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Protein

Adenylate cyclase type 5

Gene

ADCY5

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Isoform 1: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:1618857, PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca2+ in response to increased blood glucose levels and contributes to the regulation of Ca2+-dependent insulin secretion (By similarity).By similarity7 Publications
Isoform 2: Lacks catalytic activity by itself, but can associate with isoform 1 to form active adenylyl cyclase.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+3 Publications, Mn2+2 PublicationsNote: Binds 2 magnesium ions per subunit (PubMed:16766715, PubMed:19243146). Is also active with manganese (in vitro) (PubMed:11087399, PubMed:16766715).1 Publication3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by forskolin (PubMed:1618857, PubMed:8428899). Activated by GNAS. Activity is further increased by interaction with the G-protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (PubMed:1618857). Phosphorylation by RAF1 results in its activation (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi477Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi477Magnesium 2; catalytic1 Publication1
Metal bindingi478Magnesium 2; via carbonyl oxygen; catalytic1 Publication1
Metal bindingi521Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi521Magnesium 2; catalytic1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei565ATP4 Publications1
Binding sitei1127ATPBy similarity1
Binding sitei1248ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi477 – 482ATP4 Publications6
Nucleotide bindingi519 – 521ATP4 Publications3
Nucleotide bindingi1201 – 1203ATPBy similarity3
Nucleotide bindingi1208 – 1212ATPBy similarity5

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processcAMP biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Adenylate cyclase type 5 (EC:4.6.1.17 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 5
Adenylate cyclase type V
Adenylyl cyclase 5
Ca(2+)-inhibitable adenylyl cyclase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ADCY5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9615 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002254 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 244CytoplasmicSequence analysisAdd BLAST244
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Transmembranei271 – 291HelicalSequence analysisAdd BLAST21
Transmembranei302 – 322HelicalSequence analysisAdd BLAST21
Transmembranei328 – 348HelicalSequence analysisAdd BLAST21
Transmembranei352 – 372HelicalSequence analysisAdd BLAST21
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 765CytoplasmicSequence analysisCuratedAdd BLAST368
Transmembranei766 – 786HelicalSequence analysisAdd BLAST21
Transmembranei792 – 812HelicalSequence analysisAdd BLAST21
Transmembranei839 – 859HelicalSequence analysisAdd BLAST21
Transmembranei908 – 928HelicalSequence analysisAdd BLAST21
Transmembranei930 – 950HelicalSequence analysisAdd BLAST21
Transmembranei988 – 1008HelicalSequence analysisAdd BLAST21
Topological domaini1009 – 1265CytoplasmicSequence analysisCuratedAdd BLAST257

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi477D → A or N: Almost abolishes enzyme activity. Abolishes enzyme activity; when associated with A-521 or N-521. 1 Publication1
Mutagenesisi521D → A or N: Almost abolishes enzyme activity. Abolishes enzyme activity; when associated with A-396 or N-396. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001956931 – 1265Adenylate cyclase type 5Add BLAST1265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei16Omega-N-methylarginineBy similarity1
Modified residuei113PhosphoserineBy similarity1
Modified residuei168PhosphoserineBy similarity1
Modified residuei669PhosphoserineBy similarity1
Modified residuei757PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi873N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi890N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi976N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1015PhosphothreonineBy similarity1

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P30803

PRoteomics IDEntifications database

More...
PRIDEi
P30803

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is detected in heart, and at lower levels in brain (PubMed:1618857). Isoform 2 is detected in heart (PubMed:8428899).2 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with GNAS (PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (By similarity).By similarity6 Publications

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-179N

Protein interaction database and analysis system

More...
IntActi
P30803, 1 interactor

STRING: functional protein association networks

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STRINGi
9615.ENSCAFP00000017783

<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

11265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P30803

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P30803

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30803

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini472 – 599Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST128
Domaini1075 – 1214Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST140

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.5 Publications

<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

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3619 Eukaryota
COG2114 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000006941

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050458

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P30803

KEGG Orthology (KO)

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KOi
K08045

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.1230, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR009398 Adcy_conserved_dom
IPR029787 Nucleotide_cyclase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16214 AC_N, 1 hit
PF06327 DUF1053, 1 hit
PF00211 Guanylate_cyc, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF039050 Ade_cyc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00044 CYCc, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55073 SSF55073, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P30803-1) [UniParc]FASTAAdd to basket
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.

