[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). DOI=10.1038/325545a0; PubMed=2433596 [NCBI, ExPASy, EBI, Israel, Japan] Caras I.W., Davitz M.A., Rhee L., Weddell G., Martin D.W. Jr., Nussenzweig V.; "Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteins."; Nature 325:545-549(1987).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-52. SeattleSNPs variation discovery resource; Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Cervix; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100. DOI=10.1073/pnas.88.11.4675; PubMed=1711208 [NCBI, ExPASy, EBI, Israel, Japan] Ewulonu U.K., Ravi L., Medof M.E.; "Characterization of the decay-accelerating factor gene promoter region."; Proc. Natl. Acad. Sci. U.S.A. 88:4675-4679(1991).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 6-381 (ISOFORM 2). DOI=10.1073/pnas.84.7.2007; PubMed=2436222 [NCBI, ExPASy, EBI, Israel, Japan] Medof M.E., Lublin D.M., Holers V.M., Ayers D.J., Getty R.R., Leykam J.F., Atkinson J.P., Tykocinski M.L.; "Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement."; Proc. Natl. Acad. Sci. U.S.A. 84:2007-2011(1987).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 35-381 (ISOFORM 2). TISSUE=Hippocampus; Kumar V.B., Hyung C., Nakra R., Walters M., Sasser T., Bernardo A.; "Decay-acceleration factor (DAF; CD 55) in the brain of Alzheimer's disease patients."; Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[8]	PROTEIN SEQUENCE OF 35-63. PubMed=2428813 [NCBI, ExPASy, EBI, Israel, Japan] Sugita Y., Negoro T., Matsuda T., Sakamoto T., Tomita M.; "Improved method for the isolation and preliminary characterization of human DAF (decay-accelerating factor)."; J. Biochem. 100:143-150(1986).
[9]	PROTEIN SEQUENCE OF 35-46. TISSUE=Urine; DOI=10.1016/0304-4165(91)90171-C; PubMed=1712233 [NCBI, ExPASy, EBI, Israel, Japan] Nakano Y., Sugita Y., Ishikawa Y., Choi N.-H., Tobe T., Tomita M.; "Isolation of two forms of decay-accelerating factor (DAF) from human urine."; Biochim. Biophys. Acta 1074:326-330(1991).
[10]	GPI-ANCHOR AT SER-353. PubMed=1824699 [NCBI, ExPASy, EBI, Israel, Japan] Moran P., Raab H., Kohr W.J., Caras I.W.; "Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site."; J. Biol. Chem. 266:1250-1257(1991).
[11]	DISULFIDE BONDS IN SUSHI DOMAINS. DOI=10.1016/0304-4165(92)90016-N; PubMed=1377029 [NCBI, ExPASy, EBI, Israel, Japan] Nakano Y., Sumida K., Kikuta N., Miura N.-H., Tobe T., Tomita M.; "Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen)."; Biochim. Biophys. Acta 1116:235-240(1992).
[12]	FUNCTION AS A ECHOVIRUS RECEPTOR. PubMed=7525274 [NCBI, ExPASy, EBI, Israel, Japan] Ward T., Pipkin P.A., Clarkson N.A., Stone D.M., Minor P.D., Almond J.W.; "Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method."; EMBO J. 13:5070-5074(1994).
[13]	INTERACTION WITH HUMAN ECHOVIRUS 6, HUMAN ECHOVIRUS 7, HUMAN ECHOVIRUS 11, HUMAN ECHOVIRUS 12, HUMAN ECHOVIRUS 20, AND HUMAN ECHOVIRUS 21 CAPSID PROTEINS. DOI=10.1073/pnas.91.13.6245; PubMed=7517044 [NCBI, ExPASy, EBI, Israel, Japan] Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., Finberg R.W.; "Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses."; Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994).
[14]	INTERACTION WITH COXSACKIEVIRUS B1, B3, AND B5 CAPSID PROTEINS. PubMed=7538177 [NCBI, ExPASy, EBI, Israel, Japan] Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D.; "Coxsackieviruses B1, B3, and B5 use decay aCCelerating factor as a receptor for cell attachment."; J. Virol. 69:3873-3877(1995).
[15]	INTERACTION WITH HUMAN ENTEROVIRUS 70 CAPSID PROTEINS. PubMed=8764022 [NCBI, ExPASy, EBI, Israel, Japan] Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M., Dimock K.; "The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55)."; J. Virol. 70:5143-5152(1996).
