Reviewed, UniProtKB/Swiss-Prot P30803 (ADCY5_CANFA)

Names and origin

Protein names

Recommended name:
    Adenylate cyclase type 5
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type V
    ATP pyrophosphate-lyase 5
    Adenylyl cyclase 5
    Ca(2+)-inhibitable adenylyl cyclase

Gene names

Name:

ADCY5

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	1265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a membrane-bound, calcium-inhibitable adenylyl cyclase.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit.
Enzyme regulation	The activity was inhibited in a concentration-dependent manner with either P-site active agents such as adenosine or in the presence of calcium.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Most abundant in heart but weakly detectable in brain.
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	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from electronic annotation. Source: EC 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: P30803-1)

Also known as: V;

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: P30803-2)

Also known as: V-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     653-677: KEEKAMIAKMNRQRTNSIGHNPPHW → VRRGGGGPRPGGADSPGWWGASAGP
     678-1265: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1265

1265

Adenylate cyclase type 5

PRO_0000195693

Regions

Topological domain

1 – 244

244

Cytoplasmic Potential

Transmembrane

245 – 265

21

Potential

Transmembrane

271 – 291

21

Potential

Transmembrane

302 – 322

21

Potential

Transmembrane

328 – 348

21

Potential

Transmembrane

352 – 372

21

Potential

Transmembrane

377 – 397

21

Potential

Topological domain

398 – 765

368

Cytoplasmic Potential

Transmembrane

766 – 786

21

Potential

Transmembrane

792 – 812

21

Potential

Transmembrane

839 – 859

21

Potential

Transmembrane

908 – 928

21

Potential

Transmembrane

930 – 950

21

Potential

Transmembrane

988 – 1008

21

Potential

Topological domain

1009 – 1265

257

Cytoplasmic Potential

Domain

472 – 599

128

Guanylate cyclase 1

Domain

1075 – 1214

140

Guanylate cyclase 2

Sites

Metal binding

477

1

Magnesium 1

Metal binding

477

1

Magnesium 2

Metal binding

478

1

Magnesium 2; via carbonyl oxygen

Metal binding

521

1

Magnesium 1

Metal binding

521

1

Magnesium 2

Amino acid modifications

Modified residue

8

1

Phosphoserine By similarity

Glycosylation

873

1

N-linked (GlcNAc...) Potential

Glycosylation

890

1

N-linked (GlcNAc...) Potential

Glycosylation

976

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

653 – 677

25

KEEKA…NPPHW → VRRGGGGPRPGGADSPGWWG ASAGP in isoform 2.

VSP_000242

Alternative sequence

678 – 1265

588

Missing in isoform 2.

VSP_000243

Secondary structure

1

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1265

Helix Strand Turn

Details...

