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CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form]

 CD40L_HUMAN             Reviewed;         261 AA.
P29965;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
10-MAY-2017, entry version 194.
RecName: Full=CD40 ligand;
Short=CD40-L;
AltName: Full=T-cell antigen Gp39;
AltName: Full=TNF-related activation protein;
Short=TRAP;
AltName: Full=Tumor necrosis factor ligand superfamily member 5;
AltName: CD_antigen=CD154;
Contains:
RecName: Full=CD40 ligand, membrane form;
Contains:
RecName: Full=CD40 ligand, soluble form;
Name=CD40LG; Synonyms=CD40L, TNFSF5, TRAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=1280226; DOI=10.1002/eji.1830221226;
Graf D., Korthaeuer U., Mages H.W., Senger G., Kroczek R.A.;
"Cloning of TRAP, a ligand for CD40 on human T cells.";
Eur. J. Immunol. 22:3191-3194(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1385114;
Hollenbaugh D., Grosmaire L.S., Kullas C.D., Chalupny J.N.,
Braesch-Andersen S., Noelle R.J., Stamenkovic I., Ledbetter J.A.,
Aruffo A.;
"The human T cell antigen gp39, a member of the TNF gene family, is a
ligand for the CD40 receptor: expression of a soluble form of gp39
with B cell co-stimulatory activity.";
EMBO J. 11:4313-4321(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIGM1 128-ARG-GLY-129 AND
PRO-235.
PubMed=7678782; DOI=10.1016/0092-8674(93)90668-G;
Aruffo A., Farrington M., Hollenbaugh D., Li X., Milatovich A.,
Nonoyama S., Bajorath J., Grosmaire L.S., Stenkamp R., Neubauer M.,
Roberts R.L., Noelle R.J., Ledbetter J.A., Francke U., Ochs H.D.;
"The CD40 ligand, gp39, is defective in activated T cells from
patients with X-linked hyper-IgM syndrome.";
Cell 72:291-300(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1281209; DOI=10.1084/jem.176.6.1543;
Spriggs M.K., Armitage R.J., Strockbine L., Clifford K.N.,
Macduff B.M., Sato T.A., Maliszewski C.R., Fanslow W.C.;
"Recombinant human CD40 ligand stimulates B cell proliferation and
immunoglobulin E secretion.";
J. Exp. Med. 176:1543-1550(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7678552; DOI=10.1016/0014-5793(93)81175-Y;
Gauchat J.-F., Aubry J.-P., Mazzei G.J., Life P., Jomotte T.,
Elson G., Bonnefoy J.-Y.;
"Human CD40-ligand: molecular cloning, cellular distribution and
regulation of expression by factors controlling IgE production.";
FEBS Lett. 315:259-266(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7999797; DOI=10.1016/0167-4781(94)00179-7;
Shimadzu M., Nunoi H., Terasaki H., Ninomiya R., Iwata M.,
Kanegasaka S., Matsuda I.;
"Structural organization of the gene for CD40 ligand: molecular
analysis for diagnosis of X-linked hyper-IgM syndrome.";
Biochim. Biophys. Acta 1260:67-72(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PROTEIN SEQUENCE OF 113-117, PROTEOLYTIC PROCESSING, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=8626375; DOI=10.1074/jbc.271.11.5965;
Pietravalle F., Lecoanet-Henchoz S., Blasey H., Aubry J.-P., Elson G.,
Edgerton M.D., Bonnefoy J.-Y., Gauchat J.-F.;
"Human native soluble CD40L is a biologically active trimer, processed
inside microsomes.";
J. Biol. Chem. 271:5965-5967(1996).
[9]
FUNCTION.
PubMed=8617933;
Blotta M.H., Marshall J.D., DeKruyff R.H., Umetsu D.T.;
"Cross-linking of the CD40 ligand on human CD4+ T lymphocytes
generates a costimulatory signal that up-regulates IL-4 synthesis.";
J. Immunol. 156:3133-3140(1996).
[10]
STRUCTURE OF CARBOHYDRATE ON ASN-240, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBUNIT.
