ID DAF_HUMAN Reviewed; 381 AA. AC P08174; B1AP14; D3DT83; D3DT84; E7ER69; P09679; P78361; Q14UF2; Q14UF3; AC Q14UF4; Q14UF5; Q14UF6; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 4. DT 27-MAR-2024, entry version 244. DE RecName: Full=Complement decay-accelerating factor; DE AltName: CD_antigen=CD55; DE Flags: Precursor; GN Name=CD55; Synonyms=CR, DAF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=2433596; DOI=10.1038/325545a0; RA Caras I.W., Davitz M.A., Rhee L., Weddell G., Martin D.W. Jr., RA Nussenzweig V.; RT "Cloning of decay-accelerating factor suggests novel use of splicing to RT generate two proteins."; RL Nature 325:545-549(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND SUBCELLULAR RP LOCATION (ISOFORMS 3; 4; 5; 6 AND 7). RC TISSUE=Lung; RX PubMed=16503113; DOI=10.1016/j.ygeno.2006.01.006; RA Osuka F., Endo Y., Higuchi M., Suzuki H., Shio Y., Fujiu K., Kanno R., RA Oishi A., Terashima M., Fujita T., Gotoh M.; RT "Molecular cloning and characterization of novel splicing variants of human RT decay-accelerating factor."; RL Genomics 88:316-322(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-52. RG SeattleSNPs variation discovery resource; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100. RX PubMed=1711208; DOI=10.1073/pnas.88.11.4675; RA Ewulonu U.K., Ravi L., Medof M.E.; RT "Characterization of the decay-accelerating factor gene promoter region."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4675-4679(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-381 (ISOFORM 2). RX PubMed=2436222; DOI=10.1073/pnas.84.7.2007; RA Medof M.E., Lublin D.M., Holers V.M., Ayers D.J., Getty R.R., Leykam J.F., RA Atkinson J.P., Tykocinski M.L.; RT "Cloning and characterization of cDNAs encoding the complete sequence of RT decay-accelerating factor of human complement."; RL Proc. Natl. Acad. Sci. U.S.A. 84:2007-2011(1987). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-381 (ISOFORM 2). RC TISSUE=Hippocampus; RA Kumar V.B., Hyung C., Nakra R., Walters M., Sasser T., Bernardo A.; RT "Decay-acceleration factor (DAF; CD 55) in the brain of Alzheimer's disease RT patients."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 35-63. RX PubMed=2428813; DOI=10.1093/oxfordjournals.jbchem.a121686; RA Sugita Y., Negoro T., Matsuda T., Sakamoto T., Tomita M.; RT "Improved method for the isolation and preliminary characterization of RT human DAF (decay-accelerating factor)."; RL J. Biochem. 100:143-150(1986). RN [12] RP PROTEIN SEQUENCE OF 35-46. RC TISSUE=Urine; RX PubMed=1712233; DOI=10.1016/0304-4165(91)90171-c; RA Nakano Y., Sugita Y., Ishikawa Y., Choi N.-H., Tobe T., Tomita M.; RT "Isolation of two forms of decay-accelerating factor (DAF) from human RT urine."; RL Biochim. Biophys. Acta 1074:326-330(1991). RN [13] RP GPI-ANCHOR AT SER-353. RX PubMed=1824699; DOI=10.1016/s0021-9258(17)35308-5; RA Moran P., Raab H., Kohr W.J., Caras I.W.; RT "Glycophospholipid membrane anchor attachment. Molecular analysis of the RT cleavage/attachment site."; RL J. Biol. Chem. 266:1250-1257(1991). RN [14] RP DISULFIDE BONDS IN SUSHI DOMAINS. RX PubMed=1377029; DOI=10.1016/0304-4165(92)90016-n; RA Nakano Y., Sumida K., Kikuta N., Miura N.