IGM_HUMAN
ID IGM_HUMAN Reviewed; 576 AA.
AC P0DOX6;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Immunoglobulin mu heavy chain {ECO:0000305};
DE AltName: Full=Immunoglobulin mu heavy chain OU {ECO:0000305|PubMed:4742735};
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, DISULFIDE BONDS, GLYCOSYLATION AT ASN-170: ASN-332;
RP ASN-395; ASN-402 AND ASN-563, AND PYROGLUTAMATE FORMATION AT GLN-1.
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 [2]
RP REVIEW ON FUNCTION AND SUBUNIT.
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 [3]
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 [4]
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 [5]
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).
CC -!- FUNCTION: Immunoglobulins, also known as antibodies, are membrane-bound
CC or 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:20176268, PubMed:17576170).
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:16895553).
CC {ECO:0000303|PubMed:16895553, ECO:0000303|PubMed:17576170,
CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked (PubMed:20176268). It is
CC found almost exclusively as a homopentamer in the serum. Membrane-bound
CC IgM molecules are non-covalently associated with heterodimer of CD79A
CC and CD79B (PubMed:16895553). {ECO:0000303|PubMed:16895553,
CC ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}. Cell membrane
CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- CAUTION: This sequence is an example of a full-length immunoglobulin mu
CC heavy chain. {ECO:0000305}.
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DR AlphaFoldDB; P0DOX6; -.
DR SMR; P0DOX6; -.
DR iPTMnet; P0DOX6; -.
DR jPOST; P0DOX6; -.
DR PRIDE; P0DOX6; -.
DR SIGNOR; P0DOX6; -.
DR Pharos; P0DOX6; Tdark.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 5.
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 InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 4.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 4.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS00290; IG_MHC; 3.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Pyrrolidone carboxylic acid; Repeat;
KW Secreted.
FT CHAIN 1..576
FT /note="Immunoglobulin mu heavy chain"
FT /id="PRO_0000439286"
FT DOMAIN 1..97
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 132..212
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 236..334
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 352..442
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 452..553
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..124
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305|PubMed:4742735"
FT REGION 125..576
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305|PubMed:4742735"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 22..97
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 140
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 153..212
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 259..320
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 337
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 367..426
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 474..536
FT /evidence="ECO:0000269|PubMed:4742735"
FT DISULFID 575
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:4742735"
SQ SEQUENCE 576 AA; 63486 MW; CCC81DBF4164E0BD CRC64;
QVTLTESGPA LVKPKQPLTL TCTFSGFSLS TSRMRVSWIR RPPGKALEWL ARIDDDDKFY
WSTSLRTRLS ISKNDSKNQV VLIMINVNPV DTATYYCARV VNSVMAGYYY YYMDVWGKGT
TVTVSSGSAS APTLFPLVSC ENSNPSSTVA VGCLAQDFLP DSITFSWKYN QSQKISSTRG
FPSVLRGGKY AATSQVLLPS KDVMQGTDEH VCKWVQHPNG NKQKNVPLPV IAELPPKVSV
FVPPRDGFFG NPRKSKLICQ ATGFSPRQVW SLREGKQVGS GVTTDQVQAE AKESGPTTYK
VTSTLTIKES DWLGESMFTC RVDHRGLTFQ QNASSMCVPD QDTAIRVFAI PPSFASIFLT
KSTKLTCLVT DLTTYDSVTI SWTREENGAV KTHTNISESH PNATFSAVGE ASICEDDDWS
GERFTCTVTH TDLPSPLKQT ISRPKGVALH RPDVYLLPPA REQLNLRESA TITCLVTGFS
PADVFVQWMQ RGEPLSPEKY VTSAPMPEPQ APGRYFAHSI LTVSEEEWNT GQTYTCVVAH
EALPNRVTER TVDKSTGKPT LYNVSLVMSD TAGTCY