PubMed=11676606; DOI=10.1006/prep.2001.1501;
Khandekar S.S., Silverman C., Wells-Marani J., Bacon A.M., Birrell H.,
Brigham-Burke M., DeMarini D.J., Jonak Z.L., Camilleri P.,
Fishman-Lobell J.;
"Determination of carbohydrate structures N-linked to soluble CD154
and characterization of the interactions of CD40 with CD154 expressed
in Pichia pastoris and Chinese hamster ovary cells.";
Protein Expr. Purif. 23:301-310(2001).
[11]
FUNCTION.
PubMed=15193700; DOI=10.1016/j.jacc.2003.12.055;
Furman M.I., Krueger L.A., Linden M.D., Barnard M.R.,
Frelinger A.L. III, Michelson A.D.;
"Release of soluble CD40L from platelets is regulated by glycoprotein
IIb/IIIa and actin polymerization.";
J. Am. Coll. Cardiol. 43:2319-2325(2004).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15067037; DOI=10.1084/jem.20031705;
Mikolajczak S.A., Ma B.Y., Yoshida T., Yoshida R., Kelvin D.J.,
Ochi A.;
"The modulation of CD40 ligand signaling by transmembrane CD28 splice
variant in human T cells.";
J. Exp. Med. 199:1025-1031(2004).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-261, AND SUBUNIT.
PubMed=8589998; DOI=10.1016/S0969-2126(01)00239-8;
Karpsusas M., Hsu Y.-M., Wang J.-H., Thompson J., Lederman S.,
Chess L., Thomas D.;
"2-A crystal structure of an extracellular fragment of human CD40
ligand.";
Structure 3:1031-1039(1995).
[14]
3D-STRUCTURE MODELING OF COMPLEX WITH CD40.
PubMed=9605317; DOI=10.1002/pro.5560070506;
Singh J., Garber E., van Vlijmen H., Karpsusas M., Hsu Y.-M.,
Zheng Z., Naismith J.H., Thomas D.;
"The role of polar interactions in the molecular recognition of CD40L
with its receptor CD40.";
Protein Sci. 7:1124-1135(1998).
[15]
VARIANTS HIGM1 ARG-36 AND GLY-140.
PubMed=7679206; DOI=10.1038/361539a0;
Korthaeuer U., Graf D., Mages H.W., Briere F., Padayachee M.,
Malcolm S., Ugazio A.G., Notarangelo L.D., Levinsky R.J.,
Kroczek R.A.;
"Defective expression of T-cell CD40 ligand causes X-linked
immunodeficiency with hyper-IgM.";
Nature 361:539-541(1993).
[16]
VARIANT HIGM1 GLU-123.
PubMed=8094231; DOI=10.1038/361541a0;
Disanto J.P., Bonnefoy J.-Y., Gauchat J.-F., Fischer A.,
de Saint Basile G.;
"CD40 ligand mutations in X-linked immunodeficiency with hyper-IgM.";
Nature 361:541-543(1993).
[17]
VARIANTS HIGM1 PRO-155; ASN-211 AND VAL-227.
PubMed=7679801; DOI=10.1126/science.7679801;
Allen R.C., Armitage R.J., Conley M.E., Rosenblatt H., Jenkins N.A.,
Copeland N.G., Bedell M.A., Edelhoff S., Disteche C.M.,
Simoneaux D.K., Fanslow W.C., Belmont J.W., Spriggs M.K.;
"CD40 ligand gene defects responsible for X-linked hyper-IgM
syndrome.";
Science 259:990-993(1993).
[18]
VARIANTS HIGM1 ALA-126; ARG-140 AND GLU-144.
PubMed=7717401;
Macchi P., Villa A., Strina D., Sacco M.G., Morali F., Brugnoni D.,
Giliani S., Mantuano E., Fasth A., Andersson B., Zegers B.J.M.,
Cavagni G., Reznick I., Levy J., Zan-Bar I., Porat Y., Airo P.,
Plebani A., Vezzoni P., Notarangelo L.D.;
"Characterization of nine novel mutations in the CD40 ligand gene in
patients with X-linked hyper IgM syndrome of various ancestry.";
Am. J. Hum. Genet. 56:898-906(1995).
[19]
VARIANT HIGM1 GLU-237.
PubMed=7532185; DOI=10.1172/JCI117692;
Saiki O., Tanaka T., Wada Y., Uda H., Inoue A., Katada Y., Izeki M.,
Iwata M., Nunoi H., Matsuda I.;
"Signaling through CD40 rescues IgE but not IgG or IgA secretion in X-
linked immunodeficiency with hyper-IgM.";
J. Clin. Invest. 95:510-514(1995).
[20]
VARIANTS HIGM1 ARG-38; ARG-125; ARG-174 AND SER-257.