-H., Tobe T., Tomita M.; RT "Complete determination of disulfide bonds localized within the short RT consensus repeat units of decay accelerating factor (CD55 antigen)."; RL Biochim. Biophys. Acta 1116:235-240(1992). RN [15] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ECHOVIRUS CAPSID RP PROTEINS. RX PubMed=7525274; DOI=10.1002/j.1460-2075.1994.tb06836.x; RA Ward T., Pipkin P.A., Clarkson N.A., Stone D.M., Minor P.D., Almond J.W.; RT "Decay-accelerating factor CD55 is identified as the receptor for echovirus RT 7 using CELICS, a rapid immuno-focal cloning method."; RL EMBO J. 13:5070-5074(1994). RN [16] RP INTERACTION WITH HUMAN ECHOVIRUSES 6/7/11/12/20/21 CAPSID PROTEINS. RX PubMed=7517044; DOI=10.1073/pnas.91.13.6245; RA Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., Finberg R.W.; RT "Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored RT complement regulatory protein, is a receptor for several echoviruses."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994). RN [17] RP INTERACTION WITH COXSACKIEVIRUSES B1/B3/B5 CAPSID PROTEINS. RX PubMed=7538177; DOI=10.1128/jvi.69.6.3873-3877.1995; RA Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D.; RT "Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a RT receptor for cell attachment."; RL J. Virol. 69:3873-3877(1995). RN [18] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ENTEROVIRUS 70 RP CAPSID PROTEINS. RX PubMed=8764022; DOI=10.1128/jvi.70.8.5143-5152.1996; RA Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M., RA Dimock K.; RT "The HeLa cell receptor for enterovirus 70 is decay-accelerating factor RT (CD55)."; RL J. Virol. 70:5143-5152(1996). RN [19] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A21 RP CAPSID PROTEINS. RX PubMed=9151867; DOI=10.1128/jvi.71.6.4736-4743.1997; RA Shafren D.R., Dorahy D.J., Ingham R.A., Burns G.F., Barry R.D.; RT "Coxsackievirus A21 binds to decay-accelerating factor but requires RT intercellular adhesion molecule 1 for cell entry."; RL J. Virol. 71:4736-4743(1997). RN [20] RP INTERACTION WITH ADGRE5. RX PubMed=11297558; DOI=10.1074/jbc.m101770200; RA Lin H.-H., Stacey M., Saxby C., Knott V., Chaudhry Y., Evans D., Gordon S., RA McKnight A.J., Handford P., Lea S.; RT "Molecular analysis of the epidermal growth factor-like short consensus RT repeat domain-mediated protein-protein interactions: dissection of the RT CD97-CD55 complex."; RL J. Biol. Chem. 276:24160-24169(2001). RN [21] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ENTEROVIRUS D68 CAPSID RP PROTEINS. RX PubMed=12409401; DOI=10.1128/jcm.40.11.4218-4223.2002; RA Blomqvist S., Savolainen C., Raman L., Roivainen M., Hovi T.; RT "Human rhinovirus 87 and enterovirus 68 represent a unique serotype with RT rhinovirus and enterovirus features."; RL J. Clin. Microbiol. 40:4218-4223(2002). RN [22] RP INTERACTION WITH COXSACKIEVIRUS B3 CAPSID PROTEINS. RX PubMed=17804498; DOI=10.1128/jvi.00931-07; RA Hafenstein S., Bowman V.D., Chipman P.R., Bator Kelly C.M., Lin F., RA Medof M.E., Rossmann M.G.; RT "Interaction of decay-accelerating factor with coxsackievirus B3."; RL J. Virol. 