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Q61475

- DAF1_MOUSE

UniProt

Q61475 - DAF1_MOUSE

Protein

Complement decay-accelerating factor, GPI-anchored

Gene

Cd55

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Protection of cells from complement-mediated damage.By similarity

    GO - Biological processi

    1. complement activation, classical pathway Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW
    3. regulation of complement activation, classical pathway Source: MGI

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_198562. Regulation of Complement cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement decay-accelerating factor, GPI-anchored
    Short name:
    DAF-GPI
    Alternative name(s):
    CD_antigen: CD55
    Gene namesi
    Name:Cd55
    Synonyms:Cd55a, Daf, Daf1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:104850. Cd55.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. external side of plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Sequence AnalysisAdd
    BLAST
    Chaini35 – 362328Complement decay-accelerating factor, GPI-anchoredPRO_0000006004Add
    BLAST
    Propeptidei363 – 39028Removed in mature formSequence AnalysisPRO_0000006005Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 81PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi98 ↔ 145PROSITE-ProRule annotation
    Disulfide bondi129 ↔ 158PROSITE-ProRule annotation
    Disulfide bondi163 ↔ 204PROSITE-ProRule annotation
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi190 ↔ 220PROSITE-ProRule annotation
    Disulfide bondi225 ↔ 267PROSITE-ProRule annotation
    Disulfide bondi253 ↔ 284PROSITE-ProRule annotation
    Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
    Lipidationi362 – 3621GPI-anchor amidated glycineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ61475.
    PRIDEiQ61475.

    PTM databases

    PhosphoSiteiQ61475.

    Expressioni

    Tissue specificityi

    Brain, secretory epithelia, skeletal muscle, liver, testes, thymus, spleen and lymph node.

    Gene expression databases

    BgeeiQ61475.
    CleanExiMM_CD55.
    GenevestigatoriQ61475.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61475.
    SMRiQ61475. Positions 35-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 9662Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 16064Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini161 – 22262Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini223 – 28664Sushi 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi288 – 36275Ser/Thr-richAdd
    BLAST

    Domaini

    The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 By similarity.By similarity

    Sequence similaritiesi

    Contains 4 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG150769.
    GeneTreeiENSGT00750000117418.
    HOVERGENiHBG001406.
    InParanoidiQ61475.
    KOiK04006.
    OMAiGHTCLIT.
    OrthoDBiEOG78WKS7.
    PhylomeDBiQ61475.
    TreeFamiTF334137.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 4 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 4 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 4 hits.
    PROSITEiPS50923. SUSHI. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61475-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIRGRAPRTR PSPPPPLLPL LSLSLLLLSP TVRGDCGPPP DIPNARPILG    50
    RHSKFAEQSK VAYSCNNGFK QVPDKSNIVV CLENGQWSSH ETFCEKSCVA 100
    PERLSFASLK KEYLNMNFFP VGTIVEYECR PGFRKQPPLP GKATCLEDLV 150
    WSPVAQFCKK KSCPNPKDLD NGHINIPTGI LFGSEINFSC NPGYRLVGVS 200
    STFCSVTGNT VDWDDEFPVC TEIHCPEPPK INNGIMRGES DSYTYSQVVT 250
    YSCDKGFILV GNASIYCTVS KSDVGQWSSP PPRCIEKSKV PTKKPTINVP 300
    STGTPSTPQK PTTESVPNPG DQPTPQKPST VKVSATQHVP VTKTTVRHPI 350
    RTSTDKGEPN TGGDRYIYGH TCLITLTVLH VMLSLIGYLT 390
    Length:390
    Mass (Da):42,618
    Last modified:February 26, 2008 - v2
    Checksum:iB4B872186947F8E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 93PRT → ARA in BAA09830. (PubMed:8671624)Curated
    Sequence conflicti83 – 831E → G in BAA09830. (PubMed:8671624)Curated
    Sequence conflicti91 – 911E → G in BAA09830. (PubMed:8671624)Curated
    Sequence conflicti98 – 981C → L in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti115 – 1151N → H in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti135 – 1351K → E in AAB00091. (PubMed:7545711)Curated
    Sequence conflicti143 – 1431A → S in CAJ18536. 1 PublicationCurated
    Sequence conflicti143 – 1431A → S in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti173 – 1731H → L in BAA09830. (PubMed:8671624)Curated
    Sequence conflicti180 – 1801I → T in BAA09830. (PubMed:8671624)Curated
    Sequence conflicti258 – 2581I → V in CAJ18536. 1 PublicationCurated
    Sequence conflicti258 – 2581I → V in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti313 – 3131T → L in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti381 – 3811V → A in CAJ18536. 1 PublicationCurated
    Sequence conflicti381 – 3811V → A in AAH11314. (PubMed:15489334)Curated
    Sequence conflicti381 – 3811V → A in AAD51449. (PubMed:10417349)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41366 mRNA. Translation: AAB00091.1.
    AK160994 mRNA. Translation: BAE36139.1.
    CT010328 mRNA. Translation: CAJ18536.1.
    BC011314 mRNA. Translation: AAH11314.1.
    D63679 mRNA. Translation: BAA09830.1.
    AB003320 Genomic DNA. Translation: BAA22908.1.
    AF143541 mRNA. Translation: AAD51449.1.
    CCDSiCCDS15256.1.
    RefSeqiNP_034146.2. NM_010016.2.
    UniGeneiMm.101591.

