILSPNC WQLCDRSMIE 
        60         70         80         90        100
IESVPDQRAV KVNFLKPPPN FNFDEFFTKC TTFMHYYPSG EHKNLLRLAC 
       110        120        130        140        150
TLKPDPELEM SLQKYVMESI LKQIDNKQLQ GYLSELRPVT IVFVNLMFED 
       160        170        180        190        200
QDKAEEIGPA IQDAYMHITS VLKIFQGQIN KVFMFDKGCS FLCVFGFPGE 
       210        220        230        240        250
KVPDELTHAL ECAMDIFDFC SQVHKIQTVS IGVASGIVFC GIVGHTVRHE 
       260        270        280        290        300
YTVIGQKVNL AARMMMYYPG IVTCDSVTYN GSNLPAYFFK ELPKKVMKGV 
       310        320        330        340        350
ADSGPLYQYW GRTEKVMFGM ACLICNRKED YPLLGRNKEI NYFMYTMKKF 
       360        370        380        390        400
LISNSSQVLM YEGLPGYGKS QILMKIEYLA QGKNHRIIAI SLNKISFHQT 
       410        420        430        440        450
FYTIQMFMAN VLGLDTCKHY KERQTNLRNK VMTLLDEKFY CLLNDIFHVQ 
       460        470        480        490        500
FPISREISRM STLKKQKQLE ILFMKILKLI VKEERIIFII DEAQFVDSTS 
       510        520        530        540        550
WRFMEKLIRT LPIFIIMSLC PFVNIPCAAA RAVIKNRNTT YIVIGAVQPN 
       560        570        580        590        600
DISNKICLDL NVSCISKELD SYLGEGSCGI PFYCEELLKN LEHHEVLVFQ 
       610        620        630        640        650
QTESEEKTNR TWNNLFKYSI KLTEKLNMVT LHSDKESEEV CHLTSGVRLK 
       660        670        680        690        700
NLSPPTSLKE ISLIQLDSMR LSHQMLVRCA AIIGLTFTTE LLFEILPCWN 
       710        720        730        740        750
MKMMIKTLAT LVESNIFYCF RNGKELQKAL KQNDPSFEVH YRSLSLKPSE 
       760        770        780        790        800
GMDHGEEEQL RELENEVIEC HRIRFCNPMM QKTAYELWLK DQRKAMHLKC 
       810        820        830        840        850
ARFLEEDAHR CDHCRGRDFI PYHHFTVNIR LNALDMDAIK KMAMSHGFKT 
       860        870        880        890        900
EEKLILSNSE IPETSAFFPE NRSPEEIREK ILNFFDHVLT KMKTSDEDII 
       910        920        930        940        950
PLESCQCEEI LEIVILPLAH HFLALGENDK ALYYFLEIAS AYLIFCDNYM 
       960        970        980        990       1000
AYMYLNEGQK LLKTLKKDKS WSQTFESATF YSLKGEVCFN MGQIVLAKKM 
      1010       1020       1030       1040       1050
LRKALKLLNR IFPYNLISLF LHIHVEKNRH FHYVNRQAQE SPPPGKKRLA 
      1060       1070       1080       1090       1100
QLYRQTVCLS LLWRIYSYSY LFHCKYYAHL AVMMQMNTAL ETQNCFQIIK 
      1110       1120       1130       1140       1150
AYLDYSLYHH LAGYKGVWFK YEVMAMEHIF NLPLKGEGIE IVAYVAETLV 
      1160       1170       1180       1190       1200
FNKLIMGHLD LAIELGSRAL QMWALLQNPN RHYQSLCRLS RCLLLNSRYP 
      1210       1220       1230       1240       1250
QLIQVLGRLW ELSVTQEHIF SKAFFYFVCL DILLYSGFVY RTFEECLEFI 
      1260       1270       1280       1290       1300
HQYENNRILK FHSGLLLGLY SSVAIWYARL QEWDNFYKFS NRAKNLLPRR 
      1310       1320       1330       1340       1350
TMTLTYYDGI SRYMEGQVLH LQKQIKEQSE NAQASGEELL KNLENLVAQN 
      1360       1370       1380       1390       1400
TTGPVFCPRL YHLMAYVCIL MGDGQKCGLF LNTALRLSET QGNILEKCWL 
      1410       1420       1430       1440       1450
NMNKESWYST SELKEDQWLQ TILSLPSWEK IVAGRVNIQD LQKNKFLMRA 

