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Immunoglobulin heavy constant mu (Ig mu chain C region) (Ig mu chain C region BOT) (Ig mu chain C region GAL) (Ig mu chain C region OU)

 IGHM_HUMAN              Reviewed;         453 AA.
P01871; A0A075B6N9; A0A0G2JQL4; P04220; P20769;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 4.
25-OCT-2017, entry version 176.
RecName: Full=Immunoglobulin heavy constant mu {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
AltName: Full=Ig mu chain C region {ECO:0000305};
AltName: Full=Ig mu chain C region BOT {ECO:0000305|PubMed:6425189};
AltName: Full=Ig mu chain C region GAL {ECO:0000305|PubMed:4803843};
AltName: Full=Ig mu chain C region OU {ECO:0000305|PubMed:4742735};
Name=IGHM {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE.
PubMed=4803843;
Watanabe S., Barnikol H.U., Horn J., Bertram J., Hilschmann N.;
"The primary structure of a monoclonal IgM-immunoglobulin
(macroglobulin Gal.), II: the amino acid sequence of the H-chain (mu-
type), subgroup H III. Architecture of the complete IgM-molecule.";
Hoppe-Seyler's Z. Physiol. Chem. 354:1505-1509(1973).
[2]
SEQUENCE REVISION.
PubMed=6777162;
Mihaesco E., Barnikol-Watanabe S., Barnikol H.U., Mihaesco C.,
Hilschmann N.;
"The primary structure of the constant part of mu-chain-disease
protein BOT.";
Eur. J. Biochem. 111:275-286(1980).
[3]
PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION.
PubMed=4742735; DOI=10.1126/science.182.4109.287;
Putnam F.W., Florent G., Paul C., Shinoda T., Shimizu A.;
"Complete amino acid sequence of the Mu heavy chain of a human IgM
immunoglobulin.";
Science 182:287-291(1973).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 434-453 (ISOFORM 2), AND VARIANTS LEU-40 AND VAL-414
DEL.
PubMed=2505237; DOI=10.1093/nar/17.15.6412;
Dorai H., Gillies S.D.;
"The complete nucleotide sequence of a human immunoglobulin genomic C
mu gene.";
Nucleic Acids Res. 17:6412-6412(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-191.
PubMed=2115996; DOI=10.1093/nar/18.14.4278;
Friedlander R.M., Nussenzweig M.C., Leder P.;
"Complete nucleotide sequence of the membrane form of the human IgM
heavy chain.";
Nucleic Acids Res. 18:4278-4278(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Calvo B.F., Schlom J., Kashmiri S.;
"Complete nucleotide sequence of a cDNA encoding human IgM heavy chain
constant domains.";
Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHM*04).
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
PROTEIN SEQUENCE OF 104-453, AND VARIANT GLY-215.
PubMed=6425189; DOI=10.1515/bchm2.1984.365.1.105;
Barnikol-Watanabe S., Mihaesco E., Mihaesco C., Barnikol H.U.,
Hilschmann N.;
"The primary structure of mu-chain-disease protein BOT. Peculiar
amino-acid sequence of the N-terminal 42 positions.";
Hoppe-Seyler's Z. Physiol. Chem. 365:105-118(1984).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 298-386 AND 436-452.
PubMed=6777778; DOI=10.1073/pnas.77.10.6027;
Dolby T.W., Devuono J., Croce C.M.;
"Cloning and partial nucleotide sequence of human immunoglobulin mu
chain cDNA from B cells and mouse-human hybridomas.";
Proc. Natl. Acad. Sci. U.S.A. 77:6027-6031(1980).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-453 (ISOFORM 2), AND VARIANTS
VAL-414 DEL AND ASP-418.
PubMed=6795593; DOI=10.1093/nar/9.18.4509;
Rabbitts T.H., Forster A., Milstein C.P.;
"Human immunoglobulin heavy chain genes: evolutionary comparisons of C
mu, C delta and C gamma genes and associated switch sequences.";
Nucleic Acids Res. 9:4509-4524(1981).
[11]
FUNCTION.
PubMed=3137579; DOI=10.1073/pnas.85.18.6914;
Tisch R., Roifman C.M., Hozumi N.;
"Functional differences between immunoglobulins M and D expressed on
the surface of an immature B-cell line.";
Proc. Natl. Acad. Sci. U.S.A. 85:6914-6918(1988).
