DAF2_MOUSE
ID DAF2_MOUSE Reviewed; 407 AA.
AC Q61476; E9QLT3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Complement decay-accelerating factor transmembrane isoform;
DE Short=DAF-TM;
DE AltName: CD_antigen=CD55;
DE Flags: Precursor;
GN Name=Cd55b; Synonyms=Daf2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis, 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; L41365; AAB00092.1; -; mRNA.
DR EMBL; AC111067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001304290.1; NM_001317361.1.
DR RefSeq; NP_031853.2; NM_007827.3.
DR AlphaFoldDB; Q61476; -.
DR SMR; Q61476; -.
DR STRING; 10090.ENSMUSP00000108107; -.
DR GlyGen; Q61476; 2 sites.
DR MaxQB; Q61476; -.
DR PaxDb; Q61476; -.
DR PRIDE; Q61476; -.
DR ProteomicsDB; 279359; -.
DR DNASU; 13137; -.
DR GeneID; 13137; -.
DR KEGG; mmu:13137; -.
DR CTD; 13137; -.
DR MGI; MGI:104849; Cd55b.
DR eggNOG; ENOG502RXMW; Eukaryota.
DR InParanoid; Q61476; -.
DR OrthoDB; 1101732at2759; -.
DR BioGRID-ORCS; 13137; 3 hits in 39 CRISPR screens.
DR PRO; PR:Q61476; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61476; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 2: Evidence at transcript level;
KW Complement pathway; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Reference proteome; Repeat; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..407
FT /note="Complement decay-accelerating factor transmembrane
FT isoform"
FT /id="PRO_0000006006"
FT TOPO_DOM 40..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..101
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 102..165
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 166..227
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 228..291
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 301..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 70..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 103..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 134..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 168..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 195..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 230..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 258..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 212
FT /note="I -> T (in Ref. 1; AAB00092)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="T -> A (in Ref. 1; AAB00092)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> D (in Ref. 1; AAB00092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 44511 MW; 12C461C9A69A9C76 CRC64;
MVSSTWGYDP RAGAGDLVIT TTAAGAVTIA VLLFQTVCGD CGPPPDIPNA RPILGRHSKF
AEQSKVAYSC NNGFKQVPDK SNIVVCLENG QWSSHETFCE KSCDTPERLS FASLKKEYFN
MNFFPVGTIV EYECRPGFRK QPSLSGKSTC LEDLVWSPVA QFCKKKSCPN PKDLDNGHIN
IPTGILFGSE INFSCNPGYR LVGITSILCT IIGNTVDWDD EFPVCTEIFC PDPPKINNGI
MRGESDSYKY SQVVIYSCDK GFILFGNSTI YCTVSKSDVG QWSSPPPQCI EESKVPIKKP
VVNVPSTGIP STPQKPTTES VPNPGDQPTP QKPSTVKVPA TQHEPDTTTR TSTDKGESNS
GGDRYIYGFV AVIAMIDSLI IVKTLWTILS PNRRSDFQGK ERKDVSK
