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Q99P84

- PLCE1_RAT

UniProt

Q99P84 - PLCE1_RAT

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1

Gene

Plce1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation.3 Publications

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.1 Publication

    Cofactori

    Calcium.1 Publication

    Enzyme regulationi

    Activated by the heterotrimeric G-protein subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by G(i)-coupled GPCRs.5 Publications

    Kineticsi

    1. KM=6.0 µM for PtdIns(4,5)P21 Publication

    Vmax=10 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1388 – 13881PROSITE-ProRule annotation
    Active sitei1433 – 14331PROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. enzyme binding Source: UniProtKB
    3. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
    4. phosphatidylinositol phospholipase C activity Source: UniProtKB
    5. phospholipase C activity Source: UniProtKB
    6. Ras GTPase binding Source: RGD
    7. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of MAPK activity Source: UniProtKB
    2. G-protein coupled receptor signaling pathway Source: RGD
    3. lipid catabolic process Source: UniProtKB-KW
    4. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    5. Ras protein signal transduction Source: RGD
    6. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    7. regulation of protein kinase activity Source: UniProtKB
    8. regulation of Ras protein signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor, Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BRENDAi3.1.4.11. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-epsilon-1
    Phospholipase C-epsilon-1
    Short name:
    PLC-epsilon-1
    Gene namesi
    Name:Plce1
    Synonyms:Plce
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69424. Plce1.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cell membrane By similarity. Golgi apparatus membrane By similarity
    Note: Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Associates with Golgi membranes By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. cytosol Source: UniProtKB
    3. Golgi membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2150 – 21501K → A: Inhibits binding to HRAS by 59% and phospholipase stimulation by HRAS by 51%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 86%; when associated with A-2152. 1 Publication
    Mutagenesisi2150 – 21501K → E: Inhibits binding to HRAS by 99% and phospholipase stimulation by HRAS by 94%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 94%; when associated with E-2152. 1 Publication
    Mutagenesisi2152 – 21521K → A: Inhibits binding to HRAS by 19% and phospholipase stimulation by HRAS by 30%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 86%; when associated with A-2150. 1 Publication
    Mutagenesisi2152 – 21521K → E: Inhibits binding to HRAS by 67% and phospholipase stimulation by HRAS by 47%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 94%; when associated with E-2150. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 228122811-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1PRO_0000256240Add
    BLAST

    Proteomic databases

    PaxDbiQ99P84.
    PRIDEiQ99P84.

    PTM databases

    PhosphoSiteiQ99P84.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Detected in glomerular podocytes (at protein level).2 Publications

    Gene expression databases

    GenevestigatoriQ99P84.

    Interactioni

    Subunit structurei

    Interacts with GTP-bound HRAS, RAP1A and probably with RAP2A, RAP2B and RRAS. Interacts with RHOA. Interacts with IQGAP1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ99P84. 1 interaction.
    STRINGi10116.ENSRNOP00000019771.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99P84.
    SMRiQ99P84. Positions 1985-2093, 2110-2225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini528 – 781254Ras-GEFPROSITE-ProRule annotationAdd
    BLAST
    Domaini1373 – 1521149PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini1709 – 1825117PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini1835 – 1935101C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1991 – 2093103Ras-associating 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2114 – 2217104Ras-associating 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1667 – 174377Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gammaAdd
    BLAST

