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Protein

cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

Gene

Pde10a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.1 Publication

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.1 Publication
Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.1 Publication

Cofactori

a divalent metal cationNote: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.

Enzyme regulationi

Inhibited by dipyridamole and moderately by IBMX, zaprinast and rolipram.1 Publication

Kineticsi

  1. KM=0.26 µM for cAMP1 Publication
  2. KM=9.3 µM for cGMP1 Publication

    Pathway: 3',5'-cyclic AMP degradation

    This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
    Proteins known to be involved in this subpathway in this organism are:
    1. High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (Pde4b), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (Pde4a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Pde4c)
    This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

    Pathway: 3',5'-cyclic GMP degradation

    This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.
    Proteins known to be involved in this subpathway in this organism are:
    1. High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (Pde9a), cGMP-specific 3',5'-cyclic phosphodiesterase (Pde5a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a)
    This subpathway is part of the pathway 3',5'-cyclic GMP degradation, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei374 – 3741Allosteric effectorBy similarity
    Binding sitei393 – 3931Allosteric effectorBy similarity
    Active sitei525 – 5251Proton donorBy similarity
    Binding sitei525 – 5251SubstrateBy similarity
    Metal bindingi529 – 5291Divalent metal cation 1
    Metal bindingi563 – 5631Divalent metal cation 1
    Metal bindingi564 – 5641Divalent metal cation 1
    Metal bindingi564 – 5641Divalent metal cation 2
    Metal bindingi674 – 6741Divalent metal cation 1
    Binding sitei726 – 7261SubstrateBy similarity

    GO - Molecular functioni

    • 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
    • cAMP binding Source: RGD
    • cGMP binding Source: RGD
    • cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    • cyclic-nucleotide phosphodiesterase activity Source: RGD
    • drug binding Source: RGD
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • cAMP catabolic process Source: RGD
    • cGMP catabolic process Source: RGD
    • signal transduction Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cAMP-binding, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_287445. G alpha (s) signalling events.
    REACT_349609. cGMP effects.
    UniPathwayiUPA00762; UER00747.
    UPA00763; UER00748.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC:3.1.4.17, EC:3.1.4.35)
    Gene namesi
    Name:Pde10a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi68434. Pde10a.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • membrane Source: RGD
    • neuronal cell body Source: RGD
    • perikaryon Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 794794cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10APRO_0000355559Add
    BLAST

    Proteomic databases

    PaxDbiQ9QYJ6.
    PRIDEiQ9QYJ6.

    Miscellaneous databases

    PMAP-CutDBQ9QYJ6.

    Expressioni

    Tissue specificityi

    Detected in striatum and testis (at protein level). Detected in whole brain, hippocampus, olfactory bulb, striatum neurons and testis.2 Publications

    Inductioni

    Up-regulated in brain after seizures. Up-regulated in the hippocampus one hour after induction of long-term potentiation.1 Publication

    Gene expression databases

    ExpressionAtlasiQ9QYJ6. baseline.
    GenevisibleiQ9QYJ6. RN.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000060834.

    Structurei

    Secondary structure

    1
    794
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi466 – 4716Combined sources
    Helixi483 – 4853Combined sources
    Helixi486 – 49813Combined sources
    Helixi500 – 5023Combined sources
    Helixi505 – 51713Combined sources
    Beta strandi523 – 5264Combined sources
    Helixi527 – 54216Combined sources
    Turni545 – 5473Combined sources
    Helixi550 – 56213Combined sources
    Turni563 – 5664Combined sources
    Helixi572 – 5787Combined sources
    Helixi581 – 5855Combined sources
    Beta strandi587 – 5893Combined sources
    Helixi590 – 60314Combined sources
    Turni610 – 6134Combined sources
    Helixi616 – 63217Combined sources
    Helixi635 – 65016Combined sources
    Helixi659 – 67416Combined sources
    Helixi676 – 6794Combined sources
    Helixi682 – 70524Combined sources
    Helixi712 – 7143Combined sources
    Helixi716 – 7216Combined sources
    Helixi722 – 73211Combined sources
    Helixi734 – 74411Combined sources
    Helixi746 – 7483Combined sources
    Helixi749 – 76618Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O8HX-ray1.80A452-794[»]
    2OVVX-ray2.00A452-794[»]
    2OVYX-ray1.80A452-794[»]
    3HQWX-ray1.70A452-794[»]
    3HQYX-ray2.00A452-794[»]
    3HQZX-ray1.70A452-794[»]
    3HR1X-ray1.53A452-794[»]
    3LXGX-ray2.30A463-770[»]
    3QPNX-ray2.00A452-794[»]
    3QPOX-ray1.80A452-794[»]
    3QPPX-ray1.80A452-794[»]
    ProteinModelPortaliQ9QYJ6.
    SMRiQ9QYJ6. Positions 256-432, 464-770.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QYJ6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni296 – 2972Allosteric effector bindingBy similarity
    Regioni340 – 3412Allosteric effector bindingBy similarity