[12]
NOMENCLATURE.
PubMed=11340299;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin heavy (IGH) genes.";
Exp. Clin. Immunogenet. 18:100-116(2001).
[13]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-46.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[15]
REVIEW.
PubMed=16895553; DOI=10.1111/j.1365-2567.2006.02386.x;
Geisberger R., Lamers M., Achatz G.;
"The riddle of the dual expression of IgM and IgD.";
Immunology 118:429-437(2006).
[16]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-46 AND ASN-279.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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).
[18]
GLYCOSYLATION AT ASN-46 AND ASN-209.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[19]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
[22]
INVOLVEMENT IN AGM1.
PubMed=8890099; DOI=10.1056/NEJM199611143352003;
Yel L., Minegishi Y., Coustan-Smith E., Buckley R.H., Trubel H.,
Pachman L.M., Kitchingman G.R., Campana D., Rohrer J., Conley M.E.;
"Mutations in the mu heavy-chain gene in patients with
agammaglobulinemia.";
N. Engl. J. Med. 335:1486-1493(1996).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Constant region of immunoglobulin heavy chains.
Immunoglobulins, also known as antibodies, are membrane-bound or
secreted glycoproteins produced by B lymphocytes. In the
recognition phase of humoral immunity, the membrane-bound
immunoglobulins serve as receptors which, upon binding of a
specific antigen, trigger the clonal expansion and differentiation
of B lymphocytes into immunoglobulins-secreting plasma cells.
Secreted immunoglobulins mediate the effector phase of humoral
immunity, which results in the elimination of bound antigens
(PubMed:22158414, PubMed:20176268). The antigen binding site is
formed by the variable domain of one heavy chain, together with
that of its associated light chain. Thus, each immunoglobulin has
two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:17576170, PubMed:20176268). IgM antibodies play an
important role in primary defense mechanisms. They have been shown
to be involved in early recognition of external invaders like
bacteria and viruses, cellular waste and modified self, as well as
in recognition and elimination of precancerous and cancerous
lesions. The membrane-bound form is found in the majority of
normal B-cells alongside with IgD. Membrane-bound IgM induces the
phosphorylation of CD79A and CD79B by the Src family of protein
tyrosine kinases. It may cause death of cells by apoptosis. It is
also found in soluble form, which represents about 30% of the
total serum immunoglobulins where it is found almost exclusively
as a homopentamer. After the antigen binds to the B-cell receptor,
the secreted form is secreted in large amounts (PubMed:3137579,
PubMed:16895553). {ECO:0000269|PubMed:3137579,
ECO:0000303|PubMed:16895553, ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- INTERACTION:
P15391:CD19; NbExp=2; IntAct=EBI-953797, EBI-79902;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Note=During
differentiation, B-lymphocytes switch from expression of membrane-
bound IgM to secretion of IgM.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Secreted;
IsoId=P01871-1; Sequence=Displayed;
Name=2; Synonyms=Membrane-bound;
IsoId=P01871-2; Sequence=VSP_034488;
Note=Ref.10 (AAB59422) sequence is in conflict in position:
438:S->N. Ref.10 (AAB59422) sequence is in conflict in position:
440:D->E. Ref.10 (AAB59422) sequence is in conflict in position:
449:A->T. Ref.10 (AAB59422) and Ref.4 (CAA33065) sequences are
in conflict in positions: 472:KVK->K. {ECO:0000305};
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGHM*04. {ECO:0000305}.
-!- DISEASE: Agammaglobulinemia 1, autosomal recessive (AGM1)
[MIM:601495]: A primary immunodeficiency characterized by
profoundly low or absent serum antibodies and low or absent
circulating B cells due to an early block of B-cell development.
Affected individuals develop severe infections in the first years
of life. {ECO:0000269|PubMed:8890099}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- CAUTION: For an example of a full-length immunoglobulin mu heavy
chain see AC P0DOX6. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA33065.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA33069.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA33071.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA34971.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAE82013.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAE82014.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=IGHMbase; Note=IGHM mutation db;
URL="http://structure.bmc.lu.se/idbase/IGHMbase/";
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EMBL; X14940; CAE82013.1; ALT_INIT; Genomic_DNA.
EMBL; X14940; CAE82014.1; ALT_INIT; Genomic_DNA.