« Hide
        10         20         30         40         50
MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP
60 70 80 90 100
GGAVTPQLQQ QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL
110 120 130 140 150
GGDDPLAGGF GFSFRSRSAW QERGGDDCGR GSRRRRRGAA GGGSSRAPPA
160 170 180 190 200
GGGGGPAAAG GAEVRPRSVE LGLDERRGRG RAEPEPEAEA GAPGGDRGAR
210 220 230 240 250
DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL NQSSLTMLMA
260 270 280 290 300
VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH
310 320 330 340 350
MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM
360 370 380 390 400
RAAVLSGVLL SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH
410 420 430 440 450
YPAEVSQRQA FQETRECIQA RLHSQRENQQ QERLLLSVLP RHVAMEMKAD
460 470 480 490 500
INAKQEDMMF HKIYIQKHDN VSILFADIEG FTSLASQCTA QELVMTLNEL
510 520 530 540 550
FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC VEMGMDMIEA
560 570 580 590 600
ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA
610 620 630 640 650
GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ
660 670 680 690 700
KRKEEKAMIA KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG
710 720 730 740 750
FEDPKDKNAQ ESANPEDEVD EFLGRAIDAR SIDRLRSEHV RKFLLTFREP
760 770 780 790 800
DLEKKYSKQV DDRFGAYVAC ASLVFLFICF VQITIVPHSV FMLSFYLTCF
810 820 830 840 850
LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV GVFTITLVFL
860 870 880 890 900
SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC
910 920 930 940 950
GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV
960 970 980 990 1000
EVPRVTLFDN ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV
1010 1020 1030 1040 1050
FVLALYLHAQ QVESTARLDF LWKLQATEEK EEMEELQAYN RRLLHNILPK
1060 1070 1080 1090 1100
DVAAHFLARE RRNDELYYQS CECVAVMFAS IANFSEFYVE LEANNEGVEC
1110 1120 1130 1140 1150
LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN DSTYDKVGKT
1160 1170 1180 1190 1200
HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY
1210 1220 1230 1240 1250
DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK
1260
GEMMTYFLNG GPPLS
Length:1,265
Mass (Da):140,319
Last modified:May 30, 2000 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i414322F64153DFB4
GO
Isoform 2 (identifier: P30803-2) [UniParc]FASTAAdd to basket
Also known as: V-alpha

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

Show »
Length:677
Mass (Da):73,690
Checksum:iAAB94BCFEBE08CC0
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000242653 – 677KEEKA…NPPHW → VRRGGGGPRPGGADSPGWWG ASAGP in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_000243678 – 1265Missing in isoform 2. 1 PublicationAdd BLAST588

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M88649 mRNA Translation: AAC32726.1
M97886 mRNA Translation: AAA30827.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
A42904
A45195

NCBI Reference Sequences

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RefSeqi
NP_001161932.1, NM_001168460.1 [P30803-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Cfa.1267

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
403859

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cfa:403859

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88649 mRNA Translation: AAC32726.1
M97886 mRNA Translation: AAA30827.1 Sequence problems.
PIRiA42904
A45195
RefSeqiNP_001161932.1, NM_001168460.1 [P30803-1]
UniGeneiCfa.1267

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30A442-656[»]
1CJKX-ray3.00A445-661[»]
1CJTX-ray2.80A445-661[»]
1CJUX-ray2.80A445-661[»]
1CJVX-ray3.00A445-661[»]
1CS4X-ray2.50A442-661[»]
1CULX-ray2.40A445-661[»]
1TL7X-ray2.80A445-661[»]
1U0HX-ray2.90A442-661[»]
2GVDX-ray2.90A444-661[»]
2GVZX-ray3.27A444-661[»]
3C14X-ray2.68A444-661[»]
3C15X-ray2.78A444-661[»]
3C16X-ray2.87A444-661[»]
3G82X-ray3.11A444-661[»]
3MAAX-ray3.00A444-661[»]
ProteinModelPortaliP30803
SMRiP30803
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-179N
IntActiP30803, 1 interactor
STRINGi9615.ENSCAFP00000017783

Proteomic databases

PaxDbiP30803
PRIDEiP30803

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403859
KEGGicfa:403859

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
111

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiP30803
KOiK08045

Miscellaneous databases

EvolutionaryTraceiP30803

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR009398 Adcy_conserved_dom
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF06327 DUF1053, 1 hit
PF00211 Guanylate_cyc, 2 hits
PIRSFiPIRSF039050 Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044 CYCc, 2 hits
SUPFAMiSSF55073 SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADCY5_CANLF
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P30803
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: December 5, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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