[16]	INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS. PubMed=9151867 [NCBI, ExPASy, EBI, Israel, Japan] Shafren D.R., Dorahy D.J., Ingham R.A., Burns G.F., Barry R.D.; "Coxsackievirus A21 binds to decay-aCCelerating factor but requires intercellular adhesion molecule 1 for cell entry."; J. Virol. 71:4736-4743(1997).
[17]	GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1074/mcp.M300079-MCP200; PubMed=14517339 [NCBI, ExPASy, EBI, Israel, Japan] Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.; "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."; Mol. Cell. Proteomics 2:1261-1270(2003).
[18]	GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1021/pr050419u; PubMed=16602701 [NCBI, ExPASy, EBI, Israel, Japan] Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.; "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."; J. Proteome Res. 5:935-943(2006).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[20]	INTERACTION WITH COXSACKIEVIRUS B3 CAPSID PROTEINS. DOI=10.1128/JVI.00931-07; PubMed=17804498 [NCBI, ExPASy, EBI, Israel, Japan] Hafenstein S., Bowman V.D., Chipman P.R., Bator Kelly C.M., Lin F., Medof M.E., Rossmann M.G.; "Interaction of decay-aCCelerating factor with coxsackievirus B3."; J. Virol. 81:12927-12935(2007).
[21]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[22]	VARIANT BLOOD GROUP DR(A-) LEU-199. PubMed=7519480 [NCBI, ExPASy, EBI, Israel, Japan] Lublin D.M., Mallinson G., Poole J., Reid M.E., Thompson E.S., Ferdman B.R., Telen M.J., Anstee D.J., Tanner M.J.A.; "Molecular basis of reduced or absent expression of decay-accelerating factor in Cromer blood group phenotypes."; Blood 84:1276-1282(1994).
[23]	VARIANT BLOOD GROUP GUTI(-) HIS-240. DOI=10.1046/j.1537-2995.2003.00319.x; PubMed=12675719 [NCBI, ExPASy, EBI, Israel, Japan] Storry J.R., Sausais L., Hue-Roye K., Mudiwa F., Ferrer Z., Blajchman M.A., Lublin D.M., Ma B.W., Miquel J.F., Nervi F., Pereira J., Reid M.E.; "GUTI: a new antigen in the Cromer blood group system."; Transfusion 43:340-344(2003).
[24]	INVOLVEMENT IN BLOOD GROUP INAB. PubMed=1720702 [NCBI, ExPASy, EBI, Israel, Japan] Reid M.E., Mallinson G., Sim R.B., Poole J., Pausch V., Merry A.H., Liew Y.W., Tanner M.J.A.; "Biochemical studies on red blood cells from a patient with the Inab phenotype (decay-accelerating factor deficiency)."; Blood 78:3291-3297(1991).
[25]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 161-285. DOI=10.1074/jbc.M212561200; PubMed=12499389 [NCBI, ExPASy, EBI, Israel, Japan] Williams P., Chaudhry Y., Goodfellow I.G., Billington J., Powell R., Spiller O.B., Evans D.J., Lea S.; "Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A."; J. Biol. Chem. 278:10691-10696(2003).
[26]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF OF 35-286. DOI=10.1073/pnas.0307200101; PubMed=14734808 [NCBI, ExPASy, EBI, Israel, Japan] Lukacik P., Roversi P., White J., Esser D., Smith G.P., Billington J., Williams P.A., Rudd P.M., Wormald M.R., Harvey D.J., Crispin M.D., Radcliffe C.M., Dwek R.A., Evans D.J., Morgan B.P., Smith R.A., Lea S.M.; "Complement regulation at the molecular level: the structure of decay-accelerating factor."; Proc. Natl. Acad. Sci. U.S.A. 101:1279-1284(2004).
[27]	STRUCTURE BY NMR OF 95-223. DOI=10.1073/pnas.0730844100; PubMed=12672958 [NCBI, ExPASy, EBI, Israel, Japan] Uhrinova S., Lin F., Ball G., Bromek K., Uhrin D., Medof M.E., Barlow P.N.; "Solution structure of a functionally active fragment of decay-accelerating factor."; Proc. Natl. Acad. Sci. U.S.A. 100:4718-4723(2003).