PubMed=8889581;
DOI=10.1002/(SICI)1098-1004(1996)8:3<223::AID-HUMU5>3.0.CO;2-A;
Katz F., Hinshelwood S., Rutland P., Jones A., Kinnon C., Morgan G.;
"Mutation analysis in CD40 ligand deficiency leading to X-linked
hypogammaglobulinemia with hyper IgM syndrome.";
Hum. Mutat. 8:223-228(1996).
[21]
VARIANTS HIGM1 PRO-155 AND VAL-227, AND VARIANT ARG-219.
PubMed=8550833; DOI=10.1172/JCI118389;
Lin Q., Rohrer J., Allen R.C., Larche M., Greene J.M., Shigeoka A.O.,
Gatti R.A., Derauf D.C., Belmont J.W., Conley M.E.;
"A single strand conformation polymorphism study of CD40 ligand.
Efficient mutation analysis and carrier detection for X-linked hyper
IgM syndrome.";
J. Clin. Invest. 97:196-201(1996).
[22]
VARIANTS HIGM1 ARG-36; CYS-140; GLY-227 DEL; SER-231 AND MET-254.
PubMed=9150729; DOI=10.1007/s004390050417;
Nonoyama S., Shimadzu M., Toru H., Seyama K., Nunoi H., Neubauer M.,
Yata J., Och H.D.;
"Mutations of the CD40 ligand gene in 13 Japanese patients with X-
linked hyper-IgM syndrome.";
Hum. Genet. 99:624-627(1997).
[23]
VARIANTS HIGM1 SER-116; ASN-147; CYS-170; VAL-227; SER-231; PRO-235;
MET-254 AND SER-258.
PubMed=9746782;
Seyama K., Nonoyama S., Gangsaas I., Hollenbaugh D., Pabst H.F.,
Aruffo A., Ochs H.D.;
"Mutations of the CD40 ligand gene and its effect on CD40 ligand
expression in patients with X-linked hyper IgM syndrome.";
Blood 92:2421-2434(1998).
[24]
VARIANT HIGM1 SER-116.
PubMed=26545377; DOI=10.1007/s00251-015-0878-6;
Ouadani H., Ben-Mustapha I., Ben-ali M., Ben-khemis L., Largueche B.,
Boussoffara R., Maalej S., Fetni I., Hassayoun S., Mahfoudh A.,
Mellouli F., Yalaoui S., Masmoudi H., Bejaoui M., Barbouche M.R.;
"Novel and recurrent AID mutations underlie prevalent autosomal
recessive form of HIGM in consanguineous patients.";
Immunogenetics 68:19-28(2016).
-!- FUNCTION: Cytokine that binds to CD40/TNFRSF5 (PubMed:1280226).
Costimulates T-cell proliferation and cytokine production. Its
cross-linking on T-cells generates a costimulatory signal which
enhances the production of IL4 and IL10 in conjunction with the
TCR/CD3 ligation and CD28 costimulation (PubMed:8617933). Induces
the activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-
cells. Induces tyrosine phosphorylation of isoform 3 of CD28
(PubMed:15067037). Mediates B-cell proliferation in the absence of
co-stimulus as well as IgE production in the presence of IL4.
Involved in immunoglobulin class switching (By similarity).
{ECO:0000250|UniProtKB:P27548, ECO:0000269|PubMed:1280226,
ECO:0000269|PubMed:15067037, ECO:0000269|PubMed:8617933}.
-!- FUNCTION: Release of soluble CD40L from platelets is partially
regulated by GP IIb/IIIa, actin polymerization, and an matrix
metalloproteinases (MMP) inhibitor-sensitive pathway.
{ECO:0000269|PubMed:15193700}.
-!- SUBUNIT: Homotrimer (PubMed:8589998, PubMed:8626375,
PubMed:11676606). Interacts with isoform 3 of CD28
(PubMed:15067037). {ECO:0000269|PubMed:11676606,
ECO:0000269|PubMed:15067037, ECO:0000269|PubMed:8589998,
ECO:0000269|PubMed:8626375}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8626375};
Single-pass type II membrane protein {ECO:0000303|PubMed:8626375}.
