IGHM_HUMAN
ID IGHM_HUMAN Reviewed; 453 AA.
AC P01871; A0A075B6N9; A0A0G2JQL4; P04220; P20769;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Immunoglobulin heavy constant mu {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
DE AltName: Full=Ig mu chain C region {ECO:0000305};
DE AltName: Full=Ig mu chain C region BOT {ECO:0000305|PubMed:6425189};
DE AltName: Full=Ig mu chain C region GAL {ECO:0000305|PubMed:4803843};
DE AltName: Full=Ig mu chain C region OU {ECO:0000305|PubMed:4742735};
GN Name=IGHM {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.13};
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 PROTEIN SEQUENCE.
RX PubMed=4803843;
RA Watanabe S., Barnikol H.U., Horn J., Bertram J., Hilschmann N.;
RT "The primary structure of a monoclonal IgM-immunoglobulin (macroglobulin
RT Gal.), II: the amino acid sequence of the H-chain (mu-type), subgroup H
RT III. Architecture of the complete IgM-molecule.";
RL Hoppe-Seyler's Z. Physiol. Chem. 354:1505-1509(1973).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=6777162; DOI=10.1111/j.1432-1033.1980.tb06103.x;
RA Mihaesco E., Barnikol-Watanabe S., Barnikol H.U., Mihaesco C.,
RA Hilschmann N.;
RT "The primary structure of the constant part of mu-chain-disease protein
RT BOT.";
RL Eur. J. Biochem. 111:275-286(1980).
RN [3]
RP PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-272 ASN-279 AND
RP ASN-440.
RX PubMed=4742735; DOI=10.1126/science.182.4109.287;
RA Putnam F.W., Florent G., Paul C., Shinoda T., Shimizu A.;
RT "Complete amino acid sequence of the Mu heavy chain of a human IgM
RT immunoglobulin.";
RL Science 182:287-291(1973).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 434-453 (ISOFORM 2), AND VARIANTS LEU-40 AND VAL-414 DEL.
RX PubMed=2505237; DOI=10.1093/nar/17.15.6412;
RA Dorai H., Gillies S.D.;
RT "The complete nucleotide sequence of a human immunoglobulin genomic C mu
RT gene.";
RL Nucleic Acids Res. 17:6412-6412(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-191.
RX PubMed=2115996; DOI=10.1093/nar/18.14.4278;
RA Friedlander R.M., Nussenzweig M.C., Leder P.;
RT "Complete nucleotide sequence of the membrane form of the human IgM heavy
RT chain.";
RL Nucleic Acids Res. 18:4278-4278(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Calvo B.F., Schlom J., Kashmiri S.;
RT "Complete nucleotide sequence of a cDNA encoding human IgM heavy chain
RT constant domains.";
RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHM*04).
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
RP PROTEIN SEQUENCE OF 104-453, AND VARIANT GLY-215.
RX PubMed=6425189; DOI=10.1515/bchm2.1984.365.1.105;
RA Barnikol-Watanabe S., Mihaesco E., Mihaesco C., Barnikol H.U.,
RA Hilschmann N.;
RT "The primary structure of mu-chain-disease protein BOT. Peculiar amino-acid
RT sequence of the N-terminal 42 positions.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:105-118(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 298-386 AND 436-452.
RX PubMed=6777778; DOI=10.1073/pnas.77.10.6027;
RA Dolby T.W., Devuono J., Croce C.M.;
RT "Cloning and partial nucleotide sequence of human immunoglobulin mu chain
RT cDNA from B cells and mouse-human hybridomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:6027-6031(1980).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-453 (ISOFORM 2), AND VARIANTS
RP VAL-414 DEL AND ASP-418.
RX PubMed=6795593; DOI=10.1093/nar/9.18.4509;
RA Rabbitts T.H., Forster A., Milstein C.P.;
RT "Human immunoglobulin heavy chain genes: evolutionary comparisons of C mu,
RT C delta and C gamma genes and associated switch sequences.";
RL Nucleic Acids Res. 9:4509-4524(1981).
RN [11]
RP FUNCTION.
RX PubMed=3137579; DOI=10.1073/pnas.85.18.6914;
RA Tisch R., Roifman C.M., Hozumi N.;
RT "Functional differences between immunoglobulins M and D expressed on the
RT surface of an immature B-cell line.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6914-6918(1988).
RN [12]
RP NOMENCLATURE.
