DAF_HUMAN
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 03-AUG-2022, entry version 235.
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";
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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 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 AlphaFoldDB; P08174; -.
DR BMRB; P08174; -.
DR SMR; P08174; -.
DR BioGRID; 107974; 49.
DR IntAct; P08174; 13.
DR STRING; 9606.ENSP00000356030; -.
DR DrugBank; DB00446; Chloramphenicol.
DR GlyConnect; 1151; 6 N-Linked glycans (1 site).
DR GlyGen; P08174; 2 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site).
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; P08174; -.
DR PeptideAtlas; P08174; -.
DR PRIDE; P08174; -.
DR ProteomicsDB; 52078; -. [P08174-1]
DR ProteomicsDB; 52079; -. [P08174-2]
DR ProteomicsDB; 60351; -.
DR ProteomicsDB; 60352; -.
DR ProteomicsDB; 60353; -.
DR ABCD; P08174; 5 sequenced antibodies.
DR Antibodypedia; 710; 1768 antibodies from 49 providers.
DR DNASU; 1604; -.
DR Ensembl; ENST00000314754.12; ENSP00000316333.8; ENSG00000196352.17. [P08174-2]
DR Ensembl; ENST00000367064.9; ENSP00000356031.4; ENSG00000196352.17. [P08174-1]
DR Ensembl; ENST00000644836.1; ENSP00000495518.1; ENSG00000196352.17. [P08174-3]
DR Ensembl; ENST00000645323.1; ENSP00000496251.1; ENSG00000196352.17. [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 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; DTREDQK; -.
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; 6 hits in 1084 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 208 other tissues.
DR ExpressionAtlas; P08174; baseline and differential.
DR Genevisible; P08174; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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: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; 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 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 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
