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Protein

Adenylate cyclase type 3

Gene

Adcy3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:9768837, PubMed:11055432, PubMed:25329148). Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis (PubMed:9768837, PubMed:11055432). Required for the perception of odorants (PubMed:11055432). Required for normal sperm motility and normal male fertility (PubMed:15705663). Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet (PubMed:25329148).3 Publications

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.3 Publications

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Enzyme regulationi

Activated by forskolin (PubMed:11055432, PubMed:25329148). After forskolin treatment, activity is further increased by calcium/calmodulin. In the absence of forskolin, calcium/calmodulin has little effect on enzyme activity (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi324 – 3241Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi324 – 3241Magnesium 2; catalyticPROSITE-ProRule annotation
Metal bindingi325 – 3251Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi368 – 3681Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi368 – 3681Magnesium 2; catalyticPROSITE-ProRule annotation
Binding sitei412 – 4121ATPBy similarity
Binding sitei976 – 9761ATPBy similarity
Binding sitei1110 – 11101ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi324 – 3296ATPBy similarity
Nucleotide bindingi366 – 3683ATPBy similarity
Nucleotide bindingi1063 – 10653ATPBy similarity
Nucleotide bindingi1070 – 10745ATPBy similarity

GO - Molecular functioni

  • adenylate cyclase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: Ensembl
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • acrosome reaction Source: UniProtKB
  • activation of adenylate cyclase activity Source: MGI
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • cAMP biosynthetic process Source: UniProtKB
  • cAMP-mediated signaling Source: GO_Central
  • cellular response to forskolin Source: UniProtKB
  • female meiotic division Source: Ensembl
  • olfactory learning Source: UniProtKB
  • sensory perception of smell Source: UniProtKB
  • single fertilization Source: UniProtKB
  • sperm motility Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis, Olfaction, Sensory transduction

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-MMU-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 3 (EC:4.6.1.13 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 3
Adenylate cyclase type III
Short name:
AC-III
Adenylate cyclase, olfactive type
Adenylyl cyclase 3
Short name:
AC31 Publication
Gene namesi
Name:Adcy3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:99675. Adcy3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7979CytoplasmicSequence analysisAdd
BLAST
Transmembranei80 – 10021HelicalSequence analysisAdd
BLAST
Transmembranei105 – 12521HelicalSequence analysisAdd
BLAST
Transmembranei139 – 15921HelicalSequence analysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence analysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence analysisAdd
BLAST
Topological domaini402 – 631230CytoplasmicSequence analysisAdd
BLAST
Transmembranei632 – 65221HelicalSequence analysisAdd
BLAST
Transmembranei663 – 68321HelicalSequence analysisAdd
BLAST
Transmembranei707 – 72721HelicalSequence analysisAdd
BLAST
Transmembranei753 – 77321HelicalSequence analysisAdd
BLAST
Transmembranei774 – 79421HelicalSequence analysisAdd
BLAST
Transmembranei834 – 85421HelicalSequence analysisAdd
BLAST
Topological domaini855 – 1145291CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cilium Source: UniProtKB
  • cytoplasm Source: MGI
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: MGI
  • membrane raft Source: Ensembl
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate, but up to 80% of the pups die within 48 h after birth. Survival is improved by paring down the litter size shortly after birth. Mutant mice are initially smaller than wild-type, but achieve normal size within three months. Mutant mice do not display the normal electrophysiological responses to odorants that stimulate production of cAMP or inositoltrisphosphate (IP3). Likewise, behavorial responses to smells are abolished (PubMed:11055432). In spite of normal mating behavior, they do not produce any offspring (PubMed:11055432, PubMed:15705663). Male mice have strongly reduced fertility due to defects in sperm motility, an increased rate of spontaneous acrosome reactions and an impaired ability to penetrate the oocyte zona (PubMed:15705663).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi279 – 2791M → I in Jll; dominant allele that increases enzyme activity, and decreases fasting insulin levels, fasting leptin levels, weight gain and fat accumulation when mice are kept on a high fat diet. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11451145Adenylate cyclase type 3PRO_0000195688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki465 – 465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)By similarity
Modified residuei579 – 5791PhosphoserineCombined sources
Glycosylationi735 – 7351N-linked (GlcNAc...)Sequence analysis
Modified residuei1077 – 10771Phosphoserine; by CaMK21 Publication

Post-translational modificationi

N-glycosylated.1 Publication
Rapidly phosphorylated after stimulation by odorants or forskolin. Phosphorylation by CaMK2 at Ser-1077 down-regulates enzyme activity.1 Publication
Sumoylated (PubMed:25908845). Sumoylation is required for targeting ot olfactory cilia.By similarity1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8VHH7.
PaxDbiQ8VHH7.
PRIDEiQ8VHH7.