Comments

FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.
SUBUNIT: Monomer (major form) and non-disulfide-linked, covalent homodimer (minor form). Binds to coxsackievirus A21, coxsackieviruses B1, B3 and B5, human enterovirus 70, human echoviruses 6, 7, 11, 12, 20 and 21 capsid proteins and acts as a receptor for these viruses.
SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein.
SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-anchor.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	2
Synonyms	DAF-2
Isoform ID	P08174-1
Note: GPI-anchored form.
This is the isoform sequence displayed in this entry.

Name	1
Synonyms	DAF-1
Isoform ID	P08174-2
Features which should be applied to build the isoform sequence: VSP_001200.

TISSUE SPECIFICITY: Expressed on the plasma membranes of all cell types that are in intimate contact with plasma complement proteins. It is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of the molecule are present in body fluids and in extracellular matrix.
DOMAIN: The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 (By similarity).
PTM: The Ser/Thr-rich domain is heavily O-glycosylated.
POLYMORPHISM: Responsible for the Cromer blood group system. It consists of at least 8 high-incidence (Cr(a), Tc(a), Dr(a), Es(a), WES(b), UMC, IFC and GUTI) and three low-incidence (Tc(b), Tc(c) and WES(a)) antigens that reside on DAF. In the Cromer phenotypes Dr(a-) and Inab there is reduced or absent expression of DAF, respectively. In the case of the Dr(a-) phenotype, a single nucleotide substitution within exon 5 accounts for two changes: a simple amino acid substitution, Leu-199 that is the basis of the antigenic variation, and an alternative splicing event that underlies the decreased expression of DAF in this phenotype. The Inab phenotype is a very rare one in which the red blood cells lack all Cromer system antigens. The red blood cells of individuals with Inab phenotype have a deficiency of DAF, but these individuals are not known to have any associated hematologic or other abnormalities.
SIMILARITY: Belongs to the receptors of complement activation (RCA) family.
SIMILARITY: Contains 4 Sushi (CCP/SCR) domains.
WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=cromer";.
WEB RESOURCE: Name=CD55base; Note=CD55 mutation db; URL="http://bioinf.uta.fi/CD55base/";.
WEB RESOURCE: Name=Wikipedia; Note=Decay-accelerating factor entry; URL="http://en.wikipedia.org/wiki/Decay_accelerating_factor";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/daf/";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1upn";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M31516; AAA52169.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30142; AAA52168.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007159; AAP35823.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY851161; AAW29942.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001288; AAH01288.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64653; AAA52170.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64356; AAA52170.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15799; AAA52167.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U88576; AAB48622.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S72858; AAC60633.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00216550; -.
IPI00292069; -.

PIR

A26359; A26359.
B26359; B26359.

RefSeq

NP_000565.1; -.
NP_001108224.1; -.

