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P39205

- CIN_DROME

UniProt

P39205 - CIN_DROME

Protein

Molybdenum cofactor synthesis protein cinnamon

Gene

cin

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.1 Publication

    Catalytic activityi

    ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
    Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. molybdopterin adenylyltransferase activity Source: UniProtKB-EC
    4. molybdopterin molybdotransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. embryonic development via the syncytial blastoderm Source: FlyBase
    2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_180227. Molybdenum cofactor biosynthesis.
    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdenum cofactor synthesis protein cinnamon
    Including the following 2 domains:
    Molybdopterin adenylyltransferase (EC:2.7.7.75)
    Short name:
    MPT adenylyltransferase
    Alternative name(s):
    Domain G
    Molybdopterin molybdenumtransferase (EC:2.10.1.1)
    Short name:
    MPT Mo-transferase
    Alternative name(s):
    Domain E
    Gene namesi
    Name:cin
    ORF Names:CG2945
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0000316. cin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601Molybdenum cofactor synthesis protein cinnamonPRO_0000170962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei376 – 3761Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP39205.

    Expressioni

    Developmental stagei

    Detected primarily in the epidermal cells of the segmental grooves during germ-band retraction (7-9 hours after egg laying).1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP39205.
    SMRiP39205. Positions 7-156, 198-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3 – 153151MPT adenylyltransferaseAdd
    BLAST
    Regioni184 – 596413MPT Mo-transferaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the MoaB/Mog family.Curated
    In the C-terminal section; belongs to the MoeA family.Curated

    Phylogenomic databases

    eggNOGiCOG0303.
    GeneTreeiENSGT00390000016577.
    HOGENOMiHOG000218563.
    InParanoidiP39205.
    KOiK15376.
    OMAiNIPPFRA.
    OrthoDBiEOG70087N.
    PhylomeDBiP39205.

    Family and domain databases

    Gene3Di2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProiIPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view]
    PfamiPF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view]
    SMARTiSM00852. MoCF_biosynth. 2 hits.
    [Graphical view]
    SUPFAMiSSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
    PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESITFGVLT ISDTCWQEPE KDTSGPILRQ LIGETFANTQ VIGNIVPDEK    50
    DIIQQELRKW IDREELRVIL TTGGTGFAPR DVTPEATRQL LEKECPQLSM 100
    YITLESIKQT QYAALSRGLC GIAGNTLILN LPGSEKAVKE CFQTISALLP 150
    HAVHLIGDDV SLVRKTHAEV QGSAQKSHIC PHKTGTGTDS DRNSPYPMLP 200
    VQEVLSIIFN TVQKTANLNK ILLEMNAPVN IPPFRASIKD GYAMKSTGFS 250
    GTKRVLGCIA AGDSPNSLPL AEDECYKINT GAPLPLEADC VVQVEDTKLL 300
    QLDKNGQESL VDILVEPQAG LDVRPVGYDL STNDRIFPAL DPSPVVVKSL 350
    LASVGNRLIL SKPKVAIVST GSELCSPRNQ LTPGKIFDSN TTMLTELLVY 400
    FGFNCMHTCV LSDSFQRTKE SLLELFEVVD FVICSGGVSM GDKDFVKSVL 450
    EDLQFRIHCG RVNIKPGKPM TFASRKDKYF FGLPGNPVSA FVTFHLFALP 500
    AIRFAAGWDR CKCSLSVLNV KLLNDFSLDS RPEFVRASVI SKSGELYASV 550
    NGNQISSRLQ SIVGADVLIN LPARTSDRPL AKAGEIFPAS VLRFDFISKY 600
    E 601
    Length:601
    Mass (Da):65,733
    Last modified:January 23, 2007 - v3
    Checksum:iDFA6926E955BF287
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti414 – 4141S → T in AAA65877. (PubMed:8088525)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19876 mRNA. Translation: AAA65877.1.
    AE014298 Genomic DNA. Translation: AAN09010.1.
    AL050231 Genomic DNA. Translation: CAB65851.1. Sequence problems.
    AL050231 Genomic DNA. Translation: CAB65852.1.
    AY069078 mRNA. Translation: AAL39223.1.
    PIRiS47896.
    RefSeqiNP_477030.1. NM_057682.3.
    NP_726659.1. NM_166835.3.
    UniGeneiDm.2294.

    Genome annotation databases

    EnsemblMetazoaiFBtr0070064; FBpp0070063; FBgn0000316.
    FBtr0070065; FBpp0070064; FBgn0000316.
    GeneIDi30973.
    KEGGidme:Dmel_CG2945.
    UCSCiCG2945-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19876 mRNA. Translation: AAA65877.1 .
    AE014298 Genomic DNA. Translation: AAN09010.1 .
    AL050231 Genomic DNA. Translation: CAB65851.1 . Sequence problems.
    AL050231 Genomic DNA. Translation: CAB65852.1 .
    AY069078 mRNA. Translation: AAL39223.1 .
    PIRi S47896.
    RefSeqi NP_477030.1. NM_057682.3.
    NP_726659.1. NM_166835.3.
    UniGenei Dm.2294.

    3D structure databases

    ProteinModelPortali P39205.
    SMRi P39205. Positions 7-156, 198-592.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P39205.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070064 ; FBpp0070063 ; FBgn0000316 .
    FBtr0070065 ; FBpp0070064 ; FBgn0000316 .
    GeneIDi 30973.
    KEGGi dme:Dmel_CG2945.
    UCSCi CG2945-RA. d. melanogaster.

    Organism-specific databases

    CTDi 30973.
    FlyBasei FBgn0000316. cin.

    Phylogenomic databases

    eggNOGi COG0303.
    GeneTreei ENSGT00390000016577.
    HOGENOMi HOG000218563.
    InParanoidi P39205.
    KOi K15376.
    OMAi NIPPFRA.
    OrthoDBi EOG70087N.
    PhylomeDBi P39205.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    Reactomei REACT_180227. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    GenomeRNAii 30973.
    NextBioi 771251.
    PROi P39205.

    Family and domain databases

    Gene3Di 2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProi IPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view ]
    Pfami PF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view ]
    SMARTi SM00852. MoCF_biosynth. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsi TIGR00177. molyb_syn. 2 hits.
    PROSITEi PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin."
      Kamdar K.P., Shelton M.E., Finnerty V.
      Genetics 137:791-801(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Berkeley.
    3. "The Drosophila cinnamon gene is functionally homologous to Arabidopsis cnx1 and has a similar expression pattern to the mammalian gephyrin gene."
      Wittle A.E., Kamdar K.P., Finnerty V.
      Mol. Gen. Genet. 261:672-680(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Oregon-R.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    7. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCIN_DROME
    AccessioniPrimary (citable) accession number: P39205
    Secondary accession number(s): Q0KHX9, Q9U1M0, Q9V3E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3