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Q9V3B7

- PGSC1_DROME

UniProt

Q9V3B7 - PGSC1_DROME

Protein

Peptidoglycan-recognition protein SC1a/b

Gene

PGRP-SC1a

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.

    Catalytic activityi

    Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.1 Publication

    Cofactori

    Zinc.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi52 – 521ZincBy similarity
    Metal bindingi86 – 861ZincBy similarity
    Metal bindingi160 – 1601ZincBy similarity
    Metal bindingi168 – 1681ZincBy similarity

    GO - Molecular functioni

    1. N-acetylmuramoyl-L-alanine amidase activity Source: FlyBase
    2. peptidoglycan binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. immune response Source: FlyBase
    2. innate immune response Source: UniProtKB
    3. negative regulation of innate immune response Source: FlyBase
    4. peptidoglycan catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidoglycan-recognition protein SC1a/b (EC:3.5.1.28)
    Gene namesi
    Name:PGRP-SC1a
    ORF Names:CG14746
    AND
    Name:PGRP-SC1b
    ORF Names:CG8577
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0043576. PGRP-SC1a.
    FBgn0033327. PGRP-SC1b.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681C → A: Abolishes enzyme activity but retains PGN-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 185164Peptidoglycan-recognition protein SC1a/bPRO_0000023910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 64By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9V3B7.
    PRIDEiQ9V3B7.

    Expressioni

    Tissue specificityi

    Constitutively expressed at high level in gut, in addition to the induced expression in fat body.1 Publication

    Inductioni

    Up-regulated by PGN from B.subtilis.1 Publication

    Gene expression databases

    BgeeiQ9V3B7.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CG9184Q9W0H11EBI-109541,EBI-143367

    Protein-protein interaction databases

    BioGridi61708. 1 interaction.
    61710. 1 interaction.
    IntActiQ9V3B7. 1 interaction.
    MINTiMINT-1610118.
    STRINGi7227.FBpp0087786.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9V3B7.
    SMRiQ9V3B7. Positions 24-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5479.
    GeneTreeiENSGT00390000016833.
    InParanoidiQ9V3B7.
    KOiK01446.
    OMAiTLEPNMI.
    OrthoDBiEOG757CZ5.
    PhylomeDBiQ9V3B7.

    Family and domain databases

    Gene3Di3.40.80.10. 1 hit.
    InterProiIPR002502. Amidase_domain.
    IPR017331. Peptidoglycan_recognition.
    IPR015510. PGRP.
    IPR006619. PGRP_domain_met/bac.
    [Graphical view]
    PANTHERiPTHR11022. PTHR11022. 1 hit.
    PfamiPF01510. Amidase_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037945. PGRPs. 1 hit.
    SMARTiSM00644. Ami_2. 1 hit.
    SM00701. PGRP. 1 hit.
    [Graphical view]
    SUPFAMiSSF55846. SSF55846. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9V3B7-1 [UniParc]FASTAAdd to Basket

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    MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVG LGNYLSYAII    50
    HHTAGSYCET RAQCNAVLQS VQNYHMDSLG WPDIGYNFLI GGDGNVYEGR 100
    GWNNMGAHAA EWNPYSIGIS FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ 150
    LSSGYILYGH RQVSATECPG THIWNEIRGW SHWSG 185
    Length:185
    Mass (Da):20,395
    Last modified:May 1, 2000 - v1
    Checksum:iF23F8D80A33541AC
    GO