RX PubMed=11340299; DOI=10.1159/000049189;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin heavy (IGH) genes.";
RL Exp. Clin. Immunogenet. 18:100-116(2001).
RN [13]
RP NOMENCLATURE.
RA Lefranc M.P., Lefranc G.;
RT "The Immunoglobulin FactsBook.";
RL (In) Lefranc M.P., Lefranc G. (eds.);
RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-46.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [15]
RP REVIEW.
RX PubMed=16895553; DOI=10.1111/j.1365-2567.2006.02386.x;
RA Geisberger R., Lamers M., Achatz G.;
RT "The riddle of the dual expression of IgM and IgD.";
RL Immunology 118:429-437(2006).
RN [16]
RP REVIEW ON SOMATIC HYPERMUTATION.
RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA Teng G., Papavasiliou F.N.;
RT "Immunoglobulin somatic hypermutation.";
RL Annu. Rev. Genet. 41:107-120(2007).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-46 AND ASN-279.
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 [18]
RP GLYCOSYLATION AT ASN-46 AND ASN-209.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [19]
RP REVIEW ON IMMUNOGLOBULINS.
RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA Schroeder H.W. Jr., Cavacini L.;
RT "Structure and function of immunoglobulins.";
RL J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN [20]
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 [21]
RP REVIEW ON FUNCTION.
RX PubMed=22158414; DOI=10.1038/nri3128;
RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT "Molecular programming of B cell memory.";
RL Nat. Rev. Immunol. 12:24-34(2012).
RN [22]
RP INVOLVEMENT IN AGM1.
RX PubMed=8890099; DOI=10.1056/nejm199611143352003;
RA Yel L., Minegishi Y., Coustan-Smith E., Buckley R.H., Trubel H.,
RA Pachman L.M., Kitchingman G.R., Campana D., Rohrer J., Conley M.E.;
RT "Mutations in the mu heavy-chain gene in patients with
RT agammaglobulinemia.";
RL N. Engl. J. Med. 335:1486-1493(1996).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24] {ECO:0007744|PDB:1HEZ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-104, AND DISULFIDE BONDS.
RX PubMed=11587642; DOI=10.1016/s0969-2126(01)00630-x;
RA Graille M., Stura E.A., Housden N.G., Beckingham J.A., Bottomley S.P.,
RA Beale D., Taussig M.J., Sutton B.J., Gore M.G., Charbonnier J.B.;
RT "Complex between Peptostreptococcus magnus protein L and a human antibody
RT reveals structural convergence in the interaction modes of Fab binding
RT proteins.";
RL Structure 9:679-687(2001).
RN [25] {ECO:0007744|PDB:2AGJ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-106, GLYCOSYLATION AT ASN-46,
RP AND DISULFIDE BONDS.
RX PubMed=16422668; DOI=10.1042/bj20051739;
RA Ramsland P.A., Terzyan S.S., Cloud G., Bourne C.R., Farrugia W.,
RA Tribbick G., Geysen H.M., Moomaw C.R., Slaughter C.A., Edmundson A.B.;
RT "Crystal structure of a glycosylated Fab from an IgM cryoglobulin with
RT properties of a natural proteolytic antibody.";
RL Biochem. J. 395:473-481(2006).
CC -!- FUNCTION: Constant region of immunoglobulin heavy chains.
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:22158414, PubMed:20176268). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
CC IgM antibodies play an important role in primary defense mechanisms.
CC They have been shown to be involved in early recognition of external
CC invaders like bacteria and viruses, cellular waste and modified self,
CC as well as in recognition and elimination of precancerous and cancerous
CC lesions. The membrane-bound form is found in the majority of normal B-
CC cells alongside with IgD. Membrane-bound IgM induces the
CC phosphorylation of CD79A and CD79B by the Src family of protein
CC tyrosine kinases. It may cause death of cells by apoptosis. It is also
CC found in soluble form, which represents about 30% of the total serum
CC immunoglobulins where it is found almost exclusively as a homopentamer.
CC After the antigen binds to the B-cell receptor, the secreted form is
CC secreted in large amounts (PubMed:3137579, PubMed:16895553).
CC {ECO:0000269|PubMed:3137579, ECO:0000303|PubMed:16895553,
CC ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked.