Cell surface {ECO:0000269|PubMed:15067037,
ECO:0000269|PubMed:7678552}.
-!- SUBCELLULAR LOCATION: CD40 ligand, soluble form: Secreted
{ECO:0000269|PubMed:8626375}.
-!- TISSUE SPECIFICITY: Specifically expressed on activated CD4+ T-
lymphocytes.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing. {ECO:0000269|PubMed:8626375}.
-!- PTM: N-linked glycan is a mixture of high mannose and complex
type. Glycan structure does not influence binding affinity to
CD40.
-!- PTM: Not O-glycosylated.
-!- DISEASE: X-linked immunodeficiency with hyper-IgM 1 (HIGM1)
[MIM:308230]: Immunoglobulin isotype switch defect characterized
by elevated concentrations of serum IgM and decreased amounts of
all other isotypes. Affected males present at an early age
(usually within the first year of life) recurrent bacterial and
opportunistic infections, including Pneumocystis carinii pneumonia
and intractable diarrhea due to cryptosporidium infection. Despite
substitution treatment with intravenous immunoglobulin, the
overall prognosis is rather poor, with a death rate of about 10%
before adolescence. {ECO:0000269|PubMed:26545377,
ECO:0000269|PubMed:7532185, ECO:0000269|PubMed:7678782,
ECO:0000269|PubMed:7679206, ECO:0000269|PubMed:7679801,
ECO:0000269|PubMed:7717401, ECO:0000269|PubMed:8094231,
ECO:0000269|PubMed:8550833, ECO:0000269|PubMed:8889581,
ECO:0000269|PubMed:9150729, ECO:0000269|PubMed:9746782}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=CD40Lbase; Note=CD40L defect database;
URL="http://structure.bmc.lu.se/idbase/CD40Lbase/";
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EMBL; X68550; CAA48554.1; -; mRNA.
EMBL; Z15017; CAA78737.1; -; mRNA.
EMBL; X67878; CAA48077.1; -; mRNA.
EMBL; L07414; AAA35662.1; -; mRNA.
EMBL; D31797; BAA06599.1; -; Genomic_DNA.
EMBL; BC071754; AAH71754.1; -; mRNA.
EMBL; BC074950; AAH74950.1; -; mRNA.
CCDS; CCDS14659.1; -.
PIR; S28017; I53476.
RefSeq; NP_000065.1; NM_000074.2.
UniGene; Hs.592244; -.
PDB; 1ALY; X-ray; 2.00 A; A=116-261.
PDB; 1I9R; X-ray; 3.10 A; A/B/C=116-261.
PDB; 3LKJ; X-ray; 2.50 A; A/B/C=121-261.
PDB; 3QD6; X-ray; 3.50 A; A/B/C/D/E/F=116-261.
PDBsum; 1ALY; -.
PDBsum; 1I9R; -.
PDBsum; 3LKJ; -.
PDBsum; 3QD6; -.
ProteinModelPortal; P29965; -.
SMR; P29965; -.
BioGrid; 107397; 9.
DIP; DIP-3013N; -.
STRING; 9606.ENSP00000359663; -.
ChEMBL; CHEMBL3580491; -.
iPTMnet; P29965; -.
PhosphoSitePlus; P29965; -.
UniCarbKB; P29965; -.
BioMuta; CD40LG; -.
DMDM; 231718; -.
MaxQB; P29965; -.
PaxDb; P29965; -.
PeptideAtlas; P29965; -.
PRIDE; P29965; -.
DNASU; 959; -.
Ensembl; ENST00000370629; ENSP00000359663; ENSG00000102245.
GeneID; 959; -.
KEGG; hsa:959; -.
UCSC; uc004faa.4; human.
CTD; 959; -.
DisGeNET; 959; -.
GeneCards; CD40LG; -.
GeneReviews; CD40LG; -.
HGNC; HGNC:11935; CD40LG.
HPA; HPA045827; -.
MalaCards; CD40LG; -.
MIM; 300386; gene.
MIM; 308230; phenotype.
neXtProt; NX_P29965; -.
OpenTargets; ENSG00000102245; -.
Orphanet; 101088; X-linked hyper-IgM syndrome.
PharmGKB; PA36626; -.
eggNOG; ENOG410IVYF; Eukaryota.
eggNOG; ENOG4111TET; LUCA.
GeneTree; ENSGT00510000048489; -.
HOGENOM; HOG000111291; -.
HOVERGEN; HBG079629; -.
InParanoid; P29965; -.
KO; K03161; -.
OMA; SMKIFMY; -.
OrthoDB; EOG091G0I9G; -.
PhylomeDB; P29965; -.
TreeFam; TF332169; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
SIGNOR; P29965; -.
EvolutionaryTrace; P29965; -.
GeneWiki; CD154; -.
GenomeRNAi; 959; -.
PMAP-CutDB; P29965; -.
PRO; PR:P29965; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102245; -.
CleanEx; HS_CD40LG; -.
ExpressionAtlas; P29965; baseline and differential.
Genevisible; P29965; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005174; F:CD40 receptor binding; IPI:UniProtKB.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0042100; P:B cell proliferation; IDA:UniProtKB.
GO; GO:0048305; P:immunoglobulin secretion; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; TAS:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR003263; CD40L.
InterPro; IPR021184; TNF_CS.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00229; TNF; 1.
PIRSF; PIRSF016527; TNF_5; 1.
PRINTS; PR01702; CD40LIGAND.
SMART; SM00207; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS00251; TNF_1; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytokine;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Membrane; Polymorphism; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 261 CD40 ligand, membrane form.
/FTId=PRO_0000034484.
CHAIN 113 261 CD40 ligand, soluble form.
{ECO:0000269|PubMed:8626375}.
/FTId=PRO_0000034485.
TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.
TRANSMEM 23 46 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 47 261 Extracellular. {ECO:0000255}.
SITE 112 113 Cleavage.
CARBOHYD 240 240 N-linked (GlcNAc...) (complex)
asparagine; alternate.
CARBOHYD 240 240 N-linked (GlcNAc...) (high mannose)
asparagine; alternate.
DISULFID 178 218 {ECO:0000255}.
VARIANT 36 36 M -> R (in HIGM1; dbSNP:rs104894774).
{ECO:0000269|PubMed:7679206,
ECO:0000269|PubMed:9150729}.
/FTId=VAR_007513.
VARIANT 38 38 G -> R (in HIGM1).
{ECO:0000269|PubMed:8889581}.
/FTId=VAR_017925.
VARIANT 116 116 G -> R (in HIGM1).
/FTId=VAR_017929.
VARIANT 116 116 G -> S (in HIGM1).
{ECO:0000269|PubMed:26545377,
ECO:0000269|PubMed:9746782}.
/FTId=VAR_017930.
VARIANT 123 123 A -> E (in HIGM1; dbSNP:rs104894778).
{ECO:0000269|PubMed:8094231}.
/FTId=VAR_007514.
VARIANT 125 125 H -> R (in HIGM1).
{ECO:0000269|PubMed:8889581}.
/FTId=VAR_017926.
VARIANT 126 126 V -> A (in HIGM1).
{ECO:0000269|PubMed:7717401}.
/FTId=VAR_007515.
VARIANT 126 126 V -> D (in HIGM1).
/FTId=VAR_017931.
VARIANT 128 129 SE -> RG (in HIGM1).
/FTId=VAR_007516.
VARIANT 140 140 W -> C (in HIGM1).
{ECO:0000269|PubMed:9150729}.
/FTId=VAR_007517.
VARIANT 140 140 W -> G (in HIGM1; dbSNP:rs104894777).
{ECO:0000269|PubMed:7679206}.
/FTId=VAR_007518.
VARIANT 140 140 W -> R (in HIGM1).
{ECO:0000269|PubMed:7717401}.
/FTId=VAR_007519.
VARIANT 143 143 K -> T (in HIGM1).
/FTId=VAR_017932.
VARIANT 144 144 G -> E (in HIGM1).
{ECO:0000269|PubMed:7717401}.
/FTId=VAR_007520.
VARIANT 147 147 T -> N (in HIGM1).
{ECO:0000269|PubMed:9746782}.
/FTId=VAR_017922.
VARIANT 155 155 L -> P (in HIGM1; dbSNP:rs104894769).
{ECO:0000269|PubMed:7679801,
ECO:0000269|PubMed:8550833}.
/FTId=VAR_007521.
VARIANT 170 170 Y -> C (in HIGM1; dbSNP:rs756468554).
{ECO:0000269|PubMed:9746782}.