    Sequence cautioni

    The sequence AAL28193.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781R → P in AAL28193. (PubMed:12537569)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → T in PGRP-SC1a; strain: KY038 and in PGRP-SC1b; strain: KY024 and KY038.
    Natural varianti13 – 131V → I in PGRP-SC1b; strain: KY024.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207542 mRNA. Translation: AAG23736.1.
    AJ556588 Genomic DNA. Translation: CAD89153.1.
    AJ556589 Genomic DNA. Translation: CAD89154.1.
    AJ556590 Genomic DNA. Translation: CAD89155.1.
    AJ556591 Genomic DNA. Translation: CAD89156.1.
    AJ556592 Genomic DNA. Translation: CAD89157.1.
    AJ556593 Genomic DNA. Translation: CAD89158.1.
    AJ556594 Genomic DNA. Translation: CAD89159.1.
    AJ556595 Genomic DNA. Translation: CAD89160.1.
    AJ556596 Genomic DNA. Translation: CAD89161.1.
    AJ556597 Genomic DNA. Translation: CAD89162.1.
    AJ556598 Genomic DNA. Translation: CAD89163.1.
    AJ556599 Genomic DNA. Translation: CAD89164.1.
    AJ556600 Genomic DNA. Translation: CAD89165.1.
    AJ556601 Genomic DNA. Translation: CAD89166.1.
    AJ556602 Genomic DNA. Translation: CAD89167.1.
    AJ556603 Genomic DNA. Translation: CAD89168.1.
    AJ556604 Genomic DNA. Translation: CAD89169.1.
    AJ556605 Genomic DNA. Translation: CAD89170.1.
    AJ556606 Genomic DNA. Translation: CAD89171.1.
    AJ556607 Genomic DNA. Translation: CAD89172.1.
    AJ556608 Genomic DNA. Translation: CAD89173.1.
    AJ556609 Genomic DNA. Translation: CAD89174.1.
    AE013599 Genomic DNA. Translation: AAF59052.1.
    AE013599 Genomic DNA. Translation: AAF59054.1.
    AY060645 mRNA. Translation: AAL28193.2. Different initiation.
    BT044352 mRNA. Translation: ACH92417.2.
    RefSeqiNP_610407.1. NM_136563.1.
    NP_610409.1. NM_136565.1.
    UniGeneiDm.3372.
    Dm.38443.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088707; FBpp0087786; FBgn0043576.
    FBtr0088708; FBpp0087787; FBgn0033327.
    GeneIDi35859.
    35861.
    KEGGidme:Dmel_CG14746.
    dme:Dmel_CG8577.
    UCSCiCG14746-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207542 mRNA. Translation: AAG23736.1 .
    AJ556588 Genomic DNA. Translation: CAD89153.1 .
    AJ556589 Genomic DNA. Translation: CAD89154.1 .
    AJ556590 Genomic DNA. Translation: CAD89155.1 .
    AJ556591 Genomic DNA. Translation: CAD89156.1 .
    AJ556592 Genomic DNA. Translation: CAD89157.1 .
    AJ556593 Genomic DNA. Translation: CAD89158.1 .
    AJ556594 Genomic DNA. Translation: CAD89159.1 .
    AJ556595 Genomic DNA. Translation: CAD89160.1 .
    AJ556596 Genomic DNA. Translation: CAD89161.1 .
    AJ556597 Genomic DNA. Translation: CAD89162.1 .
    AJ556598 Genomic DNA. Translation: CAD89163.1 .
    AJ556599 Genomic DNA. Translation: CAD89164.1 .
    AJ556600 Genomic DNA. Translation: CAD89165.1 .
    AJ556601 Genomic DNA. Translation: CAD89166.1 .
    AJ556602 Genomic DNA. Translation: CAD89167.1 .
    AJ556603 Genomic DNA. Translation: CAD89168.1 .
    AJ556604 Genomic DNA. Translation: CAD89169.1 .
    AJ556605 Genomic DNA. Translation: CAD89170.1 .
    AJ556606 Genomic DNA. Translation: CAD89171.1 .
    AJ556607 Genomic DNA. Translation: CAD89172.1 .
    AJ556608 Genomic DNA. Translation: CAD89173.1 .
    AJ556609 Genomic DNA. Translation: CAD89174.1 .
    AE013599 Genomic DNA. Translation: AAF59052.1 .
    AE013599 Genomic DNA. Translation: AAF59054.1 .
    AY060645 mRNA. Translation: AAL28193.2 . Different initiation.
    BT044352 mRNA. Translation: ACH92417.2 .
    RefSeqi NP_610407.1. NM_136563.1.
    NP_610409.1. NM_136565.1.
    UniGenei Dm.3372.
    Dm.38443.

    3D structure databases

    ProteinModelPortali Q9V3B7.
    SMRi Q9V3B7. Positions 24-183.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61708. 1 interaction.
    61710. 1 interaction.
    IntActi Q9V3B7. 1 interaction.
    MINTi MINT-1610118.
    STRINGi 7227.FBpp0087786.

    Proteomic databases

    PaxDbi Q9V3B7.
    PRIDEi Q9V3B7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088707 ; FBpp0087786 ; FBgn0043576 .
    FBtr0088708 ; FBpp0087787 ; FBgn0033327 .
    GeneIDi 35859.
    35861.
    KEGGi dme:Dmel_CG14746.
    dme:Dmel_CG8577.
    UCSCi CG14746-RA. d. melanogaster.

    Organism-specific databases

    CTDi 35859.
    35861.
    FlyBasei FBgn0043576. PGRP-SC1a.
    FBgn0033327. PGRP-SC1b.

    Phylogenomic databases

    eggNOGi COG5479.
    GeneTreei ENSGT00390000016833.
    InParanoidi Q9V3B7.
    KOi K01446.
    OMAi TLEPNMI.
    OrthoDBi EOG757CZ5.
    PhylomeDBi Q9V3B7.

    Miscellaneous databases

    NextBioi 795548.

    Gene expression databases

    Bgeei Q9V3B7.

    Family and domain databases

    Gene3Di 3.40.80.10. 1 hit.
    InterProi IPR002502. Amidase_domain.
    IPR017331. Peptidoglycan_recognition.
    IPR015510. PGRP.
    IPR006619. PGRP_domain_met/bac.
    [Graphical view ]
    PANTHERi PTHR11022. PTHR11022. 1 hit.
    Pfami PF01510. Amidase_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037945. PGRPs. 1 hit.
    SMARTi SM00644. Ami_2. 1 hit.
    SM00701. PGRP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55846. SSF55846. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster."
      Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.
      Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (PGRP-SC1B), PGN-BINDING, TISSUE SPECIFICITY, INDUCTION.
    2. "The evolution of parasite recognition genes in the innate immune system: purifying selection on Drosophila melanogaster peptidoglycan recognition proteins."
      Jiggins F.M., Hurst G.D.D.
      J. Mol. Evol. 57:598-605(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PGRP-SC1A AND PGRP-SC1B).
      Strain: DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti, Texas and ZW141.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (PGRP-SC1A AND PGRP-SC1B).
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (PGRP-SC1B).
      Strain: Berkeley.
      Tissue: Head.
    6. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (PGRP-SC1B).
      Strain: Berkeley.
      Tissue: Head.
    7. "A scavenger function for a Drosophila peptidoglycan recognition protein."
      Mellroth P., Karlsson J., Steiner H.
      J. Biol. Chem. 278:7059-7064(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY (PGRP-SC1B), PGN-BINDING, MUTAGENESIS OF CYS-168.

    Entry informationi

    Entry nameiPGSC1_DROME
    AccessioniPrimary (citable) accession number: Q9V3B7
    Secondary accession number(s): B5RJ78
    , Q70PU9, Q70PV0, Q95SQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3