PTM databases

iPTMnetiQ8VHH7.
PhosphoSiteiQ8VHH7.

Expressioni

Tissue specificityi

Detected in the acrosomal region of epididymal spermatozoa, the acrosomal region of round spermatids and in elongating spermatids (PubMed:15705663). Detected in cilia in the olfactory epithelium (at protein level) (PubMed:9768837, PubMed:11055432, PubMed:25908845). Detected in olfactory epithelium neurons (PubMed:11055432). Detected in brain, testis, late pachytene spermatocytes, round spermatids and elongating spermatids (PubMed:15705663).2 Publications

Gene expression databases

BgeeiQ8VHH7.
CleanExiMM_ADCY3.
ExpressionAtlasiQ8VHH7. baseline and differential.
GenevisibleiQ8VHH7. MM.

Interactioni

Protein-protein interaction databases

BioGridi222368. 2 interactions.
IntActiQ8VHH7. 1 interaction.
MINTiMINT-7290275.
STRINGi10090.ENSMUSP00000020984.

Structurei

3D structure databases

ProteinModelPortaliQ8VHH7.
SMRiQ8VHH7. Positions 307-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ8VHH7.
OMAiNIYAWRP.
OrthoDBiEOG7B8S30.
PhylomeDBiQ8VHH7.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VHH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRNQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP
60 70 80 90 100
RFMRLTFVPE SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF
110 120 130 140 150
SSDKLAPLMV AGFGLVLDII LFVLCKKGLL PDRVSRKVVP YLLWLLISAQ
160 170 180 190 200
IFSYLGLNFS RAHAASDTVG WQAFFVFSFF ITLPLSLSPI VIISVVSCVV
210 220 230 240 250
HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG IMSYYMADRK
260 270 280 290 300
HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
310 320 330 340 350
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR
360 370 380 390 400
FDKLAAKYHQ LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY
410 420 430 440 450
VREKTKTGVD MRVGVHTGTV LGGVLGQKRW QYDVWSTDVT VANKMEAGGI
460 470 480 490 500
PGRVHISQST MDCLKGEFDV EPGDGGSRCD YLDEKGIETY LIIASKPEVK
510 520 530 540 550
KTAQNGLNGS AVPNGAPASS KPSSPALIET KEPNGSAHAS GSTSEEAEEQ
560 570 580 590 600
EAQADNPSFP NPRRRLRLQD LADRVVDASE DEHELNQLLN EALLERESAQ
610 620 630 640 650
VVKKRNTFLL TMRFMDPEME TRYSVEKEKQ SGAAFSCSCV VLFCTAMVEI
660 670 680 690 700
LIDPWLMTNY VTFVVGEVLL LILTICSMAA IFPRSFPKKL VAFSSWIDRT
710 720 730 740 750
RWARNTWAML AIFILVMANV VDMLSCLQYY MGPYNMTAGM ELDGGCMENP
760 770 780 790 800
KYYNYVAVLS LIATIMLVQV SHMVKLTLML LVTGAVTALN LYAWCPVFDE
810 820 830 840 850
YDHKRFQEKD SPMVALEKMQ VLATPGLNGT DSRLPLVPSK YSMTVMMFVM
860 870 880 890 900
MLSFYYFSRH VEKLARTLFL WKIEVHDQKE RVYEMRRWNE ALVTNMLPEH
910 920 930 940 950
VARHFLGSKK RDEELYSQSY DEIGVMFASL PNFADFYTEE SINNGGIECL
960 970 980 990 1000
RFLNEIISDF DSLLDNPKFR VITKIKTIGS TYMAASGVTP DVNTNGFTSS
1010 1020 1030 1040 1050
SKEEKSDKER WQHLADLADF ALAMKDTLTN INNQSFNNFM LRIGMNKGGV
1060 1070 1080 1090 1100
LAGVIGARKP HYDIWGNTVN VASRMESTGV MGNIQVVEET QVILREYGFR
1110 1120 1130 1140
FVRRGPIFVK GKGELLTFFL KGRDRPAAFP NGSSVTLPHQ VVDNP
Length:1,145
Mass (Da):129,085
Last modified:July 27, 2011 - v2
Checksum:i09195176F4B3D61F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521F → L in AAL59384 (Ref. 1) Curated
Sequence conflicti833 – 8353RLP → MLL in AAL59384 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458089 mRNA. Translation: AAL59384.1.
CT572999 Genomic DNA. Translation: CAX15321.1.
CH466623 Genomic DNA. Translation: EDL01374.1.
CCDSiCCDS25787.1.
RefSeqiNP_612178.2. NM_138305.3.
XP_006514995.1. XM_006514932.1.
XP_006514996.1. XM_006514933.1.
XP_006514997.1. XM_006514934.2.
XP_006514998.1. XM_006514935.2.
UniGeneiMm.489807.