EMBL; X14940; CAA33069.1; ALT_INIT; Genomic_DNA.
EMBL; X14940; CAA33070.1; -; Genomic_DNA.
EMBL; X14940; CAA33071.1; ALT_SEQ; Genomic_DNA.
EMBL; X14939; CAA33065.1; ALT_INIT; Genomic_DNA.
EMBL; X17115; CAA34971.1; ALT_INIT; mRNA.
EMBL; X57086; CAB37838.1; -; mRNA.
EMBL; AC244226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC246787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC247036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K01310; AAB59422.1; -; Genomic_DNA.
PIR; A02163; MHHUBT.
PIR; S14683; S14683.
PIR; S16510; MHHUM.
UniGene; Hs.510635; -.
PDB; 1HEZ; X-ray; 2.70 A; B/D=1-104.
PDB; 2AGJ; X-ray; 2.60 A; H=169-428.
PDBsum; 1HEZ; -.
PDBsum; 2AGJ; -.
ProteinModelPortal; P01871; -.
SMR; P01871; -.
CORUM; P01871; -.
IntAct; P01871; 62.
MINT; MINT-2860005; -.
IMGT_GENE-DB; IGHM; -.
iPTMnet; P01871; -.
PhosphoSitePlus; P01871; -.
UniCarbKB; P01871; -.
DMDM; 193806374; -.
UCD-2DPAGE; P01871; -.
PeptideAtlas; P01871; -.
PRIDE; P01871; -.
Ensembl; ENST00000390559; ENSP00000375001; ENSG00000211899. [P01871-1]
Ensembl; ENST00000626472; ENSP00000485962; ENSG00000282657. [P01871-1]
Ensembl; ENST00000637539; ENSP00000490253; ENSG00000211899. [P01871-2]
DisGeNET; 3507; -.
EuPathDB; HostDB:ENSG00000211899.8; -.
GeneCards; IGHM; -.
HGNC; HGNC:5541; IGHM.
MalaCards; IGHM; -.
MIM; 147020; gene.
MIM; 601495; phenotype.
neXtProt; NX_P01871; -.
OpenTargets; ENSG00000211899; -.
Orphanet; 33110; Autosomal agammaglobulinemia.
GeneTree; ENSGT00530000063726; -.
HOGENOM; HOG000202819; -.
HOVERGEN; HBG005814; -.
InParanoid; P01871; -.
PhylomeDB; P01871; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; P01871; -.
PRO; PR:P01871; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000211899; -.
ExpressionAtlas; P01871; baseline and differential.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0071757; C:hexameric IgM immunoglobulin complex; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IDA:UniProtKB.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
Pfam; PF07654; C1-set; 4.
SMART; SM00407; IGc1; 4.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 4.
PROSITE; PS00290; IG_MHC; 2.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin C region;
Immunoglobulin domain; Membrane; Polymorphism; Reference proteome;
Secreted; Transmembrane.
CHAIN <1 453 Immunoglobulin heavy constant mu.
/FTId=PRO_0000153619.
DOMAIN 6 102 Ig-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 111 211 Ig-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 229 319 Ig-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 329 430 Ig-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
REGION 1 105 CH1.
REGION 106 217 CH2.
REGION 218 323 CH3.
REGION 324 452 CH4.
CARBOHYD 46 46 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 209 209 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:19139490}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:4742735}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4742735}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:4742735}.
/FTId=CAR_000219.
DISULFID 14 14 Interchain (with light chain).
{ECO:0000269|PubMed:4742735}.
DISULFID 28 88 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 134 197 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 214 214 Interchain (with heavy chain).
{ECO:0000269|PubMed:4742735}.
DISULFID 244 303 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 291 291 Interchain (with heavy chain of another
subunit). {ECO:0000269|PubMed:4742735}.
DISULFID 351 413 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 452 452 Interchain (with heavy chain).
{ECO:0000269|PubMed:4742735}.
VAR_SEQ 434 453 GKPTLYNVSLVMSDTAGTCY -> EGEVSADEEGFENLWAT
ASTFIVLFLLSLFYSTTVTLFKVK (in isoform 2).
{ECO:0000303|PubMed:2115996,
ECO:0000303|PubMed:6795593}.
/FTId=VSP_034488.
VARIANT 40 40 F -> L (in IMGT allele IGHM*01).