UniGene

Hs.527653

3D structure databases

PDB

1H03; X-ray; 1.70 A; P/Q=161-285.	[ExPASy / RCSB / EBI]
1H04; X-ray; 2.00 A; P=161-285.	[ExPASy / RCSB / EBI]
1H2P; X-ray; 2.80 A; P=161-285.	[ExPASy / RCSB / EBI]
1H2Q; X-ray; 3.00 A; P=161-285.	[ExPASy / RCSB / EBI]
1M11; EM; 16.00 A; R=35-277.	[ExPASy / RCSB / EBI]
1NWV; NMR; -; A=96-222.	[ExPASy / RCSB / EBI]
1OJV; X-ray; 2.30 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1OJW; X-ray; 2.30 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1OJY; X-ray; 2.60 A; A/B/C/D=35-285.	[ExPASy / RCSB / EBI]
1OK1; X-ray; 2.60 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1OK2; X-ray; 2.50 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1OK3; X-ray; 2.20 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1OK9; X-ray; 3.00 A; A/B=35-285.	[ExPASy / RCSB / EBI]
1UOT; X-ray; 3.00 A; P=161-285.	[ExPASy / RCSB / EBI]
1UPN; EM; -; E=157-285.	[ExPASy / RCSB / EBI]
2C8I; EM; 14.00 A; E=35-285.	[ExPASy / RCSB / EBI]
2QZD; EM; -; A=222-285.	[ExPASy / RCSB / EBI]
2QZF; EM; -; A=35-94.	[ExPASy / RCSB / EBI]
2QZH; EM; 14.00 A; A=96-222.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H03; -.
1H04; -.
1H2P; -.
1H2Q; -.
1M11; -.
1NWV; -.
1OJV; -.
1OJW; -.
1OJY; -.
1OK1; -.
1OK2; -.
1OK3; -.
1OK9; -.
1UOT; -.
1UPN; -.
2C8I; -.
2QZD; -.
2QZF; -.
2QZH; -.

ModBase

P08174.

Organism-specific databases

GC01P205561; -.

HIX0001538; -.

HGNC:2665; CD55.

CAB010454; -.
HPA002190; -.

MIM

125240; gene+phenotype. [NCBI / EBI]

Gene expression databases

P08174; -.

P08174; -.

HS_CD55; -.

ENSG00000196352; Homo sapiens.

Ontologies

GO:0031225;	Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0045121;	Cellular component: membrane raft (inferred from direct assay from UniProtKB).
GO:0005625;	Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0006958;	Biological process: complement activation, classical pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0007204;	Biological process: elevation of cytosolic calcium ion concentration (inferred from direct assay from UniProtKB).
GO:0045087;	Biological process: innate immune response (inferred from electronic annotation from UniProtKB-KW).
GO:0045730;	Biological process: respiratory burst (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016060; Complement_control_module.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.

Gene3D

G3DSA:2.10.70.10; Complement_control_module; 4.

Pfam

PF00084; Sushi; 4.
Pfam graphical view of domain structure.

SMART

SM00032; CCP; 4.
SMART graphical view of domain structure.

PROSITE

PS50923; SUSHI; 4.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P08174; -.

Genome annotation databases

Ensembl

ENSG00000196352; Homo sapiens. [Contig view]

GeneID

1604; -.

KEGG

hsa:1604; -.

Phylogenomic databases

HOVERGEN

P08174; -.

Other

DrugBank

DB00446; Chloramphenicol.

6582; -.

