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   24-JAN-2024, entry version 165.
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   BioGRID; 199046; 1.
DR   STRING; 10090.ENSMUSP00000027650; -.
DR   GlyCosmos; Q61475; 2 sites, No reported glycans.
DR   GlyGen; Q61475; 2 sites.
DR   PhosphoSitePlus; Q61475; -.
DR   SwissPalm; Q61475; -.
DR   CPTAC; non-CPTAC-3972; -.
DR   EPD; Q61475; -.
DR   MaxQB; Q61475; -.
DR   PaxDb; 10090-ENSMUSP00000027650; -.
DR   PeptideAtlas; Q61475; -.
DR   ProteomicsDB; 279312; -.
DR   DNASU; 13136; -.
DR   Ensembl; ENSMUST00000027650.13; ENSMUSP00000027650.7; ENSMUSG00000026399.13.
DR   GeneID; 13136; -.
DR   KEGG; mmu:13136; -.
DR   UCSC; uc007cly.1; mouse.
DR   AGR; MGI:104850; -.
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; PTCTEIF; -.
DR   OrthoDB; 2901311at2759; -.
DR   PhylomeDB; Q61475; -.
DR   TreeFam; TF334137; -.
DR   Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-977606; Regulation of Complement cascade.
DR   BioGRID-ORCS; 13136; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q61475; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q61475; Protein.
DR   Bgee; ENSMUSG00000026399; Expressed in decidua and 206 other cell types or tissues.
DR   ExpressionAtlas; Q61475; baseline and differential.
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: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   CDD; cd00033; CCP; 4.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF317; COMPLEMENT DECAY-ACCELERATING FACTOR; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   SMART; SM00032; CCP; 4.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR   PROSITE; PS50923; SUSHI; 4.
DR   Genevisible; Q61475; MM.
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
//