    Domaini

    The Ras-associating domain 1 is degenerated and may not bind HRAS By similarity. The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A and probably RAP2A and RAP2B and recruitment of HRAS to the cell membrane.By similarity
    The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway By similarity.By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
    Contains 2 Ras-associating domains.PROSITE-ProRule annotation
    Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG149692.
    HOGENOMiHOG000090225.
    HOVERGENiHBG059220.
    InParanoidiQ99P84.
    KOiK05860.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.840.10. 2 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 3 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR001192. PI-PLC_fam.
    IPR028398. PLC-epsilon1.
    IPR017946. PLC-like_Pdiesterase_TIM-brl.
    IPR015359. PLipase_C_EF-hand-like.
    IPR000909. PLipase_C_PInositol-sp_X_dom.
    IPR001711. PLipase_C_Pinositol-sp_Y.
    IPR000159. Ras-assoc.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF6. PTHR10336:SF6. 1 hit.
    PfamiPF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    PF00788. RA. 1 hit.
    PF00617. RasGEF. 1 hit.
    [Graphical view]
    PRINTSiPR00390. PHPHLIPASEC.
    SMARTiSM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    SM00314. RA. 1 hit.
    SM00147. RasGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48366. SSF48366. 2 hits.
    SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 3 hits.
    SSF54236. SSF54236. 2 hits.
    PROSITEiPS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99P84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSEEMAASF LIPVPQRKVA SAQSVAEERG EKVSEAGIPK TRAGRQGGLT     50
    PRTISQRNEP EEESPRTDFS QVFSIARGEL DSDENHNERC WEENVPGSTK 100
    NHAVNCNSLL QSHQHALPPS QLCEVCDSVT EEHLCLQPGI PSPLERKVFP 150
    GIELEMEDSP MDVSPLGNQP GIMESSGPHS DRNMAVFHFH YAGDRTMPGA 200
    FHTLSEKFIL DDCANCVTLP GGQQNKNYMA YTCKLVELTR TCGSKNGQLK 250
    CDHCTSLRDE YLCFESSCRK AEALSSGGGF CEDGFTHGPS AKTFLNPLEE 300
    FSDNCEDVDD IFKGKKERST LLVRRFCKND REVKKSVYTG TRAIVRTLPS 350
    GHIGLAAWSY VDQKKAGLMW PCGNGMRPLS TVDVRQSGRQ RLSEAQWCLI 400
    YSAVRREETE DTVGSLLHCS TQLPTPDTAH GRIGDGPCLK QCVRDSECEY 450
    RATLQRTSIA QYITGSLLEA TTSLGARSSL LSSFGGSTGR IMLKERQPGT 500
    SMANSSPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE QNIYRRVLPM 550
    DYLCFLTRDL SSPECQRSLP RLKACISESI LMSQSGEHNA LEDLVMRFNE 600
    VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS 650
    RKVLKMWQFM DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV 700
    PFCGVFLKEL CEVLDGASGL LKLCPRYSSQ EEALEFVADY SGQDNFLQRV 750
    GQNGLKNPEK ELTVNSIFQI IRSCSRSLET EDEESASEGS GSRKNSLKDK 800
    TRWQFIIGDL LDSDNDIFEK SKECDPHGSE ESQKAFDHGT ELIPWYVLSI 850
    QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG 900
    ARLKLGVLSN VAEPGKFPSL GNAGVSGLVE GILDLFSVKA VYMGHPGIDI 950
    HTVCVQNKLS SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAKMLFSGLL 1000
    ELTTAVRKIR KFPDQRQQWL RKQYVSFYQE DGRYEGPTLA HAVELFGGRR 1050
    WSTRNPSPGM SAKNAEKPNM QRNNTLGIST TKKKKKMLMR GESGEVTDDE 1100
    MATRKAKMYR ECRSRSGSDP QEANEQEDSE ANVITNPPNP LHSRRAYSLT 1150
    TAGSPNLATG MSSPISAWSS SSWHGRIKGG MKGFQSFMVS DSNMSFIEFV 1200
    ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESTPLYTNLT IEENTNDLQP 1250
    DLDLLTRNVS DLGLFMKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL 1300
    GIFGVGILQL NDFLVNCQGE HCTYDEILSI IQKFEPNISM CHQGLLSFEG 1350
    FARFLMDKDN FASKNDESRE NKKDLQLPLS YYYIESSHNT YLTGHQLKGE 1400
    SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK IPFKEVVEAI 1450
    DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF 1500
    SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQTQAFTG 1550
    GNANPPPASN EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY 1600
    NEEVPKRIKK ADNSSGNKGK VYDMELGEEF YLPQNKKESR QIAPELSDLV 1650
    IYCQAVKFPG LSTLNSSGSG RGKERKSRKS IFGNNPGRMS PGETASFNRT 1700
    SGKSSCEGIR QIWEEPPLSP NTSLSAIIRT PKCYHISSLN ENAAKRLCRR 1750
    YSQKLIQHTA CQLLRTYPAA TRIDSSNPNP LMFWLHGIQL VALNYQTDDL 1800
    PLHLNAAMFE ANGGCGYVLK PPVLWDKSCP MYQKFSPLER DLDAMDPATY 1850
    SLTIISGQNV CPSNSTGSPC IEVDVLGMPL DSCHFRTKPI HRNTLNPMWN 1900
    EQFLFRVHFE DLVFLRFAVV ENNSSAITAQ RIIPLKALKR GYRHLQLRNL 1950
    HNEILEISSL FINSRRMEDN PSGSTRPASL MFNTEERKCS QTHKVTVHGV 2000
    PGPEPFAVFT INEGTKAKQL LQQILAVDQD TKLTAADYFL MEEKHFISKE 2050
    KNECRKQPFQ RAVGPEEDIV QILNSWFPEE GYVGRIVLKP QQETLEEKNI 2100
    VHDDREVILS SEEESFFVQV HDVSPEQPRT VIKAPRVSTA QDVIQQTLCK 2150
    AKYSYSILNN PNPCDYVLLE EVMKDAPNKK SSTPKSSQRI LLDQECVFQA 2200
    QSKWKGAGKF ILKLKEQVQA SREDKRRGIS FASELKKLTK STKQTRGLTS 2250
    PPQLVASESV QSKEEKPMGA LASGDTAGYQ S 2281
    Length:2,281
    Mass (Da):255,393
    Last modified:June 1, 2001 - v1
    Checksum:i7409A739B61F69EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323615 mRNA. Translation: AAK06775.1.
    RefSeqiNP_446210.1. NM_053758.2.
    UniGeneiRn.64650.