CD55; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Blood group antigen; Cell membrane; Complement pathway; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Immune response; Innate immunity; Lipoprotein; Membrane; Phosphoprotein; Polymorphism; Repeat; Signal; Sushi.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 34`	`34`
`CHAIN`	`35 353`	`319`	`Complement decay-accelerating factor.`	`PRO_0000006000`
`PROPEP`	`354 381`	`28`	`Removed in mature form.`	`PRO_0000006001`
`DOMAIN`	`35 96`	`62`	`Sushi 1.`
`DOMAIN`	`96 160`	`65`	`Sushi 2.`
`DOMAIN`	`161 222`	`62`	`Sushi 3.`
`DOMAIN`	`223 285`	`63`	`Sushi 4.`
`COMPBIAS`	`287 356`	`70`	`Ser/Thr-rich.`
`MOD_RES`	`140 140`		`Phosphoserine.`
`LIPID`	`353 353`		`GPI-anchor amidated serine.`
`CARBOHYD`	`95 95`		`N-linked (GlcNAc...).`
`DISULFID`	`36 81`
`DISULFID`	`65 94`
`DISULFID`	`98 145`
`DISULFID`	`129 158`
`DISULFID`	`163 204`
`DISULFID`	`190 220`
`DISULFID`	`225 267`
`DISULFID`	`253 283`
`VAR_SEQ`	`362 381`		`HTCFTLTGLLGTLVTMGLLT -> SRPVTQAGMRWCDRSSLQSRTPGFKRSFHFSLPSSWYYRA` `HVFHVDRFAWDASNHGLADLAKEELRRKYTQVYRLFLVS (in isoform 1).`	`VSP_001200`
`VARIANT`	`52 52`	`1`	`R -> L (in Tc(b) antigen; dbSNP:rs28371588 [NCBI]).`	`VAR_001997`
`VARIANT`	`52 52`	`1`	`R -> P (in Tc(c) antigen).`	`VAR_001998`
`VARIANT`	`82 82`	`1`	`L -> R (in WES(a) antigen).`	`VAR_001999`
`VARIANT`	`199 199`	`1`	`S -> L (in Dr(a-) antigen).`	`VAR_002000 [3D]`
`VARIANT`	`227 227`	`1`	`A -> P (in Cr(a-) antigen).`	`VAR_002001 [3D]`
`VARIANT`	`240 240`	`1`	`R -> H (in GUTI(-) antigen).`	`VAR_015884 [3D]`
`CONFLICT`	`80 80`		`I -> T (in Ref. 5; AAA52170 and 6; AAA52167).`
`CONFLICT`	`85 85`		`S -> M (in Ref. 6; AAA52167).`
`CONFLICT`	`187 187`		`S -> T (in Ref. 7; AAB48622).`
`CONFLICT`	`297 297`		`Q -> H (in Ref. 7; AAB48622).`
`STRAND`	`45 47`	`3`
`STRAND`	`60 65`	`6`
`STRAND`	`78 82`	`5`
`TURN`	`83 85`	`3`
`STRAND`	`105 109`	`5`
`HELIX`	`113 115`	`3`
`STRAND`	`124 129`	`6`
`STRAND`	`133 135`	`3`
`STRAND`	`142 145`	`4`
`STRAND`	`172 175`	`4`
`STRAND`	`185 190`	`6`
`STRAND`	`194 198`	`5`
`STRAND`	`200 207`	`8`
`STRAND`	`210 215`	`6`
`STRAND`	`219 222`	`4`
`STRAND`	`234 236`	`3`
`STRAND`	`248 253`	`6`
`STRAND`	`258 261`	`4`
`STRAND`	`263 270`	`8`
`STRAND`	`273 278`	`6`
`STRAND`	`282 284`	`3`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 41400 Da [This is the MW of the unprocessed precursor]

CRC64: C1CBE5300F60C176 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE GRTSFPEDTV 

        70         80         90        100        110        120 
ITYKCEESFV KIPGEKDSVI CLKGSQWSDI EEFCNRSCEV PTRLNSASLK QPYITQNYFP 

       130        140        150        160        170        180 
VGTVVEYECR PGYRREPSLS PKLTCLQNLK WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI 

       190        200        210        220        230        240 
LFGATISFSC NTGYKLFGST SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER 

       250        260        270        280        290        300 
DHYGYRQSVT YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT 

       310        320        330        340        350        360 
TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG TTSGTTRLLS 

       370        380 
GHTCFTLTGL LGTLVTMGLL T

P08174 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools