Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9VN93

- CPR1_DROME

UniProt

Q9VN93 - CPR1_DROME

Protein

Putative cysteine proteinase CG12163

Gene

CG12163

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (11 Jul 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May have a role in autophagic cell death.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei418 – 4181By similarity
    Active sitei555 – 5551By similarity
    Active sitei581 – 5811By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity Source: InterPro
    2. cysteine-type peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. autophagic cell death Source: FlyBase
    2. chaeta development Source: FlyBase
    3. salivary gland cell autophagic cell death Source: FlyBase
    4. wing disc development Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    ReactomeiREACT_180993. MHC class II antigen presentation.

    Protein family/group databases

    MEROPSiC01.A27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative cysteine proteinase CG12163 (EC:3.4.22.-)
    Gene namesi
    ORF Names:CG12163
    OrganismiDrosophila melanogaster (Fruit fly)Imported
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0260462. CG12163.

    Subcellular locationi

    GO - Cellular componenti

    1. fusome Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 393373Activation peptideBy similarityPRO_0000026368Add
    BLAST
    Chaini394 – 614221Putative cysteine proteinase CG12163PRO_0000026369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi415 ↔ 456By similarity
    Disulfide bondi449 ↔ 489By similarity
    Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi548 ↔ 602By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9VN93.
    PRIDEiQ9VN93.

    Expressioni

    Gene expression databases

    BgeeiQ9VN93.

    Interactioni

    Protein-protein interaction databases

    BioGridi65841. 4 interactions.
    DIPiDIP-17491N.
    IntActiQ9VN93. 1 interaction.
    MINTiMINT-763966.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VN93.
    SMRiQ9VN93. Positions 194-273, 318-613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    GeneTreeiENSGT00750000117440.
    InParanoidiQ9VN93.
    KOiK01373.
    OMAiGPRWGEQ.
    OrthoDBiEOG7DJSKG.
    PhylomeDBiQ9VN93.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR000010. Prot_inh_cystat.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00043. CY. 1 hit.
    SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A1 Publication (identifier: Q9VN93-1) [UniParc]FASTAAdd to Basket

    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

    MRLFAAATVA LVLLLGQAAG EELAEERAGQ AQGDAESTES SETTTDQAVS    50
    EPPITLVHVL NPGEREYLSP NLIGVQNIAM TFLPLSMNFV NIIDAFREIT 100
    AGVRYEILLN ALDTKAIQPA EADIVCRLVI LEKPWLRTQW GDKHRELVTS 150
    NCTDPAVNSV AGDPAEKARL LNEKYVHRSR RSANDILGRH KPYDEEAAKA 200
    QLQKSLDKLT AGEGPHYKIV KVYSASRQVD SGILTRIDAD LIDGSEEQHR 250
    CIVDIWTKVW VRKDEHEITF KCRNQPVVQA RHTRSVEWAE KKTHKKHSHR 300
    FDKVDHLFYK FQVRFGRRYV STAERQMRLR IFRQNLKTIE ELNANEMGSA 350
    KYGITEFADM TSSEYKERTG LWQRDEAKAT GGSAAVVPAY HGELPKEFDW 400
    RQKDAVTQVK NQGSCGSCWA FSVTGNIEGL YAVKTGELKE FSEQELLDCD 450
    TTDSACNGGL MDNAYKAIKD IGGLEYEAEY PYKAKKNQCH FNRTLSHVQV 500
    AGFVDLPKGN ETAMQEWLLA NGPISIGINA NAMQFYRGGV SHPWKALCSK 550
    KNLDHGVLVV GYGVSDYPNF HKTLPYWIVK NSWGPRWGEQ GYYRVYRGDN 600
    TCGVSEMATS AVLA 614

    Note: No experimental confirmation available.Curated

    Length:614
    Mass (Da):68,961
    Last modified:July 11, 2003 - v2
    Checksum:iC44D32383375E032
    GO
    Isoform B1 Publication (identifier: Q9VN93-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         37-175: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:475
    Mass (Da):53,545
    Checksum:i130DE83869498EF1
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 175139Missing in isoform B. 1 PublicationVSP_050566Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF52055.2.
    AE014297 Genomic DNA. Translation: AAN13266.1.
    AY121614 mRNA. Translation: AAM51941.1. Sequence problems.
    BT003231 mRNA. Translation: AAO24986.1.
    RefSeqiNP_649521.1. NM_141264.4. [Q9VN93-2]
    NP_730901.1. NM_169033.4. [Q9VN93-1]
    NP_730902.2. NM_169034.4.
    UniGeneiDm.7315.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078823; FBpp0078465; FBgn0260462. [Q9VN93-1]
    GeneIDi40628.
    KEGGidme:Dmel_CG12163.
    UCSCiCG12163-RA. d. melanogaster. [Q9VN93-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF52055.2 .
    AE014297 Genomic DNA. Translation: AAN13266.1 .
    AY121614 mRNA. Translation: AAM51941.1 . Sequence problems.
    BT003231 mRNA. Translation: AAO24986.1 .
    RefSeqi NP_649521.1. NM_141264.4. [Q9VN93-2 ]
    NP_730901.1. NM_169033.4. [Q9VN93-1 ]
    NP_730902.2. NM_169034.4.
    UniGenei Dm.7315.

    3D structure databases

    ProteinModelPortali Q9VN93.
    SMRi Q9VN93. Positions 194-273, 318-613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65841. 4 interactions.
    DIPi DIP-17491N.
    IntActi Q9VN93. 1 interaction.
    MINTi MINT-763966.

    Protein family/group databases

    MEROPSi C01.A27.

    Proteomic databases

    PaxDbi Q9VN93.
    PRIDEi Q9VN93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078823 ; FBpp0078465 ; FBgn0260462 . [Q9VN93-1 ]
    GeneIDi 40628.
    KEGGi dme:Dmel_CG12163.
    UCSCi CG12163-RA. d. melanogaster. [Q9VN93-1 ]

    Organism-specific databases

    FlyBasei FBgn0260462. CG12163.

    Phylogenomic databases

    eggNOGi COG4870.
    GeneTreei ENSGT00750000117440.
    InParanoidi Q9VN93.
    KOi K01373.
    OMAi GPRWGEQ.
    OrthoDBi EOG7DJSKG.
    PhylomeDBi Q9VN93.

    Enzyme and pathway databases

    Reactomei REACT_180993. MHC class II antigen presentation.

    Miscellaneous databases

    GenomeRNAii 40628.
    NextBioi 819744.
    PROi Q9VN93.

    Gene expression databases

    Bgeei Q9VN93.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR000010. Prot_inh_cystat.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00043. CY. 1 hit.
    SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: Berkeley1 Publication.
    2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley1 Publication.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley1 Publication.
      Tissue: Head1 Publication, Larva1 Publication and Pupae1 Publication.
    4. Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiCPR1_DROME
    AccessioniPrimary (citable) accession number: Q9VN93
    Secondary accession number(s): Q867H7, Q9VN92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: July 11, 2003
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3