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O54786

- DFFA_MOUSE

UniProt

O54786 - DFFA_MOUSE

Protein

DNA fragmentation factor subunit alpha

Gene

Dffa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Inhibitor of the caspase-activated DNase (DFF40).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei117 – 1182Cleavage; by caspase-3By similarity
    Sitei224 – 2252Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: Ensembl
    2. negative regulation of apoptotic DNA fragmentation Source: MGI
    3. negative regulation of execution phase of apoptosis Source: RefGenome
    4. positive regulation of apoptotic process Source: MGI
    5. thymocyte apoptotic process Source: MGI

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_205002. Activation of DNA fragmentation factor.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA fragmentation factor subunit alpha
    Alternative name(s):
    DNA fragmentation factor 45 kDa subunit
    Short name:
    DFF-45
    Inhibitor of CAD
    Short name:
    ICAD
    Gene namesi
    Name:Dffa
    Synonyms:Icad
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1196227. Dffa.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear chromatin Source: RefGenome
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 331331DNA fragmentation factor subunit alphaPRO_0000144717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Post-translational modificationi

    Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO54786.
    PaxDbiO54786.
    PRIDEiO54786.

    PTM databases

    PhosphoSiteiO54786.

    Miscellaneous databases

    PMAP-CutDBQ8BQC7.

    Expressioni

    Gene expression databases

    BgeeiO54786.
    CleanExiMM_DFFA.
    GenevestigatoriO54786.

    Interactioni

    Subunit structurei

    Heterodimer of DFFA and DFFB.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DffbO547886EBI-1634519,EBI-7365197

    Protein-protein interaction databases

    BioGridi199211. 2 interactions.
    IntActiO54786. 2 interactions.
    MINTiMINT-142152.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116
    Beta strandi19 – 257
    Beta strandi28 – 3811
    Helixi39 – 5012
    Helixi54 – 563
    Beta strandi60 – 667
    Beta strandi72 – 798
    Beta strandi84 – 885
    Beta strandi90 – 923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F2RNMR-I1-100[»]
    ProteinModelPortaliO54786.
    SMRiO54786. Positions 1-100, 239-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO54786.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9680CIDE-NPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CIDE-N domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG40170.
    GeneTreeiENSGT00510000048128.
    HOGENOMiHOG000112204.
    HOVERGENiHBG000683.
    InParanoidiQ8BQC7.
    KOiK02310.
    OMAiNEKWAYN.
    OrthoDBiEOG7JQBP8.
    TreeFamiTF102021.

    Family and domain databases

    Gene3Di1.10.1490.10. 1 hit.
    InterProiIPR003508. CIDE-N_dom.
    IPR027296. DFF-C_dom.
    IPR017299. DNA_fragmentation_factor_asu.
    IPR015121. DNA_fragmentation_mid_dom.
    [Graphical view]
    PfamiPF02017. CIDE-N. 1 hit.
    PF09033. DFF-C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037865. DFF_alpha. 1 hit.
    ProDomiPD316494. DNA_fragmentation_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00266. CAD. 1 hit.
    [Graphical view]
    SUPFAMiSSF81783. SSF81783. 1 hit.
    PROSITEiPS51135. CIDE_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform ICAD-L (identifier: O54786-1) [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

    MELSRGASAP DPDDVRPLKP CLLRRNHSRD QHGVAASSLE ELRSKACELL    50
    AIDKSLTPIT LVLAEDGTIV DDDDYFLCLP SNTKFVALAC NEKWIYNDSD 100
    GGTAWVSQES FEADEPDSRA GVKWKNVARQ LKEDLSSIIL LSEEDLQALI 150
    DIPCAELAQE LCQSCATVQG LQSTLQQVLD QREEARQSKQ LLELYLQALE 200
    KEGNILSNQK ESKAALSEEL DAVDTGVGRE MASEVLLRSQ ILTTLKEKPA 250
    PELSLSSQDL ESVSKEDPKA LAVALSWDIR KAETVQQACT TELALRLQQV 300
    QSLHSLRNLS ARRSPLPGEP QRPKRAKRDS S 331
    Length:331
    Mass (Da):36,572
    Last modified:July 27, 2011 - v2
    Checksum:i4EA9314DD470040F
    GO
    Isoform ICAD-S (identifier: O54786-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-265: SVSK → VGKN
         266-331: Missing.

