DAF_PONPY
ID DAF_PONPY Reviewed; 340 AA.
AC P49457;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Complement decay-accelerating factor;
DE AltName: CD_antigen=CD55;
DE Flags: Precursor; Fragment;
GN Name=CD55; Synonyms=DAF;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7506731;
RA Nickells M.W., Alvarez J.I., Lublin D.M., Atkinson J.P.;
RT "Characterization of DAF-2, a high molecular weight form of decay-
RT accelerating factor (DAF; CD55), as a covalently cross-linked dimer of DAF-
RT 1.";
RL J. Immunol. 152:676-685(1994).
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 -!- SUBUNIT: Monomer (major form) and non-disulfide-linked, covalent
CC homodimer (minor form). Interacts with ADGRE5.
CC {ECO:0000250|UniProtKB:P08174}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=DAF-2;
CC IsoId=P49457-1; Sequence=Displayed;
CC Name=DAF-1;
CC IsoId=P49457-2; Sequence=Not described;
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 -!- PTM: The Ser/Thr-rich domain is heavily O-glycosylated.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; S67775; AAC60609.1; -; mRNA.
DR PIR; I56234; I56234.
DR AlphaFoldDB; P49457; -.
DR SMR; P49457; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd00033; CCP; 3.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 3.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Complement pathway; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunity; Innate immunity; Lipoprotein; Membrane;
KW Repeat; Sushi.
FT CHAIN <1..312
FT /note="Complement decay-accelerating factor"
FT /id="PRO_0000006002"
FT PROPEP 313..340
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000006003"
FT DOMAIN <1..55
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 56..119
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 120..181
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 182..244
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 235..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 312
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 57..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 88..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 122..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 149..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 184..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 212..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT NON_TER 1
SQ SEQUENCE 340 AA; 37180 MW; D3D865C058204290 CRC64;
VPNAQPALEG RTSFPEDTVV TYKCEESFMK IPGKKDSVIC LKGSQWSDIE EFCNRSCEVP
TRLNFASLKQ PYITQNYFPV GTTVEYVCRP GYRRELSLST KLTCLQNLTW STAVEFCKKK
SCPNPGEIRN GQIDVSNGIL FGATISFSCN TGYKLFGPTS SLCLISGSSV QWSDPLPECR
EIYCPAPPQI DNGIIQGKRD HYGYRQSITY ACNKGYTMIG EHSIYCTVND DEGEWSGPPP
ECRGKSLTSK VPPTVQKPTT VNVPTTEVSP TSQKTTTKTT TPNAQATRST PVSRTTKHFH
ETTPNKGSGT TSGTTSLLSG HKCFTLTGLL GTLVTMGLLT
