ID DAF_HUMAN STANDARD; PRT; 381 AA. AC P08174; P09679; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE COMPLEMENT DECAY-ACCELERATING FACTOR PRECURSOR (CD55). GN DAF OR CD55. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87115845. RA CARAS I.W., DAVITZ M.A., RHEE L., WEDDELL G., MARTIN D.W. JR., RA NUSSENZWEIG V.; RL NATURE 325:545-549(1987). RN [2] RP SEQUENCE OF 6-381 FROM N.A. (DAF-2 FORM). RX MEDLINE; 87175602. RA MEDOF M.E., LUBLIN D.M., HOLERS V.M., AYERS D.J., GETTY R.R., RA LEYKAM J.F., ATKINSON J.P., TYKOCINSKI M.L.; RL PROC. NATL. ACAD. SCI. U.S.A. 84:2007-2011(1987). RN [3] RP SEQUENCE OF 1-100 FROM N.A. RX MEDLINE; 91271256. RA EWULONU U.K., RAVI L., MEDOF M.E.; RL PROC. NATL. ACAD. SCI. U.S.A. 88:4675-4679(1991). RN [4] RP SEQUENCE OF 35-46. RC TISSUE=URINE; RX MEDLINE; 91291869. RA NAKANO Y., SUGITA Y., ISHIKAWA Y., CHOI N.-H., TOBE T., TOMITA M.; RL BIOCHIM. BIOPHYS. ACTA 1074:326-330(1991). RN [5] RP GPI-ANCHOR. RX MEDLINE; 91093238. RA MORAN P., RAAB H., KOHR W.J., CARAS I.W.; RL J. BIOL. CHEM. 266:1250-1257(1991). RN [6] RP DISULFIDE BONDS IN SUSHI DOMAINS. RX MEDLINE; 92305034. RA NAKANO Y., SUMIDA K., KIKUTA N., MIURA N.-H., TOBE T., TOMITA M.; RL BIOCHIM. BIOPHYS. ACTA 1116:235-240(1992). RN [7] RP FUNCTION AS A ECHOVIRUS RECEPTOR. RX MEDLINE; 95045399. RA WARD T., PIPKIN P.A., CLARKSON N.A., STONE D.M., MINOR P.D., RA ALMOND J.W.; RL EMBO J. 13:5070-5074(1994). RN [8] RP VARIANT BLOOD GROUP DR(A-). RX MEDLINE; 94325573. RA LUBLIN D.M., MALLINSON G., POOLE J., REID M.E., THOMPSON E.S., RA FERDMAN B.R., TELEN M.J., ANSTEE D.J., TANNER M.J.A.; RL BLOOD 84:1276-1282(1994). CC -!- FUNCTION: THIS PROTEIN RECOGNIZES C4B AND C3B FRAGMENTS THAT CC CONDENSE WITH CELL-SURFACE HYDROXYL OR AMINO GROUPS WHEN NASCENT CC C4B AND C3B ARE LOCALLY GENERATED DURING C4 AND C3 ACTIVATION. CC INTERACTION OF DAF WITH CELL-ASSOCIATED C4B AND C3B POLYPEPTIDES CC INTERFERES WITH THEIR ABILITY TO CATALYZE THE CONVERSION OF C2 AND CC FACTOR B TO ENZYMATICALLY ACTIVE C2A AND BB AND THEREBY PREVENTS CC THE FORMATION OF C4B2A AND C3BBB, THE AMPLIFICATION CONVERTASES OF CC THE COMPLEMENT CASCADE. CC -!- FUNCTION: ALSO ACTS AS THE RECEPTOR FOR ECHOVIRUS 7 AND RELATED CC VIRUSES (ECHOVIRUSES 13, 21, 29 AND 33). CC -!- SUBUNIT: MONOMER (MAJOR FORM) AND NON-DISULFIDE-LINKED, COVALENT CC HOMODIMER (MINOR FORM). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: EXPRESSED ON THE PLASMA MEMBRANES OF ALL CELL CC TYPES THAT ARE IN INTIMATE CONTACT WITH PLASMA COMPLEMENT CC PROTEINS. IT IS ALSO FOUND ON THE SURFACES OF EPITHELIAL CELLS CC LINING EXTRACELLULAR COMPARTMENTS, AND VARIANTS OF THE MOLECULE CC ARE PRESENT IN BODY FLUIDS AND IN EXTRACELLULAR MATRIX. CC -!- DOMAIN: THE FIRST SUSHI DOMAIN (SCR1) IS NOT NECESSARY FOR CC FUNCTION. SCR2 AND SCR4 PROVIDE THE PROPER CONFORMATION FOR THE CC ACTIVE SITE ON SCR3 (BY SIMILARITY). CC -!- PTM: THE SER/THR-RICH DOMAIN IS HEAVILY O-GLYCOSYLATED. CC -!- POLYMORPHISM: DAF IS RESPONSIBLE FOR THE CROMER BLOOD GROUP CC SYSTEM. IT CONSISTS OF AT LEAST SEVEN HIGH-INCIDENCE (CR(A), CC TC(A), DR(A), ES(A), WES(B), UMC, AND IFC) AND LOW-INCIDENCE CC (TC(B), TC(C), AND WES(A)) ANTIGENS THAT RESIDE ON DAF. IN THE CC CROMER PHENOTYPES DR(A-) AND INAB THERE IS REDUCED OR ABSENT CC EXPRESSION OF DAF, RESPECTIVELY. IN THE CASE OF THE DR(A-) CC PHENOTYPE, A SINGLE NUCLEOTIDE SUBSTITUTION WITHIN EXON 5 ACCOUNTS CC FOR TWO CHANGES: A SIMPLE AMINO ACID SUBSTITUTION THAT IS THE CC BASIS OF THE ANTIGENIC VARIATION, AND AN ALTERNATIVE SPLICING CC EVENT THAT UNDERLIES THE DECREASED EXPRESSION OF DAF IN THIS CC PHENOTYPE. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS OF DAF (DAF-2, SHOWN HERE, AND CC DAF-1) ARE PRODUCED BY ALTERNATIVE SPLICING OF THE SAME GENE. CC -!- SIMILARITY: CONTAINS 4 SUSHI (SCR) REPEATS. CC -!- SIMILARITY: BELONGS TO THE RECEPTORS OF COMPLEMENT ACTIVATION CC (RCA) FAMILY. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CD55 entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd55.htm". DR EMBL; M31516; G181468; -. DR EMBL; M30142; G181465; -. DR EMBL; M15799; G181463; -. DR EMBL; M64653; G181476; -. DR EMBL; M64356; G181476; JOINED. DR EMBL; S72858; G639600; -. DR PIR; B26359; B26359. DR PIR; A26359; A26359. DR PIR; S16187; S16187. DR PIR; A39101; A39101. DR PIR; S23138; S23138. DR HSSP; P08603; 1HFI. DR MIM; 125240; -. KW COMPLEMENT PATHWAY; PLASMA; GLYCOPROTEIN; MEMBRANE; REPEAT; KW ALTERNATIVE SPLICING; GPI-ANCHOR; SIGNAL; SUSHI; POLYMORPHISM; KW BLOOD GROUP ANTIGEN. FT SIGNAL 1 34 FT CHAIN 35 353 COMPLEMENT DECAY-ACCELERATING FACTOR. FT PROPEP 354 381 REMOVED IN MATURE FORM. FT DOMAIN 35 284 4 X SUSHI (SCR) REPEATS. FT REPEAT 35 95 SUSHI 1. FT REPEAT 97 159 SUSHI 2. FT REPEAT 162 221 SUSHI 3. FT REPEAT 224 284 SUSHI 4. FT DOMAIN 287 356 SER/THR-RICH. FT DISULFID 36 81 FT DISULFID 65 94 FT DISULFID 98 145 FT DISULFID 129 158 FT DISULFID 163 204 FT DISULFID 190 220 FT DISULFID 225 267 FT DISULFID 253 283 FT CARBOHYD 95 95 POTENTIAL. FT LIPID 353 353 GPI-ANCHOR. FT VARIANT 52 52 R -> L (IN TC(B) ANTIGEN). FT VARIANT 52 52 R -> P (IN TC(C) ANTIGEN). FT VARIANT 82 82 L -> R (IN WES(A) ANTIGEN). FT VARIANT 199 199 S -> L (IN DR(A-) ANTIGEN). FT VARIANT 227 227 A -> P (IN CR(A-) ANTIGEN). FT VARSPLIC 362 381 HTCFTLTGLLGTLVTMGLLT -> SRPVTQAGMRWCDRSSL FT QSRTPGFKRSFHFSLPSSWYYRAHVFHVDRFAWDASNHGLA FT DLAKEELRRKYTQVYRLFLVS (IN DAF-1). FT CONFLICT 80 80 T -> I (IN REF. 1). FT CONFLICT 85 85 S -> M (IN REF. 2). SQ SEQUENCE 381 AA; 41388 MW; 114271A8 CRC32; MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE GRTSFPEDTV ITYKCEESFV KIPGEKDSVT CLKGSQWSDI EEFCNRSCEV PTRLNSASLK QPYITQNYFP VGTVVEYECR PGYRREPSLS PKLTCLQNLK WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI LFGATISFSC NTGYKLFGST SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER DHYGYRQSVT YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG TTSGTTRLLS GHTCFTLTGL LGTLVTMGLL T //