CC {ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Note=During
CC differentiation, B-lymphocytes switch from expression of membrane-bound
CC IgM to secretion of IgM.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Secreted;
CC IsoId=P01871-1; Sequence=Displayed;
CC Name=2; Synonyms=Membrane-bound;
CC IsoId=P01871-2; Sequence=VSP_034488;
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHM*04. {ECO:0000305}.
CC -!- DISEASE: Agammaglobulinemia 1, autosomal recessive (AGM1) [MIM:601495]:
CC A primary immunodeficiency characterized by profoundly low or absent
CC serum antibodies and low or absent circulating B cells due to an early
CC block of B-cell development. Affected individuals develop severe
CC infections in the first years of life. {ECO:0000269|PubMed:8890099}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- CAUTION: For an example of a full-length immunoglobulin mu heavy chain
CC see AC P0DOX6. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33065.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA33069.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA33071.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA34971.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE82013.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE82014.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=IGHMbase; Note=IGHM mutation db;
CC URL="http://structure.bmc.lu.se/idbase/IGHMbase/";
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DR EMBL; X14940; CAE82013.1; ALT_INIT; Genomic_DNA.
DR EMBL; X14940; CAE82014.1; ALT_INIT; Genomic_DNA.
DR EMBL; X14940; CAA33069.1; ALT_INIT; Genomic_DNA.
DR EMBL; X14940; CAA33070.1; -; Genomic_DNA.
DR EMBL; X14940; CAA33071.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X14939; CAA33065.1; ALT_INIT; Genomic_DNA.
DR EMBL; X17115; CAA34971.1; ALT_INIT; mRNA.
DR EMBL; X57086; CAB37838.1; -; mRNA.
DR EMBL; AC244226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC246787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC247036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K01310; AAB59422.1; -; Genomic_DNA.
DR PIR; A02163; MHHUBT.
DR PIR; S14683; S14683.
DR PIR; S16510; MHHUM.
DR PDB; 1HEZ; X-ray; 2.70 A; B/D=1-104.
DR PDB; 2AGJ; X-ray; 2.60 A; H=1-105.
DR PDB; 2RCJ; X-ray; -; C/D/G/H/K/L/O/P/S/T=1-326.
DR PDB; 6KXS; EM; 3.40 A; A/B/C/D/E/F/G/H/K/L=106-453.
DR PDB; 7K0C; EM; 3.30 A; A/B/E/F/G/H/I/J/K/L=103-453.
DR PDBsum; 1HEZ; -.
DR PDBsum; 2AGJ; -.
DR PDBsum; 2RCJ; -.
DR PDBsum; 6KXS; -.
DR PDBsum; 7K0C; -.
DR AlphaFoldDB; P01871; -.
DR SMR; P01871; -.
DR ComplexPortal; CPX-6911; IgM - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6922; IgM - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6923; IgM - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6925; IgM - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6926; IgM - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6927; IgM - Ig lambda 7 immunoglobulin complex, constant regions.
DR CORUM; P01871; -.
DR IntAct; P01871; 68.
DR MINT; P01871; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR IMGT_GENE-DB; IGHM; -.
DR CarbonylDB; P01871; -.
DR GlyConnect; 280; 204 N-Linked glycans (6 sites).
DR GlyGen; P01871; 7 sites, 195 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P01871; -.
DR PhosphoSitePlus; P01871; -.
DR SwissPalm; P01871; -.
DR BioMuta; IGHM; -.
DR DMDM; 193806374; -.
DR UCD-2DPAGE; P01871; -.
DR CPTAC; non-CPTAC-2676; -.
DR jPOST; P01871; -.
DR MassIVE; P01871; -.
DR PeptideAtlas; P01871; -.
DR PRIDE; P01871; -.
DR ProteomicsDB; 51498; -. [P01871-1]
DR ProteomicsDB; 51499; -. [P01871-2]
DR ABCD; P01871; 17 sequenced antibodies.
DR Ensembl; ENST00000390559.6; ENSP00000375001.2; ENSG00000211899.10. [P01871-1]
DR Ensembl; ENST00000626472.2; ENSP00000485962.2; ENSG00000282657.3. [P01871-1]
DR Ensembl; ENST00000637539.2; ENSP00000490253.1; ENSG00000211899.10. [P01871-2]
DR UCSC; uc059gdp.1; human.
DR GeneCards; IGHM; -.
DR HGNC; HGNC:5541; IGHM.
DR HPA; ENSG00000211899; Group enriched (intestine, lymphoid tissue).
DR MalaCards; IGHM; -.