Beta strand

464 – 479

16

Helix

481 – 487

7

Helix

490 – 511

22

Beta strand

514 – 519

6

Beta strand

522 – 527

6

Helix

536 – 558

23

Beta strand

563 – 577

15

Beta strand

579 – 582

4

Beta strand

586 – 589

4

Helix

590 – 600

11

Beta strand

606 – 609

4

Turn

612 – 619

8

Beta strand

623 – 625

3

Helix

628 – 630

3

Helix

633 – 637

5

Beta strand

643 – 645

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (V) [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 414322F64153DFB4	FASTA	1,265	140,319
	10 20 30 40 50 60 MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP GGAVTPQLQQ 70 80 90 100 110 120 QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL GGDDPLAGGF GFSFRSRSAW 130 140 150 160 170 180 QERGGDDCGR GSRRRRRGAA GGGSSRAPPA GGGGGPAAAG GAEVRPRSVE LGLDERRGRG 190 200 210 220 230 240 RAEPEPEAEA GAPGGDRGAR DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL 250 260 270 280 290 300 NQSSLTMLMA VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH 310 320 330 340 350 360 MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM RAAVLSGVLL 370 380 390 400 410 420 SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA 430 440 450 460 470 480 RLHSQRENQQ QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG 490 500 510 520 530 540 FTSLASQCTA QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC 550 560 570 580 590 600 VEMGMDMIEA ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA 610 620 630 640 650 660 GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA 670 680 690 700 710 720 KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD 730 740 750 760 770 780 EFLGRAIDAR SIDRLRSEHV RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF 790 800 810 820 830 840 VQITIVPHSV FMLSFYLTCF LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV 850 860 870 880 890 900 GVFTITLVFL SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC 910 920 930 940 950 960 GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV EVPRVTLFDN 970 980 990 1000 1010 1020 ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV FVLALYLHAQ QVESTARLDF 1030 1040 1050 1060 1070 1080 LWKLQATEEK EEMEELQAYN RRLLHNILPK DVAAHFLARE RRNDELYYQS CECVAVMFAS 1090 1100 1110 1120 1130 1140 IANFSEFYVE LEANNEGVEC LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN 1150 1160 1170 1180 1190 1200 DSTYDKVGKT HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY 1210 1220 1230 1240 1250 1260 DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK GEMMTYFLNG GPPLS
	Isoform 2 (V-alpha). Checksum: AAB94BCFEBE08CC0	FASTA	677	73,690
	10 20 30 40 50 60 MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP GGAVTPQLQQ 70 80 90 100 110 120 QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL GGDDPLAGGF GFSFRSRSAW 130 140 150 160 170 180 QERGGDDCGR GSRRRRRGAA GGGSSRAPPA GGGGGPAAAG GAEVRPRSVE LGLDERRGRG 190 200 210 220 230 240 RAEPEPEAEA GAPGGDRGAR DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL 250 260 270 280 290 300 NQSSLTMLMA VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH 310 320 330 340 350 360 MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM RAAVLSGVLL 370 380 390 400 410 420 SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA 430 440 450 460 470 480 RLHSQRENQQ QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG 490 500 510 520 530 540 FTSLASQCTA QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC 550 560 570 580 590 600 VEMGMDMIEA ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA 610 620 630 640 650 660 GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRVRRGGGGP 670 RPGGADSPGW WGASAGP

References

[1]	"Isolation and characterization of a novel cardiac adenylylcyclase cDNA." Ishikawa Y., Katsushika S., Chen L., Halnon N.J., Kawabe J., Homcy C.J. J. Biol. Chem. 267:13553-13557(1992) [PubMed: 1618857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart muscle.
[2]	"In vivo generation of an adenylylcyclase isoform with a half-molecule motif." Katsushika S., Kawabe J., Homcy C.J., Ishikawa Y. J. Biol. Chem. 268:2273-2276(1993) [PubMed: 8428899] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Heart muscle.
[3]	Tomlinson J., Okumura S., Ishikawa Y. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[4]	"Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS." Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R. Science 278:1907-1916(1997) [PubMed: 9417641] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
[5]	"Two-metal-ion catalysis in adenylyl cyclase." Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R. Science 285:756-760(1999) [PubMed: 10427002] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M88649 mRNA. Translation: AAC32726.1.
M97886 mRNA. Translation: AAA30827.1. Sequence problems.

PIR

A42904.
A45195.

UniGene

Cfa.1267

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZS	X-ray	2.30	A	444-656	[»]
1CJK	X-ray	3.00	A	445-661	[»]
1CJT	X-ray	2.80	A	445-661	[»]
1CJU	X-ray	2.80	A	445-661	[»]
1CJV	X-ray	3.00	A	445-661	[»]
1CS4	X-ray	2.50	A	444-661	[»]
1CUL	X-ray	2.40	A	445-661	[»]
1TL7	X-ray	2.80	A	445-661	[»]
1U0H	X-ray	2.90	A	444-661	[»]
2GVD	X-ray	2.90	A	444-661	[»]
2GVZ	X-ray	3.27	A	444-661	[»]
3C14	X-ray	2.68	A	444-661	[»]
3C15	X-ray	2.78	A	444-661	[»]
3C16	X-ray	2.87	A	444-661	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:179N.

Genome annotation databases

Ensembl

ENSCAFG00000012084. Canis familiaris. [Contig view]

Phylogenomic databases

HOVERGEN

P30803.

Enzyme and pathway databases

BRENDA

4.6.1.1. 463.

Family and domain databases

InterPro

IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Aden_cycl-like.
[Graphical view]

Gene3D

G3DSA:3.30.70.1230. A/G_cyclase. 2 hits.

Pfam

PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]

SMART

SM00044. CYCc. 2 hits.
[Graphical view]

PROSITE

PS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ADCY5_CANFA

Accession

Primary (citable) accession number: P30803

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)