    Genome annotation databases

    EnsembliENSMUST00000027650; ENSMUSP00000027650; ENSMUSG00000026399.
    GeneIDi13136.
    KEGGimmu:13136.
    UCSCiuc007cly.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41366 mRNA. Translation: AAB00091.1 .
    AK160994 mRNA. Translation: BAE36139.1 .
    CT010328 mRNA. Translation: CAJ18536.1 .
    BC011314 mRNA. Translation: AAH11314.1 .
    D63679 mRNA. Translation: BAA09830.1 .
    AB003320 Genomic DNA. Translation: BAA22908.1 .
    AF143541 mRNA. Translation: AAD51449.1 .
    CCDSi CCDS15256.1.
    RefSeqi NP_034146.2. NM_010016.2.
    UniGenei Mm.101591.

    3D structure databases

    ProteinModelPortali Q61475.
    SMRi Q61475. Positions 35-285.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q61475.

    Proteomic databases

    PaxDbi Q61475.
    PRIDEi Q61475.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027650 ; ENSMUSP00000027650 ; ENSMUSG00000026399 .
    GeneIDi 13136.
    KEGGi mmu:13136.
    UCSCi uc007cly.1. mouse.

    Organism-specific databases

    CTDi 1604.
    MGIi MGI:104850. Cd55.

    Phylogenomic databases

    eggNOGi NOG150769.
    GeneTreei ENSGT00750000117418.
    HOVERGENi HBG001406.
    InParanoidi Q61475.
    KOi K04006.
    OMAi GHTCLIT.
    OrthoDBi EOG78WKS7.
    PhylomeDBi Q61475.
    TreeFami TF334137.

    Enzyme and pathway databases

    Reactomei REACT_198562. Regulation of Complement cascade.

    Miscellaneous databases

    NextBioi 283202.
    PROi Q61475.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61475.
    CleanExi MM_CD55.
    Genevestigatori Q61475.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 4 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 4 hits.
    PROSITEi PS50923. SUSHI. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal localization of the mouse decay-accelerating factor genes. Duplicated genes encode glycosylphosphatidylinositol-anchored and transmembrane forms."
      Spicer A.P., Seldin M.F., Gendler S.J.
      J. Immunol. 155:3079-3091(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    2. "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.
      Tissue: Head.
    3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    5. "Molecular cloning of murine decay accelerating factor by immunoscreening."
      Fukuoka Y., Yasui A., Okada N., Okada H.
      Int. Immunol. 8:379-385(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-390.
      Strain: BALB/c.
      Tissue: Spleen.
    6. "A new repetitive sequence uniquely present in the decay-accelerating factor genes."
      Nonaka M., Nonaka M., Takenaka O., Okada N., Okada H.
      Immunogenetics 47:246-255(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-353.
      Strain: BALB/c.
    7. "Molecular and functional analysis of mouse decay accelerating factor (CD55)."
      Harris C.L., Rushmere N.K., Morgan B.P.
      Biochem. J. 341:821-829(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-390.
      Strain: BALB/c.

    Entry informationi

    Entry nameiDAF1_MOUSE
    AccessioniPrimary (citable) accession number: Q61475
    Secondary accession number(s): P97732
    , Q3TU32, Q4FJS4, Q61397, Q76N72, Q921P0, Q9R1C1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 108 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3