    Domaini

    The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity.
    Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    GeneTreeiENSGT00760000119066.
    HOGENOMiHOG000007068.
    HOVERGENiHBG082113.
    InParanoidiQ9QYJ6.
    KOiK18438.
    TreeFamiTF316499.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    3.30.450.40. 2 hits.
    InterProiIPR003018. GAF.
    IPR029016. GAF_dom_like.
    IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view]
    PfamiPF01590. GAF. 2 hits.
    PF00233. PDEase_I. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00065. GAF. 2 hits.
    SM00471. HDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55781. SSF55781. 2 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9QYJ6-1) [UniParc]FASTAAdd to basket

    Also known as: PDE10A2

    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
    MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA
    60 70 80 90 100
    ETVEKWLKRK NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG
    110 120 130 140 150
    DNHLLLYELS SIIRIATKAD GFALYFLGEC NNSLCVFTPP GMKEGQPRLI
    160 170 180 190 200
    PAGPITQGTT ISAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC
    210 220 230 240 250
    LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC
    260 270 280 290 300
    RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF
    310 320 330 340 350
    QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV
    360 370 380 390 400
    LNIPDAYADP RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG
    410 420 430 440 450
    SAFSKTDENN FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI
    460 470 480 490 500
    CTSEEWQGLM HFNLPARICR DIELFHFDIG PFENMWPGIF VYMIHRSCGT
    510 520 530 540 550
    SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNNGLFTD
    560 570 580 590 600
    LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV
    610 620 630 640 650
    SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ
    660 670 680 690 700
    TGSLNLHNQS HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG
    710 720 730 740 750
    DEMKKLGIQP IPMMDRDKRD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP
    760 770 780 790
    LLKACRDNLN QWEKVIRGEE TAMWISGPAT SKSTSEKPTR KVDD
    Length:794
    Mass (Da):90,161
    Last modified:May 1, 2000 - v1
    Checksum:iA36C4678B385846E
    GO
    Isoform 2 (identifier: Q9QYJ6-2) [UniParc]FASTAAdd to basket

    Also known as: PDE10A3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MEDGPSNNASCFRRLTECFLSPS → MSNDSPEGAVGSCNATG

    Show »
    Length:788
    Mass (Da):89,196
    Checksum:i44F421DF1CC8FBA0
    GO
    Isoform 3 (identifier: Q9QYJ6-3) [UniParc]FASTAAdd to basket

    Also known as: PDE10A11

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MEDGPSNNASCFRRLTECFLSPS → MSKKRKALEG...GAVGSCNATG

    Show »
    Length:852
    Mass (Da):95,777
    Checksum:i31F6E5D4DDB8F60B
    GO
    Isoform 4 (identifier: Q9QYJ6-4) [UniParc]FASTAAdd to basket

    Also known as: PDE10A12

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MEDGPSNNASCFRRLTECFLSPS → MSKKRKALEG...SDSRLALCMG

    Show »
    Length:883
    Mass (Da):99,036
    Checksum:i86527DFF337E4B4F
    GO
    Isoform 5 (identifier: Q9QYJ6-5) [UniParc]FASTAAdd to basket

    Also known as: PDE10A13

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: Missing.

    Show »
    Length:714
    Mass (Da):81,028
    Checksum:i5AFBCD366955F8F6
    GO
    Isoform 6 (identifier: Q9QYJ6-6) [UniParc]FASTAAdd to basket

    Also known as: PDE10A14

    The sequence of this isoform differs from the canonical sequence as follows:
         1-141: Missing.

    Show »
    Length:653
    Mass (Da):74,275
    Checksum:iC712183FC1CFA76F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 141141Missing in isoform 6. 1 PublicationVSP_035919Add
    BLAST
    Alternative sequencei1 – 8080Missing in isoform 5. 1 PublicationVSP_035920Add
    BLAST
    Alternative sequencei1 – 2323MEDGP…FLSPS → MSNDSPEGAVGSCNATG in isoform 2. 2 PublicationsVSP_035921Add
    BLAST
    Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT G in isoform 3. 1 PublicationVSP_035922Add
    BLAST
    Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT GSTGSTGELGKEFHTPPRRK SASDSRLALCMG in isoform 4. 1 PublicationVSP_035923Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB027155 mRNA. Translation: BAA88996.1.
    AB027156 mRNA. Translation: BAA88997.1.
    AY462091 mRNA. Translation: AAS21243.1.
    AY462092 mRNA. Translation: AAS21244.1.
    AY462093 mRNA. Translation: AAS21245.1.
    AY462094 mRNA. Translation: AAS21246.1.
    AY462095 mRNA. Translation: AAS21247.1.
    CH474059 Genomic DNA. Translation: EDL83106.1.
    RefSeqiNP_071572.1. NM_022236.1. [Q9QYJ6-1]
    UniGeneiRn.44869.