    Show »
    Length:265
    Mass (Da):29,183
    Checksum:i588DCABE1E987912
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951I → T in BAA24140. (PubMed:9422506)Curated
    Sequence conflicti95 – 951I → T in BAA24141. (PubMed:9422513)Curated
    Sequence conflicti95 – 951I → T in CAQ52098. (PubMed:19468303)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei262 – 2654SVSK → VGKN in isoform ICAD-S. CuratedVSP_001087
    Alternative sequencei266 – 33166Missing in isoform ICAD-S. CuratedVSP_001088Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009375 mRNA. Translation: BAA24140.1.
    AB009376 mRNA. Translation: BAA24141.1.
    AK051011 mRNA. Translation: BAC34496.1.
    AL611967 Genomic DNA. Translation: CAM13988.1.
    CU210839 Genomic DNA. Translation: CAQ52098.1.
    CCDSiCCDS18951.1. [O54786-1]
    CCDS18952.1. [O54786-2]
    RefSeqiNP_001020467.1. NM_001025296.2. [O54786-1]
    UniGeneiMm.41433.

    Genome annotation databases

    EnsembliENSMUST00000030816; ENSMUSP00000030816; ENSMUSG00000028974. [O54786-1]
    ENSMUST00000103216; ENSMUSP00000099505; ENSMUSG00000028974. [O54786-2]
    GeneIDi13347.
    KEGGimmu:13347.
    UCSCiuc008vvr.1. mouse. [O54786-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009375 mRNA. Translation: BAA24140.1 .
    AB009376 mRNA. Translation: BAA24141.1 .
    AK051011 mRNA. Translation: BAC34496.1 .
    AL611967 Genomic DNA. Translation: CAM13988.1 .
    CU210839 Genomic DNA. Translation: CAQ52098.1 .
    CCDSi CCDS18951.1. [O54786-1 ]
    CCDS18952.1. [O54786-2 ]
    RefSeqi NP_001020467.1. NM_001025296.2. [O54786-1 ]
    UniGenei Mm.41433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F2R NMR - I 1-100 [» ]
    ProteinModelPortali O54786.
    SMRi O54786. Positions 1-100, 239-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199211. 2 interactions.
    IntActi O54786. 2 interactions.
    MINTi MINT-142152.

    PTM databases

    PhosphoSitei O54786.

    Proteomic databases

    MaxQBi O54786.
    PaxDbi O54786.
    PRIDEi O54786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030816 ; ENSMUSP00000030816 ; ENSMUSG00000028974 . [O54786-1 ]
    ENSMUST00000103216 ; ENSMUSP00000099505 ; ENSMUSG00000028974 . [O54786-2 ]
    GeneIDi 13347.
    KEGGi mmu:13347.
    UCSCi uc008vvr.1. mouse. [O54786-1 ]

    Organism-specific databases

    CTDi 1676.
    MGIi MGI:1196227. Dffa.

    Phylogenomic databases

    eggNOGi NOG40170.
    GeneTreei ENSGT00510000048128.
    HOGENOMi HOG000112204.
    HOVERGENi HBG000683.
    InParanoidi Q8BQC7.
    KOi K02310.
    OMAi NEKWAYN.
    OrthoDBi EOG7JQBP8.
    TreeFami TF102021.

    Enzyme and pathway databases

    Reactomei REACT_205002. Activation of DNA fragmentation factor.

    Miscellaneous databases

    EvolutionaryTracei O54786.
    NextBioi 283666.
    PMAP-CutDB Q8BQC7.
    PROi O54786.
    SOURCEi Search...

    Gene expression databases

    Bgeei O54786.
    CleanExi MM_DFFA.
    Genevestigatori O54786.

    Family and domain databases

    Gene3Di 1.10.1490.10. 1 hit.
    InterProi IPR003508. CIDE-N_dom.
    IPR027296. DFF-C_dom.
    IPR017299. DNA_fragmentation_factor_asu.
    IPR015121. DNA_fragmentation_mid_dom.
    [Graphical view ]
    Pfami PF02017. CIDE-N. 1 hit.
    PF09033. DFF-C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037865. DFF_alpha. 1 hit.
    ProDomi PD316494. DNA_fragmentation_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00266. CAD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81783. SSF81783. 1 hit.
    PROSITEi PS51135. CIDE_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD."
      Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S.
      Nature 391:43-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis."
      Sakahira H., Enari M., Nagata S.
      Nature 391:96-99(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiDFFA_MOUSE
    AccessioniPrimary (citable) accession number: O54786
    Secondary accession number(s): B2KFX0, O54787, Q8BQC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    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