{ECO:0000269|PubMed:2505237}.
/FTId=VAR_077893.
VARIANT 191 191 G -> S (in IMGT allele IGHM*03).
{ECO:0000269|PubMed:2115996}.
/FTId=VAR_003903.
VARIANT 215 215 V -> G (in dbSNP:rs12365).
{ECO:0000269|PubMed:6425189}.
/FTId=VAR_003904.
VARIANT 414 414 Missing (in IMGT allele IGHM*01 IMGT
allele IGHM*02).
{ECO:0000269|PubMed:2505237,
ECO:0000269|PubMed:6795593}.
/FTId=VAR_077894.
VARIANT 418 418 E -> D (in IMGT allele IGHM*02).
{ECO:0000269|PubMed:6795593}.
/FTId=VAR_077895.
CONFLICT 128 128 R -> RS (in Ref. 5; CAA34971).
{ECO:0000305}.
CONFLICT 145 145 Q -> E (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 163 165 QVQ -> EVE (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 220 220 T -> I (in Ref. 6; CAB37838).
{ECO:0000305}.
CONFLICT 263 263 N -> D (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 296 296 N -> D (in Ref. 8; AA sequence).
{ECO:0000305}.
NON_TER 1 1
STRAND 178 184 {ECO:0000244|PDB:2AGJ}.
STRAND 196 201 {ECO:0000244|PDB:2AGJ}.
STRAND 206 208 {ECO:0000244|PDB:2AGJ}.
STRAND 210 216 {ECO:0000244|PDB:2AGJ}.
STRAND 223 227 {ECO:0000244|PDB:2AGJ}.
HELIX 236 238 {ECO:0000244|PDB:2AGJ}.
STRAND 240 242 {ECO:0000244|PDB:2AGJ}.
HELIX 249 251 {ECO:0000244|PDB:2AGJ}.
STRAND 253 258 {ECO:0000244|PDB:2AGJ}.
TURN 261 264 {ECO:0000244|PDB:2AGJ}.
STRAND 265 272 {ECO:0000244|PDB:2AGJ}.
HELIX 275 277 {ECO:0000244|PDB:2AGJ}.
STRAND 279 285 {ECO:0000244|PDB:2AGJ}.
STRAND 287 290 {ECO:0000244|PDB:2AGJ}.
STRAND 300 302 {ECO:0000244|PDB:2AGJ}.
STRAND 316 318 {ECO:0000244|PDB:2AGJ}.
STRAND 345 351 {ECO:0000244|PDB:2AGJ}.
STRAND 354 359 {ECO:0000244|PDB:2AGJ}.
STRAND 363 366 {ECO:0000244|PDB:2AGJ}.
STRAND 386 388 {ECO:0000244|PDB:2AGJ}.
STRAND 391 393 {ECO:0000244|PDB:2AGJ}.
STRAND 396 401 {ECO:0000244|PDB:2AGJ}.
HELIX 402 405 {ECO:0000244|PDB:2AGJ}.
STRAND 406 408 {ECO:0000244|PDB:2AGJ}.
STRAND 413 418 {ECO:0000244|PDB:2AGJ}.
SEQUENCE 453 AA; 49440 MW; 607CA2FA7BFA0D39 CRC64;
GSASAPTLFP LVSCENSPSD TSSVAVGCLA QDFLPDSITF SWKYKNNSDI SSTRGFPSVL
RGGKYAATSQ VLLPSKDVMQ GTDEHVVCKV QHPNGNKEKN VPLPVIAELP PKVSVFVPPR
DGFFGNPRKS KLICQATGFS PRQIQVSWLR EGKQVGSGVT TDQVQAEAKE SGPTTYKVTS
TLTIKESDWL GQSMFTCRVD HRGLTFQQNA SSMCVPDQDT AIRVFAIPPS FASIFLTKST
KLTCLVTDLT TYDSVTISWT RQNGEAVKTH TNISESHPNA TFSAVGEASI CEDDWNSGER
FTCTVTHTDL PSPLKQTISR PKGVALHRPD VYLLPPAREQ LNLRESATIT CLVTGFSPAD
VFVQWMQRGQ PLSPEKYVTS APMPEPQAPG RYFAHSILTV SEEEWNTGET YTCVVAHEAL
PNRVTERTVD KSTGKPTLYN VSLVMSDTAG TCY


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