NTVDNHF

Show »

Length:1,457

Mass (Da):169,750

Checksum:ⁱB148D881126ED9A7

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

U3KPS9	U3KPS9_HUMAN	Adenylate cyclase type 10 Adenylate cyclase type 10	ADCY10	73	Annotation score:
V9GY51	V9GY51_HUMAN	Adenylate cyclase type 10 Adenylate cyclase type 10	ADCY10	250	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	942	L → P in BAG64062 (PubMed:14702039).Curated		1
Sequence conflictⁱ	1359	L → P in AAK96045 (Ref. 4) Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_038476	234	T → M. Corresponds to variant dbSNP:rs16859886Ensembl.		1
Natural variantⁱVAR_038477	697	I → V3 PublicationsCorresponds to variant dbSNP:rs2071921Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_030866	1 – 1099	Missing in isoform 3. 1 PublicationAdd BLAST	1099
Alternative sequenceⁱVSP_046329	1 – 153	Missing in isoform 4. 1 PublicationAdd BLAST	153
Alternative sequenceⁱVSP_030867	1 – 97	MNTPK…ILKFA → MSLSE in isoform 2. 1 PublicationAdd BLAST	97
Alternative sequenceⁱVSP_030868	1100 – 1103	DNYM → MLFK in isoform 3. 1 Publication	4
Alternative sequenceⁱVSP_030869	1430 – 1471	YARLQ…MEGQV → ECEAGVGRRLHTSRDPGMPD FRNGTTFTNFPIELKIFCQE EP in isoform 3. 1 PublicationAdd BLAST	42
Alternative sequenceⁱVSP_030870	1472 – 1610	Missing in isoform 3. 1 PublicationAdd BLAST	139

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF271058 mRNA Translation: AAF74296.1 AF331033 mRNA Translation: AAL57036.1 AF176813 mRNA Translation: AAF65931.1 AF299350 mRNA Translation: AAK96045.1 AL035122 mRNA Translation: CAA22684.1 AK302884 mRNA Translation: BAG64062.1 Z97876 Genomic DNA No translation available. Z99943 Genomic DNA No translation available. CH471067 Genomic DNA Translation: EAW90804.1 CH471067 Genomic DNA Translation: EAW90807.1 BC117366 mRNA Translation: AAI17367.1 BC117372 mRNA Translation: AAI17373.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1265.1 [Q96PN6-1] CCDS53426.1 [Q96PN6-4] CCDS72977.1 [Q96PN6-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001161221.1, NM_001167749.2 [Q96PN6-4] NP_001284701.1, NM_001297772.1 [Q96PN6-2] NP_060887.2, NM_018417.5 [Q96PN6-1] XP_011508062.1, XM_011509760.2 [Q96PN6-1]

Genome annotation databases

Ensemblⁱ	ENST00000367848; ENSP00000356822; ENSG00000143199 [Q96PN6-2] ENST00000367851; ENSP00000356825; ENSG00000143199 [Q96PN6-1] ENST00000545172; ENSP00000441992; ENSG00000143199 [Q96PN6-4]
GeneIDⁱ	55811
KEGGⁱ	hsa:55811
UCSC genome browser More...UCSCⁱ	uc001ger.4, human [Q96PN6-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q96PN6	Adenylate cyclase type 10		HUMAN		1610	UniRef100_Q96PN6
Isoform 4 of Adenylate cyclase type 10		HUMAN		1457

Protein	Similar proteins		Species	Score	Length	Source
Q96PN6	Adenylate cyclase type 10		HUMAN		1610	UniRef90_Q96PN6
Adenylate cyclase type 10		PANTR		1610
Adenylate cyclase type 10		PONAB		1610
Adenylate cyclase type 10		PANPA		1610
Adenylate cyclase type 10		GORGO		1610
+25

