DAF_CAVPO
ID DAF_CAVPO Reviewed; 507 AA.
AC Q60401; P97254; P97255; P97256; Q60402; Q60403; Q60404; Q60405; Q60406;
AC Q9WTI9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Complement decay-accelerating factor;
DE AltName: CD_antigen=CD55;
DE Flags: Precursor;
GN Name=CD55; Synonyms=DAF;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GPI-ANCHOR AT ALA-358 (ISOFORM
RP 3), AND ALTERNATIVE SPLICING.
RC STRAIN=Hartley; TISSUE=Spleen;
RX PubMed=7545710;
RA Nonaka M., Miwa T., Okada N., Nonaka M., Okada H.;
RT "Multiple isoforms of guinea pig decay-accelerating factor (DAF) generated
RT by alternative splicing.";
RL J. Immunol. 155:3037-3048(1995).
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: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q60401-1; Sequence=Displayed;
CC Name=2; Synonyms=GDA-TCS;
CC IsoId=Q60401-2; Sequence=VSP_001193, VSP_001194, VSP_001199;
CC Name=3; Synonyms=GDAB-GPI;
CC IsoId=Q60401-3; Sequence=VSP_001194, VSP_001195, VSP_001196,
CC VSP_001197;
CC Name=4; Synonyms=GDAB-SEC;
CC IsoId=Q60401-4; Sequence=VSP_001194, VSP_001195, VSP_001196,
CC VSP_001198;
CC Name=5; Synonyms=GDAB-TCL;
CC IsoId=Q60401-5; Sequence=VSP_001194, VSP_001196;
CC Name=6; Synonyms=GDABC-TCL;
CC IsoId=Q60401-6; Sequence=VSP_001196;
CC Name=7; Synonyms=GDAB-TCS;
CC IsoId=Q60401-7; Sequence=VSP_001194, VSP_001199;
CC -!- TISSUE SPECIFICITY: All the isoforms are widely expressed. GPI and TCS
CC are the major forms, whereas SEC is minor and TCL is only present in
CC trace levels.
CC -!- MISCELLANEOUS: [Isoform 2]: Has a shorter cytoplasmic region.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Secreted. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Has a longer cytoplasmic region.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Has a longer cytoplasmic region.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Has a shorter cytoplasmic region.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; D55667; BAA09514.1; -; Genomic_DNA.
DR EMBL; D55667; BAA09515.1; -; Genomic_DNA.
DR EMBL; D55667; BAA09516.1; -; Genomic_DNA.
DR EMBL; D55667; BAA09517.1; -; Genomic_DNA.
DR EMBL; D55667; BAA09518.1; -; Genomic_DNA.
DR EMBL; D49416; BAA08396.1; -; mRNA.
DR EMBL; D49417; BAA08397.1; -; mRNA.
DR EMBL; D49418; BAA08398.1; -; mRNA.
DR EMBL; D49419; BAA08399.1; -; mRNA.
DR EMBL; D49420; BAA08400.1; -; mRNA.
DR EMBL; D49421; BAA08401.1; -; mRNA.
DR RefSeq; NP_001166351.1; NM_001172880.1. [Q60401-5]
DR RefSeq; NP_001166352.1; NM_001172881.1. [Q60401-6]
DR RefSeq; NP_001166353.1; NM_001172882.1.
DR RefSeq; NP_001166354.1; NM_001172883.1. [Q60401-3]
DR RefSeq; NP_001166355.1; NM_001172884.1.
DR RefSeq; NP_001166356.1; NM_001172885.1.
DR AlphaFoldDB; Q60401; -.
DR SMR; Q60401; -.
DR GeneID; 100379575; -.
DR KEGG; cpoc:100379575; -.
DR CTD; 1604; -.
DR InParanoid; Q60401; -.
DR OrthoDB; 1101732at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 Alternative splicing; Cell membrane; Complement pathway; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunity; Innate immunity; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..507
FT /note="Complement decay-accelerating factor"
FT /id="PRO_0000005997"
FT DOMAIN 32..94
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 95..159
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 160..221
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 222..284
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 281..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 64..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 96..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 127..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 162..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 189..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 224..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 252..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 302..334
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001193"
FT VAR_SEQ 335..366
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_001194"
FT VAR_SEQ 399..424
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001195"
FT VAR_SEQ 425..458
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_001196"
FT VAR_SEQ 459..507
FT /note="THVYKVDSFACGASNHWLADIAKEDLRRDFSNAQNISSLLQVLGAAQTQ ->
FT ANMRHMRTKNPMLYVIT (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_001199"
FT VAR_SEQ 459..507
FT /note="THVYKVDSFACGASNHWLADIAKEDLRRDFSNAQNISSLLQVLGAAQTQ ->
FT GHMCIKLTVLLVVLVIIG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001197"
FT VAR_SEQ 459..507
FT /note="THVYKVDSFACGASNHWLADIAKEDLRRDFSNAQNISSLLQVLGAAQTQ ->
FT DTCV (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001198"
FT LIPID Q60401-3:358
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000305|PubMed:7545710"
SQ SEQUENCE 507 AA; 55264 MW; D25BBB7749425210 CRC64;
MKRGRPAALR CLLLLRAPAL LLLLRAAAVQ GDCGPLPVVP RAHPASASAG STSFPENTTV
LYTCDQGFVK IPGKPDAVVC ISSRWTDIEE FCNRSCEVPP RLPYAILKSA YISKNYFPVD
TVVEYECRPG YRKKYPIQSG KITCRDDLTW STPAEFCEKK QCPNPGELVN GNINVTTDLL
LGSQIFFSCD PGYRLTGEAS AFCMIKGNAV GWSSSLPTCI KIICPEPPQI ENGRIVNEED
TYEYRHVVTY ECNKGFVLTG KSHISCIVRD DVGEWSDPPP TCRVKSPPVI PPQKPTTTSA
PGTTTTLPTQ KPTTVNTAGP EVPTTQRSTT VNVPGTKVPT TQRSTTVNVP GTEVPTTWKS
TTVNVPAAGN RPDTRTTIKS TTASEEKDLA SGYRTFLYGV GVGVPVIVCS LGLGVYWWIH
RTSGQYETYE NKESNVICHN LNESDATSEI TSSDKLKKTH VYKVDSFACG ASNHWLADIA
KEDLRRDFSN AQNISSLLQV LGAAQTQ