81:12927-12935(2007). RN [23] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP GLYCOSYLATION. RX PubMed=26207632; DOI=10.1371/journal.pone.0133704; RA Mizuhashi K., Chaya T., Kanamoto T., Omori Y., Furukawa T.; RT "Obif, a transmembrane protein, is required for bone mineralization and RT spermatogenesis in mice."; RL PLoS ONE 10:E0133704-E0133704(2015). RN [26] RP INVOLVEMENT IN CHAPLE. RX PubMed=28657861; DOI=10.1056/nejmc1707173; RA Kurolap A., Eshach-Adiv O., Hershkovitz T., Paperna T., Mory A., RA Oz-Levi D., Zohar Y., Mandel H., Chezar J., Azoulay D., Peleg S., RA Half E.E., Yahalom V., Finkel L., Weissbrod O., Geiger D., Tabib A., RA Shaoul R., Magen D., Bonstein L., Mevorach D., Baris H.N.; RT "Loss of CD55 in eculizumab-responsive protein-losing enteropathy."; RL N. Engl. J. Med. 377:87-89(2017). RN [27] RP VARIANT BLOOD GROUP DR(A-) LEU-199. RX PubMed=7519480; 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.; RT "Molecular basis of reduced or absent expression of decay-accelerating RT factor in Cromer blood group phenotypes."; RL Blood 84:1276-1282(1994). RN [28] RP VARIANT BLOOD GROUP GUTI(-) HIS-240, AND POLYMORPHISM. RX PubMed=12675719; DOI=10.1046/j.1537-2995.2003.00319.x; RA Storry J.R., Sausais L., Hue-Roye K., Mudiwa F., Ferrer Z., Blajchman M.A., RA Lublin D.M., Ma B.W., Miquel J.F., Nervi F., Pereira J., Reid M.E.; RT "GUTI: a new antigen in the Cromer blood group system."; RL Transfusion 43:340-344(2003). RN [29] RP INVOLVEMENT IN BLOOD GROUP INAB. RX PubMed=1720702; RA Reid M.E., Mallinson G., Sim R.B., Poole J., Pausch V., Merry A.H., RA Liew Y.W., Tanner M.J.A.; RT "Biochemical studies on red blood cells from a patient with the Inab RT phenotype (decay-accelerating factor deficiency)."; RL Blood 78:3291-3297(1991). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 161-285. RX PubMed=12499389; DOI=10.1074/jbc.m212561200; RA Williams P., Chaudhry Y., Goodfellow I.G., Billington J., Powell R., RA Spiller O.B., Evans D.J., Lea S.; RT "Mapping CD55 function. The structure of two pathogen-binding domains at RT 1.7 A."; RL J. Biol. Chem. 278:10691-10696(2003). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-286. RX PubMed=14734808; DOI=10.1073/pnas.0307200101; RA Lukacik P., Roversi P., White J., Esser D., Smith G.P., Billington J., RA Williams P.A., Rudd P.M., Wormald M.R., Harvey D.J., Crispin M.D., RA Radcliffe C.M., Dwek R.A., Evans D.J., Morgan B.P., Smith R.A., Lea S.M.; RT "Complement regulation at the molecular level: the structure of decay- RT accelerating factor."; RL Proc. Natl. Acad. Sci. U.S.A. 101:1279-1284(2004). RN [32] RP STRUCTURE BY NMR OF 95-223. RX PubMed=12672958; DOI=10.1073/pnas.0730844100; RA Uhrinova S., Lin F., Ball G., Bromek K., Uhrin D., Medof M.E., Barlow P.N.; RT "Solution structure of a functionally active fragment of decay-accelerating RT factor."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4718-4723(2003). RN [33] RP VARIANT CHAPLE SER-267, CHARACTERIZATION OF VARIANT CHAPLE SER-267, AND RP FUNCTION. RX PubMed=28657829; DOI=10.1056/nejmoa1615887; RA Ozen A., Comrie W.A., Ardy R.C., Dominguez Conde C., Dalgic B., Beser O.F., RA Morawski A.R., Karakoc-Aydiner E., Tutar E., Baris S., Ozcay F., RA Serwas N.K., Zhang Y., Matthews H.F., Pittaluga S., Folio L.R., RA Unlusoy Aksu A., McElwee J.J., Krolo A., Kiykim A., Baris Z., Gulsan M., RA Ogulur I., Snapper S.B., Houwen R.H.J., Leavis H.L., Ertem D., Kain R., RA Sari S., Erkan T., Su H.C., Boztug K., Lenardo M.J.; RT "CD55 deficiency, early-onset protein-losing enteropathy, and thrombosis."; RL N. Engl. J. Med. 377:52-61(2017). 