DAF1_MOUSE
ID DAF1_MOUSE Reviewed; 390 AA.
AC Q61475; P97732; Q3TU32; Q4FJS4; Q61397; Q76N72; Q921P0; Q9R1C1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Complement decay-accelerating factor, GPI-anchored;
DE Short=DAF-GPI;
DE AltName: CD_antigen=CD55;
DE Flags: Precursor;
GN Name=Cd55; Synonyms=Cd55a, Daf, Daf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=7545711;
RA Spicer A.P., Seldin M.F., Gendler S.J.;
RT "Molecular cloning and chromosomal localization of the mouse decay-
RT accelerating factor genes. Duplicated genes encode
RT glycosylphosphatidylinositol-anchored and transmembrane forms.";
RL J. Immunol. 155:3079-3091(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-390.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8671624; DOI=10.1093/intimm/8.3.379;
RA Fukuoka Y., Yasui A., Okada N., Okada H.;
RT "Molecular cloning of murine decay accelerating factor by
RT immunoscreening.";
RL Int. Immunol. 8:379-385(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-353.
RC STRAIN=BALB/cJ;
RX PubMed=9435343; DOI=10.1007/s002510050354;
RA Nonaka M., Nonaka M., Takenaka O., Okada N., Okada H.;
RT "A new repetitive sequence uniquely present in the decay-accelerating
RT factor genes.";
RL Immunogenetics 47:246-255(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 369-390.
RC STRAIN=BALB/cJ;
RX PubMed=10417349; DOI=10.1042/bj3410821;
RA Harris C.L., Rushmere N.K., Morgan B.P.;
RT "Molecular and functional analysis of mouse decay accelerating factor
RT (CD55).";
RL Biochem. J. 341:821-829(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This protein recognizes C4b and C3b fragments that condense
CC with cell-surface hydroxyl or amino groups when nascent C4b and C3b are
CC locally generated during C4 and c3 activation. Interaction of daf with
CC cell-associated C4b and C3b polypeptides interferes with their ability
CC to catalyze the conversion of C2 and factor B to enzymatically active
CC C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the
CC amplification convertases of the complement cascade. Inhibits
CC complement activation by destabilizing and preventing the formation of
CC C3 and C5 convertases, which prevents complement damage.
CC {ECO:0000250|UniProtKB:P08174}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain, secretory epithelia, skeletal muscle, liver,
CC testes, thymus, spleen and lymph node.
CC -!- DOMAIN: The first Sushi domain (SCR1) is not necessary for function.
CC SCR2 and SCR4 provide the proper conformation for the active site on
CC SCR3 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; L41366; AAB00091.1; -; mRNA.
DR EMBL; AK160994; BAE36139.1; -; mRNA.
DR EMBL; CT010328; CAJ18536.1; -; mRNA.
DR EMBL; BC011314; AAH11314.1; -; mRNA.
DR EMBL; D63679; BAA09830.1; -; mRNA.
DR EMBL; AB003320; BAA22908.1; -; Genomic_DNA.
DR EMBL; AF143541; AAD51449.1; -; mRNA.
DR CCDS; CCDS15256.1; -.
DR RefSeq; NP_034146.2; NM_010016.3.
DR RefSeq; XP_017169792.1; XM_017314303.1.
DR AlphaFoldDB; Q61475; -.
DR SMR; Q61475; -.
DR STRING; 10090.ENSMUSP00000027650; -.
DR GlyGen; Q61475; 2 sites.
DR PhosphoSitePlus; Q61475; -.
DR CPTAC; non-CPTAC-3972; -.
DR EPD; Q61475; -.
DR MaxQB; Q61475; -.
DR PaxDb; Q61475; -.
DR PeptideAtlas; Q61475; -.
DR PRIDE; Q61475; -.
DR ProteomicsDB; 279312; -.
DR DNASU; 13136; -.
DR Ensembl; ENSMUST00000027650; ENSMUSP00000027650; ENSMUSG00000026399.
DR GeneID; 13136; -.
DR KEGG; mmu:13136; -.
DR UCSC; uc007cly.1; mouse.
DR CTD; 1604; -.
DR MGI; MGI:104850; Cd55.
DR VEuPathDB; HostDB:ENSMUSG00000026399; -.
DR eggNOG; ENOG502RXMW; Eukaryota.
DR GeneTree; ENSGT00940000162307; -.
DR HOGENOM; CLU_020107_0_1_1; -.
DR InParanoid; Q61475; -.
DR OMA; DTREDQK; -.
DR OrthoDB; 1101732at2759; -.
DR PhylomeDB; Q61475; -.
DR TreeFam; TF334137; -.
DR BioGRID-ORCS; 13136; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q61475; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61475; protein.
DR Bgee; ENSMUSG00000026399; Expressed in decidua and 203 other tissues.
DR ExpressionAtlas; Q61475; baseline and differential.
DR Genevisible; Q61475; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045916; P:negative regulation of complement activation; ISS:UniProtKB.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; ISO:MGI.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:MGI.
DR GO; GO:0030449; P:regulation of complement activation; ISO:MGI.
DR GO; GO:0030450; P:regulation of complement activation, classical pathway; IMP:MGI.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Complement pathway; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunity; Innate immunity; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Sushi.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..362
FT /note="Complement decay-accelerating factor, GPI-anchored"
FT /id="PRO_0000006004"
FT PROPEP 363..390
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000006005"
FT DOMAIN 35..96
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 97..160
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 161..222
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 223..286
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 273..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 362
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 65..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 98..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 129..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 163..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 190..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 225..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 253..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 7..9
FT /note="PRT -> ARA (in Ref. 5; BAA09830)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="E -> G (in Ref. 5; BAA09830)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="E -> G (in Ref. 5; BAA09830)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="C -> L (in Ref. 4; AAH11314)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="N -> H (in Ref. 4; AAH11314)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> E (in Ref. 1; AAB00091)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> S (in Ref. 3; CAJ18536 and 4; AAH11314)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="H -> L (in Ref. 5; BAA09830)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="I -> T (in Ref. 5; BAA09830)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="I -> V (in Ref. 3; CAJ18536 and 4; AAH11314)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="T -> L (in Ref. 4; AAH11314)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="V -> A (in Ref. 3; CAJ18536, 4; AAH11314 and 7;
FT AAD51449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 42618 MW; B4B872186947F8E4 CRC64;
MIRGRAPRTR PSPPPPLLPL LSLSLLLLSP TVRGDCGPPP DIPNARPILG RHSKFAEQSK
VAYSCNNGFK QVPDKSNIVV CLENGQWSSH ETFCEKSCVA PERLSFASLK KEYLNMNFFP
VGTIVEYECR PGFRKQPPLP GKATCLEDLV WSPVAQFCKK KSCPNPKDLD NGHINIPTGI
LFGSEINFSC NPGYRLVGVS STFCSVTGNT VDWDDEFPVC TEIHCPEPPK INNGIMRGES
DSYTYSQVVT YSCDKGFILV GNASIYCTVS KSDVGQWSSP PPRCIEKSKV PTKKPTINVP
STGTPSTPQK PTTESVPNPG DQPTPQKPST VKVSATQHVP VTKTTVRHPI RTSTDKGEPN
TGGDRYIYGH TCLITLTVLH VMLSLIGYLT