/FTId=VAR_017923.
VARIANT 173 173 A -> D (in HIGM1).
/FTId=VAR_017933.
VARIANT 174 174 Q -> R (in HIGM1).
{ECO:0000269|PubMed:8889581}.
/FTId=VAR_017927.
VARIANT 176 176 T -> I (in HIGM1).
/FTId=VAR_017934.
VARIANT 195 195 L -> P (in HIGM1).
/FTId=VAR_017935.
VARIANT 208 208 A -> D (in HIGM1).
/FTId=VAR_017936.
VARIANT 211 211 T -> N (in HIGM1).
{ECO:0000269|PubMed:7679801}.
/FTId=VAR_007522.
VARIANT 219 219 G -> R (in dbSNP:rs148594123).
{ECO:0000269|PubMed:8550833}.
/FTId=VAR_007523.
VARIANT 224 224 H -> Y (in HIGM1).
/FTId=VAR_017937.
VARIANT 226 226 G -> A (in HIGM1).
/FTId=VAR_017938.
VARIANT 227 227 G -> V (in HIGM1; dbSNP:rs104894768).
{ECO:0000269|PubMed:7679801,
ECO:0000269|PubMed:8550833,
ECO:0000269|PubMed:9746782}.
/FTId=VAR_007524.
VARIANT 227 227 Missing (in HIGM1).
{ECO:0000269|PubMed:9150729}.
/FTId=VAR_007525.
VARIANT 231 231 L -> S (in HIGM1).
{ECO:0000269|PubMed:9150729,
ECO:0000269|PubMed:9746782}.
/FTId=VAR_007526.
VARIANT 235 235 A -> P (in HIGM1; dbSNP:rs104894771).
{ECO:0000269|PubMed:7678782,
ECO:0000269|PubMed:9746782}.
/FTId=VAR_007527.
VARIANT 237 237 V -> E (in HIGM1).
{ECO:0000269|PubMed:7532185}.
/FTId=VAR_017939.
VARIANT 254 254 T -> M (in HIGM1; dbSNP:rs193922136).
{ECO:0000269|PubMed:9150729,
ECO:0000269|PubMed:9746782}.
/FTId=VAR_007528.
VARIANT 257 257 G -> D (in HIGM1).
/FTId=VAR_017940.
VARIANT 257 257 G -> S (in HIGM1).
{ECO:0000269|PubMed:8889581}.
/FTId=VAR_017928.
VARIANT 258 258 L -> S (in HIGM1).
{ECO:0000269|PubMed:9746782}.
/FTId=VAR_017924.
STRAND 123 128 {ECO:0000244|PDB:1ALY}.
STRAND 132 134 {ECO:0000244|PDB:1ALY}.
STRAND 140 142 {ECO:0000244|PDB:1ALY}.
STRAND 153 156 {ECO:0000244|PDB:1ALY}.
TURN 157 159 {ECO:0000244|PDB:1ALY}.
STRAND 160 165 {ECO:0000244|PDB:1ALY}.
STRAND 167 179 {ECO:0000244|PDB:1ALY}.
TURN 181 183 {ECO:0000244|PDB:1ALY}.
STRAND 186 195 {ECO:0000244|PDB:1ALY}.
STRAND 203 211 {ECO:0000244|PDB:1ALY}.
STRAND 218 232 {ECO:0000244|PDB:1ALY}.
STRAND 237 242 {ECO:0000244|PDB:1ALY}.
HELIX 244 246 {ECO:0000244|PDB:1ALY}.
STRAND 251 260 {ECO:0000244|PDB:1ALY}.
SEQUENCE 261 AA; 29274 MW; 16F5CEB093BCC2BB CRC64;
MIETYNQTSP RSAATGLPIS MKIFMYLLTV FLITQMIGSA LFAVYLHRRL DKIEDERNLH
EDFVFMKTIQ RCNTGERSLS LLNCEEIKSQ FEGFVKDIML NKEETKKENS FEMQKGDQNP
QIAAHVISEA SSKTTSVLQW AEKGYYTMSN NLVTLENGKQ LTVKRQGLYY IYAQVTFCSN
REASSQAPFI ASLCLKSPGR FERILLRAAN THSSAKPCGQ QSIHLGGVFE LQPGASVFVN
VTDPSQVSHG TGFTSFGLLK L


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