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 (PubMed:7525274). CC Inhibits complement activation by destabilizing and preventing the CC formation of C3 and C5 convertases, which prevents complement damage CC (PubMed:28657829). {ECO:0000269|PubMed:7525274, CC ECO:0000305|PubMed:28657829}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus CC A21, coxsackieviruses B1, B3 and B5. {ECO:0000269|PubMed:9151867}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Human CC enterovirus 70 and D68 (Probable). {ECO:0000269|PubMed:8764022}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Human CC echoviruses 6, 7, 11, 12, 20 and 21. {ECO:0000269|PubMed:7525274, CC ECO:0000305|PubMed:12409401}. CC -!- SUBUNIT: Monomer (major form) and non-disulfide-linked, covalent CC homodimer (minor form). Interacts with ADGRE5 (PubMed:11297558). CC {ECO:0000269|PubMed:11297558, ECO:0000269|PubMed:1377029, CC ECO:0000305|PubMed:12409401}. CC -!- SUBUNIT: (Microbial infection) Interacts with coxsackievirus A21, CC coxsackieviruses B1, B3 and B5 capsid proteins. CC {ECO:0000269|PubMed:9151867}. CC -!- SUBUNIT: (Microbial infection) Interacts with human enterovirus 70 and CC D68 capsid proteins (Probable). {ECO:0000269|PubMed:8764022}. CC -!- SUBUNIT: (Microbial infection) Interacts with human echoviruses 6, 7, CC 11, 12, 20 and 21 capsid proteins. {ECO:0000269|PubMed:7525274}. CC -!- INTERACTION: CC P08174; P48960: ADGRE5; NbExp=2; IntAct=EBI-1033846, EBI-1756009; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI- CC anchor. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted CC {ECO:0000269|PubMed:16503113}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted CC {ECO:0000269|PubMed:16503113}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted CC {ECO:0000269|PubMed:16503113}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane CC {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor CC {ECO:0000305|PubMed:16503113}. CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane CC {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor CC {ECO:0000305|PubMed:16503113}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=2; Synonyms=DAF-2; CC IsoId=P08174-1; Sequence=Displayed; CC Name=1; Synonyms=DAF-1; CC IsoId=P08174-2; Sequence=VSP_001200; CC Name=3; Synonyms=VDAF3; CC IsoId=P08174-3; Sequence=VSP_047636; CC Name=4; Synonyms=VDAF2; CC IsoId=P08174-4; Sequence=VSP_047637; CC Name=5; Synonyms=VDAF1; CC IsoId=P08174-5; Sequence=VSP_047638; CC Name=6; Synonyms=VDAF4; CC IsoId=P08174-6; Sequence=VSP_047635; CC Name=7; Synonyms=VDAF5; CC IsoId=P08174-7; Sequence=VSP_047634; CC -!- TISSUE SPECIFICITY: Expressed on the plasma membranes of all cell types CC that are in intimate contact with plasma complement proteins. It is CC also found on the surfaces of epithelial cells lining extracellular CC compartments, and variants of the molecule are present in body fluids CC and in extracellular matrix. 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 {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26207632}. CC -!- POLYMORPHISM: Responsible for the Cromer blood group system (CROM) CC [MIM:613793]. It consists of at least 8 high-incidence (Cr(a), Tc(a), CC Dr(a), Es(a), WES(b), UMC, IFC and GUTI) and three low-incidence CC (Tc(b), Tc(c) and WES(a)) antigens that reside on DAF. In the Cromer CC phenotypes Dr(a-) and Inab there is reduced or absent expression of CC DAF, respectively. In the case of the Dr(a-) phenotype, a single CC nucleotide substitution within exon 5 accounts for two changes: a CC simple amino acid substitution, Leu-199 that is the basis of the CC antigenic variation, and an alternative splicing event that underlies CC the decreased expression of DAF in this phenotype. The Inab phenotype CC is a very rare one in which the red blood cells lack all Cromer system CC antigens. The red blood cells of individuals with Inab phenotype have a CC deficiency of DAF, but these individuals are not known to have any CC associated hematologic or other abnormalities (PubMed:12675719). CC {ECO:0000269|PubMed:12675719}. CC -!- DISEASE: Complement hyperactivation, angiopathic thrombosis, and CC protein-losing enteropathy (CHAPLE) [MIM:226300]: An autosomal CC recessive disease characterized by abdominal pain and diarrhea, primary CC intestinal lymphangiectasia, edema due to hypoproteinemia, CC malabsorption, and less frequently, bowel inflammation, recurrent CC infections, and angiopathic thromboembolic disease. Patients' T CC lymphocytes show increased complement activation causing surface CC deposition of complement and the generation of soluble C5a. CC {ECO:0000269|PubMed:28657829, ECO:0000269|PubMed:28657861}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CHAPLE is caused by biallelic mutations in the CD55 gene. CC -!- MISCELLANEOUS: [Isoform 6]: Includes partial sequence of the intron 7. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Includes full sequence of the intron 7. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA) CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation CC database; CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=cromer"; CC -!- WEB RESOURCE: Name=CD55base; Note=CD55 mutation db; CC URL="http://structure.bmc.lu.se/idbase/CD55base/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Decay-accelerating factor entry; CC URL="https://en.wikipedia.org/wiki/Decay_accelerating_factor"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/daf/"; CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid CC structure; CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1z7z"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M31516; AAA52169.1; -; mRNA. DR EMBL; M30142; AAA52168.1; -; mRNA. DR EMBL; AB240566; BAE97422.1; -; mRNA. DR EMBL; AB240567; BAE97423.1; -; mRNA. DR EMBL; AB240568; BAE97424.1; -; mRNA. DR EMBL; AB240569; BAE97425.1; -; mRNA. DR EMBL; AB240570; BAE97426.1; -; mRNA. DR EMBL; BT007159; AAP35823.1; -; mRNA. DR EMBL; AY851161; AAW29942.1; -; Genomic_DNA. DR EMBL; AL391597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL596218; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93485.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93487.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93488.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93491.1; -; Genomic_DNA. DR EMBL; BC001288; AAH01288.1; -; mRNA. DR EMBL; M64653; AAA52170.1; -; Genomic_DNA. DR EMBL; M64356; AAA52170.1; JOINED; Genomic_DNA. DR EMBL; M15799; AAA52167.1; -; mRNA. DR EMBL; U88576; AAB48622.1; -; mRNA. DR EMBL; S72858; AAC60633.1; -; Genomic_DNA. DR CCDS; CCDS31006.1; -. [P08174-1] DR CCDS; CCDS44307.1; -. [P08174-2] DR CCDS; CCDS86046.1; -. [P08174-5] DR CCDS; CCDS86047.1; -. [P08174-3] DR PIR; A26359; A26359. DR PIR; B26359; B26359. DR RefSeq; NP_000565.1; NM_000574.4. [P08174-1] DR RefSeq; NP_001108224.1; NM_001114752.2. [P08174-2] DR RefSeq; NP_001287832.1; NM_001300903.1. [P08174-5] DR RefSeq; NP_001287833.1; NM_001300904.1. [P08174-3] DR PDB; 1H03; X-ray; 1.70 A; P/Q=161-285. DR PDB; 1H04; X-ray; 2.00 A; P=161-285. DR PDB; 1H2P; X-ray; 2.80 A; P=161-285. DR PDB; 1H2Q; X-ray; 3.00 A; P=161-285. DR PDB; 1M11; EM; 16.00 A; R=35-277. DR PDB; 1NWV; NMR; -; A=96-222. DR PDB; 1OJV; X-ray; 2.30 A; A/B=35-285. DR PDB; 1OJW; X-ray; 2.30 A; A/B=35-285. DR PDB; 1OJY; X-ray; 2.60 A; A/B/C/D=35-285. DR PDB; 1OK1; X-ray; 2.60 A; A/B=35-285. DR PDB; 1OK2; X-ray; 2.50 A; A/B=35-285. DR PDB; 1OK3; X-ray; 2.20 A; A/B=35-285. DR PDB; 1OK9; X-ray; 3.00 A; A/B=35-285. DR PDB; 1UOT; X-ray; 3.00 A; P=161-285. DR PDB; 1UPN; EM; 16.00 A; E=157-285. DR PDB; 2C8I; EM; 14.00 A; E=35-285. DR PDB; 2QZD; EM; -; A=222-285. DR PDB; 2QZF; EM; -; A=35-94. DR PDB; 2QZH; EM; 14.00 A; A=96-222. DR PDB; 3IYP; EM; -; F=1-381. DR PDB; 3J24; EM; 9.00 A; B=35-285. DR PDB; 5FOA; X-ray; 4.19 A; E/F=97-285. DR PDB; 6ILJ; EM; 3.60 A; E=94-285. DR PDB; 6ILK; EM; 3.00 A; E=94-285. DR PDB; 6LA5; EM; 2.86 A; E=161-285. DR PDB; 7C9W; EM; 3.60 A; E=94-285. DR PDB; 7DO4; X-ray; 3.20 A; B=35-284. DR PDB; 7VY5; EM; 3.15 A; E=98-220. DR PDB; 7VY6; EM; 3.02 A; E=35-285. DR PDB; 8B8R; EM; 3.10 A; E=28-285. DR PDBsum; 1H03; -. DR PDBsum; 1H04; -. DR PDBsum; 1H2P; -. DR PDBsum; 1H2Q; -. DR PDBsum; 1M11; -. DR PDBsum; 1NWV; -. DR PDBsum; 1OJV; -. DR PDBsum; 1OJW; -. DR PDBsum; 1OJY; -. DR PDBsum; 1OK1; -. DR PDBsum; 1OK2; -. DR PDBsum; 1OK3; -. DR PDBsum; 1OK9; -. DR PDBsum; 1UOT; -. DR PDBsum; 1UPN; -. DR PDBsum; 2C8I; -. DR PDBsum; 2QZD; -. DR PDBsum; 2QZF; -. DR PDBsum; 2QZH; -. DR PDBsum; 3IYP; -. DR PDBsum; 3J24; -. DR PDBsum; 5FOA; -. DR PDBsum; 6ILJ; -. DR PDBsum; 6ILK; -. DR PDBsum; 6LA5; -. DR PDBsum; 7C9W; -. DR PDBsum; 7DO4; -. DR PDBsum; 7VY5; -. DR PDBsum; 7VY6; -. DR PDBsum; 8B8R; -. DR AlphaFoldDB; P08174; -. DR BMRB; P08174; -. DR EMDB; EMD-0856; -. DR EMDB; EMD-1412; -. DR EMDB; EMD-15920; -. DR EMDB; EMD-15930; -. DR EMDB; EMD-30319; -. DR EMDB; EMD-32194; -. DR EMDB; EMD-32195; -. DR EMDB; EMD-5179; -. DR EMDB; EMD-5475; -. DR EMDB; EMD-9684; -. DR EMDB; EMD-9685; -. DR SMR; P08174; -. DR BioGRID; 107974; 55. DR IntAct; P08174; 15. DR MINT; P08174; -. DR STRING; 9606.ENSP00000356030; -. DR BindingDB; P08174; -. DR ChEMBL; CHEMBL4879428; -. DR DrugBank; DB00446; Chloramphenicol. DR GlyConnect; 1151; 6 N-Linked glycans (1 site). DR GlyCosmos; P08174; 1 site, 6 glycans. DR GlyGen; P08174; 8 sites, 6 N-linked glycans (1 site), 2 O-linked glycans (7 sites). DR iPTMnet; P08174; -. DR PhosphoSitePlus; P08174; -. DR SwissPalm; P08174; -. DR BioMuta; CD55; -. DR DMDM; 60416353; -. DR EPD; P08174; -. DR jPOST; P08174; -. DR MassIVE; P08174; -. DR MaxQB; P08174; -. DR PaxDb; 9606-ENSP00000356030; -. DR PeptideAtlas; P08174; -. DR ProteomicsDB; 52078; -. [P08174-1] DR ProteomicsDB; 52079; -. [P08174-2] DR ProteomicsDB; 60351; -. DR ProteomicsDB; 60352; -. DR ProteomicsDB; 60353; -. DR Pumba; P08174; -. DR ABCD; P08174; 5 sequenced antibodies. DR Antibodypedia; 710; 1920 antibodies from 49 providers. DR DNASU; 1604; -. DR Ensembl; ENST00000314754.12; ENSP00000316333.8; ENSG00000196352.18. [P08174-2] DR Ensembl; ENST00000367064.9; ENSP00000356031.4; ENSG00000196352.18. [P08174-1] DR Ensembl; ENST00000644836.1; ENSP00000495518.1; ENSG00000196352.18. [P08174-3] DR Ensembl; ENST00000645323.1; ENSP00000496251.1; ENSG00000196352.18. [P08174-5] DR GeneID; 1604; -. DR KEGG; hsa:1604; -. DR MANE-Select; ENST00000367064.9; ENSP00000356031.4; NM_000574.5; NP_000565.1. DR UCSC; uc001hfq.5; human. [P08174-1] DR AGR; HGNC:2665; -. DR CTD; 1604; -. DR DisGeNET; 1604; -. DR GeneCards; CD55; -. DR HGNC; HGNC:2665; CD55. DR HPA; ENSG00000196352; Low tissue specificity. DR MalaCards; CD55; -. DR MIM; 125240; gene. DR MIM; 226300; phenotype. DR MIM; 613793; phenotype. DR neXtProt; NX_P08174; -. DR NIAGADS; ENSG00000196352; -. DR OpenTargets; ENSG00000196352; -. DR Orphanet; 566175; Complement hyperactivation-angiopathic thrombosis-protein-losing enteropathy syndrome. DR PharmGKB; PA27137; -. DR VEuPathDB; HostDB:ENSG00000196352; -. DR eggNOG; ENOG502SKPE; Eukaryota. DR GeneTree; ENSGT00940000162307; -. DR InParanoid; P08174; -. DR OMA; PTCTEIF; -. DR OrthoDB; 2901311at2759; -. DR PhylomeDB; P08174; -. DR TreeFam; TF334137; -. DR PathwayCommons; P08174; -. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SignaLink; P08174; -. DR SIGNOR; P08174; -. DR BioGRID-ORCS; 1604; 8 hits in 1169 CRISPR screens. DR ChiTaRS; CD55; human. DR EvolutionaryTrace; P08174; -. DR GeneWiki; Decay-accelerating_factor; -. DR GenomeRNAi; 1604; -. DR Pharos; P08174; Tbio. DR PRO; PR:P08174; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P08174; Protein. DR Bgee; ENSG00000196352; Expressed in parotid gland and 210 other cell types or tissues. DR ExpressionAtlas; P08174; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB. DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:UniProtKB. DR GO; GO:0030449; P:regulation of complement activation; IDA:MGI. DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IDA:MGI. DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0045730; P:respiratory burst; NAS:UniProtKB. 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; P08174; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood group antigen; Cell membrane; KW Complement pathway; Direct protein sequencing; Disease variant; KW Disulfide bond; Glycoprotein; GPI-anchor; KW Host cell receptor for virus entry; Host-virus interaction; Immunity; KW Innate immunity; Lipoprotein; Membrane; Receptor; Reference proteome; KW Repeat; Secreted; Signal; Sushi. FT SIGNAL 1..34 FT /evidence="ECO:0000269|PubMed:1712233, FT ECO:0000269|PubMed:2428813" FT CHAIN 35..353 FT /note="Complement decay-accelerating factor" FT /id="PRO_0000006000" FT PROPEP 354..381 FT /note="Removed in mature form" FT /id="PRO_0000006001" FT DOMAIN 35..96 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 96..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..285 FT /note="Sushi 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT REGION 277..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 290..354 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 353 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000269|PubMed:1824699" FT CARBOHYD 95 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 36..81 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 65..94 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 98..145 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 129..158 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 163..204 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 190..220 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 225..267 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT DISULFID 253..283 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:1377029" FT VAR_SEQ 326 FT /note="Q -> QGTETPSVLQKHTTENVSATRTPPTPQKPTTVNVPATIVTPTPQKPT FT TINVPATGVSSTPQRHTIVNVSATGTLPTLQKPTRANDSATKSPAAAQTSFISKTLSTK FT