Protein	Similar proteins		Species	Score	Length	Source
Q96PN6	Adenylate cyclase type 10		MOUSE		1614	UniRef50_Q96PN6
Adenylate cyclase type 10		RABIT		1610
Adenylate cyclase type 10		RAT		1608
Adenylate cyclase type 10		HUMAN		1610
Adenylate cyclase type 10		PONAB		1610
+354

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF271058 mRNA Translation: AAF74296.1 AF331033 mRNA Translation: AAL57036.1 AF176813 mRNA Translation: AAF65931.1 AF299350 mRNA Translation: AAK96045.1 AL035122 mRNA Translation: CAA22684.1 AK302884 mRNA Translation: BAG64062.1 Z97876 Genomic DNA No translation available. Z99943 Genomic DNA No translation available. CH471067 Genomic DNA Translation: EAW90804.1 CH471067 Genomic DNA Translation: EAW90807.1 BC117366 mRNA Translation: AAI17367.1 BC117372 mRNA Translation: AAI17373.1
CCDSⁱ	CCDS1265.1 [Q96PN6-1] CCDS53426.1 [Q96PN6-4] CCDS72977.1 [Q96PN6-2]
RefSeqⁱ	NP_001161221.1, NM_001167749.2 [Q96PN6-4] NP_001284701.1, NM_001297772.1 [Q96PN6-2] NP_060887.2, NM_018417.5 [Q96PN6-1] XP_011508062.1, XM_011509760.2 [Q96PN6-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4CLF	X-ray	1.70	A	1-469	[»]
	4CLK	X-ray	2.20	A	1-469	[»]
	4CLL	X-ray	1.70	A	1-469	[»]
	4CLP	X-ray	1.90	A	1-469	[»]
	4CLS	X-ray	1.85	A	1-469	[»]
	4CLT	X-ray	1.95	A	1-469	[»]
	4CLU	X-ray	1.90	A	1-469	[»]
	4CLW	X-ray	2.15	A	1-469	[»]
	4CLY	X-ray	2.05	A	1-469	[»]
	4CLZ	X-ray	1.90	A	1-469	[»]
	4CM0	X-ray	3.20	A	1-469	[»]
	4CM2	X-ray	1.80	A	1-469	[»]
	4OYA	X-ray	2.03	A	1-469	[»]
	4OYB	X-ray	1.70	A	1-469	[»]
	4OYI	X-ray	1.70	A	1-469	[»]
	4OYM	X-ray	1.70	A	1-469	[»]
	4OYO	X-ray	1.75	A	1-469	[»]
	4OYP	X-ray	2.28	A	1-469	[»]
	4OYW	X-ray	1.70	A	1-469	[»]
	4OYX	X-ray	1.89	A	1-469	[»]
	4OYZ	X-ray	1.74	A	1-469	[»]
	4OZ2	X-ray	2.10	A	1-469	[»]
	4OZ3	X-ray	1.70	A	1-469	[»]
	4UST	X-ray	1.90	A	1-469	[»]
	4USU	X-ray	1.95	A	1-469	[»]
	4USV	X-ray	2.00	A	1-469	[»]
	4USW	X-ray	2.05	A	1-469	[»]
	5D0R	X-ray	2.24	A	1-469	[»]
	5IV3	X-ray	1.86	A	1-469	[»]
	5IV4	X-ray	1.79	A	1-469	[»]
SMRⁱ	Q96PN6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	120921, 1 interactor
IntActⁱ	Q96PN6, 1 interactor
STRINGⁱ	9606.ENSP00000356825

Chemistry databases

BindingDBⁱ	Q96PN6
ChEMBLⁱ	CHEMBL5854
GuidetoPHARMACOLOGYⁱ	3068

PTM databases

iPTMnetⁱ	Q96PN6
PhosphoSitePlusⁱ	Q96PN6
SwissPalmⁱ	Q96PN6

Polymorphism and mutation databases

BioMutaⁱ	ADCY10
DMDMⁱ	308153637

Proteomic databases

EPDⁱ	Q96PN6
MassIVEⁱ	Q96PN6
PaxDbⁱ	Q96PN6
PeptideAtlasⁱ	Q96PN6
PRIDEⁱ	Q96PN6
ProteomicsDBⁱ	24204 77715 [Q96PN6-1] 77716 [Q96PN6-2] 77717 [Q96PN6-3]