    Genome annotation databases

    EnsembliENSRNOT00000043474; ENSRNOP00000042134; ENSRNOG00000011310. [Q9QYJ6-1]
    GeneIDi63885.
    KEGGirno:63885.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB027155 mRNA. Translation: BAA88996.1.
    AB027156 mRNA. Translation: BAA88997.1.
    AY462091 mRNA. Translation: AAS21243.1.
    AY462092 mRNA. Translation: AAS21244.1.
    AY462093 mRNA. Translation: AAS21245.1.
    AY462094 mRNA. Translation: AAS21246.1.
    AY462095 mRNA. Translation: AAS21247.1.
    CH474059 Genomic DNA. Translation: EDL83106.1.
    RefSeqiNP_071572.1. NM_022236.1. [Q9QYJ6-1]
    UniGeneiRn.44869.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O8HX-ray1.80A452-794[»]
    2OVVX-ray2.00A452-794[»]
    2OVYX-ray1.80A452-794[»]
    3HQWX-ray1.70A452-794[»]
    3HQYX-ray2.00A452-794[»]
    3HQZX-ray1.70A452-794[»]
    3HR1X-ray1.53A452-794[»]
    3LXGX-ray2.30A463-770[»]
    3QPNX-ray2.00A452-794[»]
    3QPOX-ray1.80A452-794[»]
    3QPPX-ray1.80A452-794[»]
    ProteinModelPortaliQ9QYJ6.
    SMRiQ9QYJ6. Positions 256-432, 464-770.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000060834.

    Chemistry

    BindingDBiQ9QYJ6.
    ChEMBLiCHEMBL6140.

    Proteomic databases

    PaxDbiQ9QYJ6.
    PRIDEiQ9QYJ6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000043474; ENSRNOP00000042134; ENSRNOG00000011310. [Q9QYJ6-1]
    GeneIDi63885.
    KEGGirno:63885.

    Organism-specific databases

    CTDi10846.
    RGDi68434. Pde10a.

    Phylogenomic databases

    eggNOGiNOG270709.
    GeneTreeiENSGT00760000119066.
    HOGENOMiHOG000007068.
    HOVERGENiHBG082113.
    InParanoidiQ9QYJ6.
    KOiK18438.
    TreeFamiTF316499.

    Enzyme and pathway databases

    UniPathwayiUPA00762; UER00747.
    UPA00763; UER00748.
    ReactomeiREACT_287445. G alpha (s) signalling events.
    REACT_349609. cGMP effects.

    Miscellaneous databases

    EvolutionaryTraceiQ9QYJ6.
    NextBioi612518.
    PMAP-CutDBQ9QYJ6.
    PROiQ9QYJ6.

    Gene expression databases

    ExpressionAtlasiQ9QYJ6. baseline.
    GenevisibleiQ9QYJ6. RN.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    3.30.450.40. 2 hits.
    InterProiIPR003018. GAF.
    IPR029016. GAF_dom_like.
    IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view]
    PfamiPF01590. GAF. 2 hits.
    PF00233. PDEase_I. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00065. GAF. 2 hits.
    SM00471. HDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55781. SSF55781. 2 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Striatum- and testis-specific phosphodiesterase PDE10A isolation and characterization of a rat PDE10A."
      Fujishige K., Kotera J., Omori K.
      Eur. J. Biochem. 266:1118-1127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "Differential amplification of intron-containing transcripts reveals long term potentiation-associated up-regulation of specific Pde10A phosphodiesterase splice variants."
      O'Connor V., Genin A., Davis S., Karishma K.K., Doyere V., De Zeeuw C.I., Sanger G., Hunt S.P., Richter-Levin G., Mallet J., Laroche S., Bliss T.V.P., French P.J.
      J. Biol. Chem. 279:15841-15849(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, INDUCTION.
      Strain: Wistar.
    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. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 452-794 IN COMPLEXES WITH ZINC; MAGNESIUM AND A SYNTHETIC INHIBITOR.

    Entry informationi

    Entry nameiPDE10_RAT
    AccessioniPrimary (citable) accession number: Q9QYJ6
    Secondary accession number(s): Q6S9E6
    , Q6S9E7, Q6S9E8, Q6S9E9, Q9QYJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: May 1, 2000
    Last modified: June 24, 2015
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3

    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 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.