TPSAAQNPMMTNASATQATLTAQKFTTAKVAFTQSPSAARKSTNVHSPVTNGLKSTQRF FT PSAHIT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16503113" FT /id="VSP_047634" FT VAR_SEQ 327 FT /note="A -> GTETPSVLQKHTTENVSATRTPPTPQKPTTVNVPATIVTPTPQKPTT FT INVPATGVSSTPQRHTIVNVSATGTLPTLQKPTRANDSATKSPAAAQTSFISKTLSTKT FT PSAAQNPMMTNASATQATLTAQKFTTAKVAFTQSPSAAP (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16503113" FT /id="VSP_047635" FT VAR_SEQ 361..381 FT /note="GHTCFTLTGLLGTLVTMGLLT -> ALQVRPFEVSGSSHISSKKMMCIL FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16503113" FT /id="VSP_047636" FT VAR_SEQ 361..381 FT /note="GHTCFTLTGLLGTLVTMGLLT -> VLFM (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16503113" FT /id="VSP_047637" FT VAR_SEQ 361..381 FT /note="GHTCFTLTGLLGTLVTMGLLT -> ETVFHRVIQDGLDLLASRSACLGLPKC FT WDYRREPPHLARAHVFHVDRFAWDASNHGLADLAKEELRRKYTQVYRLFLVS (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:16503113" FT /id="VSP_047638" FT VAR_SEQ 362..381 FT /note="HTCFTLTGLLGTLVTMGLLT -> SRPVTQAGMRWCDRSSLQSRTPGFKRSF FT HFSLPSSWYYRAHVFHVDRFAWDASNHGLADLAKEELRRKYTQVYRLFLVS (in FT isoform 1)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:2433596" FT /id="VSP_001200" FT VARIANT 52 FT /note="R -> L (in Tc(b) antigen; dbSNP:rs28371588)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_001997" FT VARIANT 52 FT /note="R -> P (in Tc(c) antigen; dbSNP:rs28371588)" FT /id="VAR_001998" FT VARIANT 82 FT /note="L -> R (in WES(a) antigen; dbSNP:rs147474393)" FT /id="VAR_001999" FT VARIANT 199 FT /note="S -> L (in Dr(a-) antigen; dbSNP:rs1135402914)" FT /evidence="ECO:0000269|PubMed:7519480" FT /id="VAR_002000" FT VARIANT 227 FT /note="A -> P (in Cr(a-) antigen; dbSNP:rs60822373)" FT /id="VAR_002001" FT VARIANT 240 FT /note="R -> H (in GUTI(-) antigen; dbSNP:rs199705465)" FT /evidence="ECO:0000269|PubMed:12675719" FT /id="VAR_015884" FT VARIANT 267 FT /note="C -> S (in CHAPLE; increased complement activation; FT dbSNP:rs1135402917)" FT /evidence="ECO:0000269|PubMed:28657829" FT /id="VAR_079373" FT CONFLICT 80 FT /note="I -> T (in Ref. 8; AAA52170 and 9; AAA52167)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="S -> M (in Ref. 9; AAA52167)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="S -> T (in Ref. 10; AAB48622)" FT /evidence="ECO:0000305" FT CONFLICT 297 FT /note="Q -> H (in Ref. 10; AAB48622)" FT /evidence="ECO:0000305" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1OJW" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:1OK3" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:1OJW" FT STRAND 105..109 FT /evidence="ECO:0007829|PDB:1OK3" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:7VY6" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:1OK9" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:1OK3" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:1H03" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:1UOT" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 200..207 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:1H2P" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 263..270 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 273..278 FT /evidence="ECO:0007829|PDB:1H03" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:1H03" SQ SEQUENCE 381 AA; 41400 MW; C1CBE5300F60C176 CRC64; MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE GRTSFPEDTV ITYKCEESFV KIPGEKDSVI 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 //