DR MIM; 147020; gene.
DR MIM; 601495; phenotype.
DR neXtProt; NX_P01871; -.
DR OpenTargets; ENSG00000211899; -.
DR Orphanet; 33110; Autosomal agammaglobulinemia.
DR VEuPathDB; HostDB:ENSG00000211899; -.
DR GeneTree; ENSGT00940000161491; -.
DR InParanoid; P01871; -.
DR OMA; LYFVHST; -.
DR PhylomeDB; P01871; -.
DR PathwayCommons; P01871; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P01871; -.
DR SIGNOR; P01871; -.
DR ChiTaRS; IGHM; human.
DR EvolutionaryTrace; P01871; -.
DR Pharos; P01871; Tbio.
DR PRO; PR:P01871; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01871; protein.
DR Bgee; ENSG00000211899; Expressed in spleen and 113 other tissues.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0071757; C:hexameric IgM immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071753; C:IgM immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 4.
DR SMART; SM00407; IGc1; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin; Immunoglobulin domain; Membrane; Reference proteome;
KW Secreted; Transmembrane.
FT CHAIN <1..453
FT /note="Immunoglobulin heavy constant mu"
FT /id="PRO_0000153619"
FT DOMAIN 6..102
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 111..211
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 229..319
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 329..430
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..105
FT /note="CH1"
FT REGION 106..217
FT /note="CH2"
FT REGION 218..323
FT /note="CH3"
FT REGION 324..452
FT /note="CH4"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16422668, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0007744|PDB:2AGJ"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:4742735"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT /id="CAR_000219"
FT DISULFID 14
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 28..88
FT /evidence="ECO:0000269|PubMed:11587642,
FT ECO:0000269|PubMed:16422668, ECO:0007744|PDB:1HEZ,
FT ECO:0007744|PDB:2AGJ"
FT DISULFID 134..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 214
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 244..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 291
FT /note="Interchain (with heavy chain of another subunit)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 351..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 452
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT VAR_SEQ 434..453
FT /note="GKPTLYNVSLVMSDTAGTCY -> EGEVSADEEGFENLWATASTFIVLFLLS
FT LFYSTTVTLFKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2115996,
FT ECO:0000303|PubMed:6795593"
FT /id="VSP_034488"
FT VARIANT 40
FT /note="F -> L (in IMGT allele IGHM*01)"
FT /evidence="ECO:0000269|PubMed:2505237"
FT /id="VAR_077893"
FT VARIANT 191
FT /note="G -> S (in IMGT allele IGHM*03)"
FT /evidence="ECO:0000269|PubMed:2115996"
FT /id="VAR_003903"
FT VARIANT 215
FT /note="V -> G (in dbSNP:rs12365)"
FT /evidence="ECO:0000269|PubMed:6425189"
FT /id="VAR_003904"
FT VARIANT 414
FT /note="Missing (in IMGT allele IGHM*01 IMGT allele
FT IGHM*02)"
FT /evidence="ECO:0000269|PubMed:2505237,
FT ECO:0000269|PubMed:6795593"
FT /id="VAR_077894"
FT VARIANT 418
FT /note="E -> D (in IMGT allele IGHM*02)"
FT /evidence="ECO:0000269|PubMed:6795593"
FT /id="VAR_077895"
FT CONFLICT 128
FT /note="R -> RS (in Ref. 5; CAA34971)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="Q -> E (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..165
FT /note="QVQ -> EVE (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="T -> I (in Ref. 6; CAB37838)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="N -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="N -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1HEZ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1HEZ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2AGJ"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2AGJ"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:7K0C"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:7K0C"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6KXS"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6KXS"
FT TURN 338..342
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 343..359
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:7K0C"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:6KXS"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:7K0C"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:7K0C"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:7K0C"
FT CONFLICT P01871-2:438
FT /note="S -> N (in Ref. 10; AAB59422)"
FT /evidence="ECO:0000305"
FT CONFLICT P01871-2:440
FT /note="D -> E (in Ref. 10; AAB59422)"
FT /evidence="ECO:0000305"
FT CONFLICT P01871-2:449
FT /note="A -> T (in Ref. 10; AAB59422)"
FT /evidence="ECO:0000305"
FT CONFLICT P01871-2:472..474
FT /note="KVK -> K (in Ref. 10; AAB59422 and 4; CAA33065)"
FT /evidence="ECO:0000305"
SQ 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