    Genome annotation databases

    GeneIDi114633.
    KEGGirno:114633.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323615 mRNA. Translation: AAK06775.1 .
    RefSeqi NP_446210.1. NM_053758.2.
    UniGenei Rn.64650.

    3D structure databases

    ProteinModelPortali Q99P84.
    SMRi Q99P84. Positions 1985-2093, 2110-2225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99P84. 1 interaction.
    STRINGi 10116.ENSRNOP00000019771.

    PTM databases

    PhosphoSitei Q99P84.

    Proteomic databases

    PaxDbi Q99P84.
    PRIDEi Q99P84.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 114633.
    KEGGi rno:114633.

    Organism-specific databases

    CTDi 51196.
    RGDi 69424. Plce1.

    Phylogenomic databases

    eggNOGi NOG149692.
    HOGENOMi HOG000090225.
    HOVERGENi HBG059220.
    InParanoidi Q99P84.
    KOi K05860.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 5301.

    Miscellaneous databases

    NextBioi 618799.
    PROi Q99P84.

    Gene expression databases

    Genevestigatori Q99P84.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.840.10. 2 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 3 hits.
    InterProi IPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR001192. PI-PLC_fam.
    IPR028398. PLC-epsilon1.
    IPR017946. PLC-like_Pdiesterase_TIM-brl.
    IPR015359. PLipase_C_EF-hand-like.
    IPR000909. PLipase_C_PInositol-sp_X_dom.
    IPR001711. PLipase_C_Pinositol-sp_Y.
    IPR000159. Ras-assoc.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF6. PTHR10336:SF6. 1 hit.
    Pfami PF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    PF00788. RA. 1 hit.
    PF00617. RasGEF. 1 hit.
    [Graphical view ]
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    SM00314. RA. 1 hit.
    SM00147. RasGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48366. SSF48366. 2 hits.
    SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 3 hits.
    SSF54236. SSF54236. 2 hits.
    PROSITEi PS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phospholipase C(epsilon): a novel Ras effector."
      Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.
      EMBO J. 20:743-754(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, INTERACTION WITH HRAS AND RAP1A, MUTAGENESIS OF LYS-2150 AND LYS-2152.
      Tissue: Heart.
    2. "Activation of phospholipase C-epsilon by heterotrimeric G protein betagamma-subunits."
      Wing M.R., Houston D., Kelley G.G., Der C.J., Siderovski D.P., Harden T.K.
      J. Biol. Chem. 276:48257-48261(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    3. "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation."
      Murphy G.A., Graham S.M., Morita S., Reks S.E., Rogers-Graham K., Vojtek A., Kelley G.G., Der C.J.
      J. Biol. Chem. 277:9966-9975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    4. "Direct activation of phospholipase C-epsilon by Rho."
      Wing M.R., Snyder J.T., Sondek J., Harden T.K.
      J. Biol. Chem. 278:41253-41258(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH RHOA.
    5. Cited for: FUNCTION.
    6. "RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism."
      Seifert J.P., Wing M.R., Snyder J.T., Gershburg S., Sondek J., Harden T.K.
      J. Biol. Chem. 279:47992-47997(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "G-protein-coupled receptor agonists activate endogenous phospholipase Cepsilon and phospholipase Cbeta3 in a temporally distinct manner."
      Kelley G.G., Kaproth-Joslin K.A., Reks S.E., Smrcka A.V., Wojcikiewicz R.J.H.
      J. Biol. Chem. 281:2639-2648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH IQGAP1.

    Entry informationi

    Entry nameiPLCE1_RAT
    AccessioniPrimary (citable) accession number: Q99P84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 101 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3