Protocols and materials databases

Antibodypediaⁱ	3017, 138 antibodies

Antibodypediaⁱ

3017, 138 antibodies

Genome annotation databases

Ensemblⁱ	ENST00000367848; ENSP00000356822; ENSG00000143199 [Q96PN6-2] ENST00000367851; ENSP00000356825; ENSG00000143199 [Q96PN6-1] ENST00000545172; ENSP00000441992; ENSG00000143199 [Q96PN6-4]
GeneIDⁱ	55811
KEGGⁱ	hsa:55811
UCSCⁱ	uc001ger.4, human [Q96PN6-1]

Organism-specific databases

CTDⁱ	55811
DisGeNETⁱ	55811
EuPathDBⁱ	HostDB:ENSG00000143199.17
GeneCardsⁱ	ADCY10
HGNCⁱ	HGNC:21285, ADCY10
HPAⁱ	ENSG00000143199, Group enriched (liver, testis)
MalaCardsⁱ	ADCY10
MIMⁱ	143870, phenotype 605205, gene
neXtProtⁱ	NX_Q96PN6
OpenTargetsⁱ	ENSG00000143199
Orphanetⁱ	2197, Idiopathic hypercalciuria
PharmGKBⁱ	PA162375618
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG502QPPT, Eukaryota
GeneTreeⁱ	ENSGT00390000001322
HOGENOMⁱ	CLU_004055_1_0_1
InParanoidⁱ	Q96PN6
KOⁱ	K11265
OMAⁱ	TVDIRLN
PhylomeDBⁱ	Q96PN6
TreeFamⁱ	TF329284

Enzyme and pathway databases

BRENDAⁱ	4.6.1.1, 2681
PathwayCommonsⁱ	Q96PN6
Reactomeⁱ	R-HSA-5610787, Hedgehog 'off' state
SIGNORⁱ	Q96PN6

Miscellaneous databases

BioGRID-ORCSⁱ	55811, 5 hits in 870 CRISPR screens
ChiTaRSⁱ	ADCY10, human
GeneWikiⁱ	ADCY10
GenomeRNAiⁱ	55811
Pharosⁱ	Q96PN6, Tchem
Protein Ontology More...PROⁱ	PR:Q96PN6
RNActⁱ	Q96PN6, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000143199, Expressed in testis and 97 other tissues
ExpressionAtlasⁱ	Q96PN6, baseline and differential
Genevisibleⁱ	Q96PN6, HS

Family and domain databases

Gene3Dⁱ	3.30.70.1230, 2 hits
InterProⁱ	View protein in InterPro IPR001054, A/G_cyclase IPR016577, Adenylate_cyclase_typ10 IPR029787, Nucleotide_cyclase IPR027417, P-loop_NTPase
Pfamⁱ	View protein in Pfam PF00211, Guanylate_cyc, 2 hits
PIRSFⁱ	PIRSF011131, Soluble_adenylyl_cyclase, 1 hit
SUPFAMⁱ	SSF52540, SSF52540, 1 hit SSF55073, SSF55073, 2 hits
PROSITEⁱ	View protein in PROSITE PS50125, GUANYLATE_CYCLASE_2, 2 hits
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ADCYA_HUMAN
Accessionⁱ	Q96PN6Primary (citable) accession number: Q96PN6 Secondary accession number(s): B4DZF0 Q9NNX0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
	Last sequence update:	October 5, 2010
	Last modified:	August 12, 2020
	This is version 157 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM

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UniProtKB - Q96PN6 (ADCYA_HUMAN)

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Adenylate cyclase type 10

ADCY10

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Plasma membrane

Cytoskeleton

Nucleus

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Mitochondrion

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