Genome annotation databases

EnsembliENSMUST00000020984; ENSMUSP00000020984; ENSMUSG00000020654.
ENSMUST00000127756; ENSMUSP00000115406; ENSMUSG00000020654.
GeneIDi104111.
UCSCiuc007mxm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458089 mRNA. Translation: AAL59384.1.
CT572999 Genomic DNA. Translation: CAX15321.1.
CH466623 Genomic DNA. Translation: EDL01374.1.
CCDSiCCDS25787.1.
RefSeqiNP_612178.2. NM_138305.3.
XP_006514995.1. XM_006514932.1.
XP_006514996.1. XM_006514933.1.
XP_006514997.1. XM_006514934.2.
XP_006514998.1. XM_006514935.2.
UniGeneiMm.489807.

3D structure databases

ProteinModelPortaliQ8VHH7.
SMRiQ8VHH7. Positions 307-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222368. 2 interactions.
IntActiQ8VHH7. 1 interaction.
MINTiMINT-7290275.
STRINGi10090.ENSMUSP00000020984.

PTM databases

iPTMnetiQ8VHH7.
PhosphoSiteiQ8VHH7.

Proteomic databases

MaxQBiQ8VHH7.
PaxDbiQ8VHH7.
PRIDEiQ8VHH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020984; ENSMUSP00000020984; ENSMUSG00000020654.
ENSMUST00000127756; ENSMUSP00000115406; ENSMUSG00000020654.
GeneIDi104111.
UCSCiuc007mxm.2. mouse.

Organism-specific databases

CTDi109.
MGIiMGI:99675. Adcy3.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ8VHH7.
OMAiNIYAWRP.
OrthoDBiEOG7B8S30.
PhylomeDBiQ8VHH7.

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-MMU-5610787. Hedgehog 'off' state.

Miscellaneous databases

ChiTaRSiAdcy3. mouse.
NextBioi356544.
PROiQ8VHH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHH7.
CleanExiMM_ADCY3.
ExpressionAtlasiQ8VHH7. baseline and differential.
GenevisibleiQ8VHH7. MM.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of mouse Adcy3."
    Pasternak S., Neumann P.E.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM kinase II in neurons: a mechanism for attenuation of olfactory signals."
    Wei J., Zhao A.Z., Chan G.C., Baker L.P., Impey S., Beavo J.A., Storm D.R.
    Neuron 21:495-504(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-1077, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
  5. "Disruption of the type III adenylyl cyclase gene leads to peripheral and behavioral anosmia in transgenic mice."
    Wong S.T., Trinh K., Hacker B., Chan G.C., Lowe G., Gaggar A., Xia Z., Gold G.H., Storm D.R.
    Neuron 27:487-497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function."
    Livera G., Xie F., Garcia M.A., Jaiswal B., Chen J., Law E., Storm D.R., Conti M.
    Mol. Endocrinol. 19:1277-1290(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "A gain-of-function mutation in adenylate cyclase 3 protects mice from diet-induced obesity."
    Pitman J.L., Wheeler M.C., Lloyd D.J., Walker J.R., Glynne R.J., Gekakis N.
    PLoS ONE 9:E110226-E110226(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF MET-279, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  9. "SUMOylation regulates ciliary localization of olfactory signaling proteins."
    McIntyre J.C., Joiner A.M., Zhang L., Iniguez-Lluhi J., Martens J.R.
    J. Cell Sci. 128:1934-1945(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiADCY3_MOUSE
AccessioniPrimary (citable) accession number: Q8VHH7
Secondary accession number(s): B8JK57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: July 27, 2011
Last modified: January 20, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.