IGHM_MOUSE
ID IGHM_MOUSE Reviewed; 454 AA.
AC P01872; P01873;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Immunoglobulin heavy constant mu;
DE Contains:
DE RecName: Full=Mu' chain {ECO:0000303|PubMed:29323348};
DE AltName: Full=55 kDa mu' chain {ECO:0000305|PubMed:29323348};
GN Name=Ighm; Synonyms=Igh-6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP PROTEIN SEQUENCE (MYELOMA MOPC 104E).
RC TISSUE=Myeloma;
RX PubMed=111247; DOI=10.1073/pnas.76.6.2932;
RA Kehry M.R., Sibley C.H., Fuhrman J.S., Schilling J.W., Hood L.E.;
RT "Amino acid sequence of a mouse immunoglobulin mu chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:2932-2936(1979).
RN [2]
RP SEQUENCE REVISION (MYELOMA MOPC 104E).
RX PubMed=6816276; DOI=10.1021/bi00265a006;
RA Kehry M.R., Fuhrman J.S., Schilling J.W., Rogers J., Sibley C.H.,
RA Hood L.E.;
RT "Complete amino acid sequence of a mouse mu chain: homology among heavy
RT chain constant region domains.";
RL Biochemistry 21:5415-5424(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 409-454 (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Myeloma;
RX PubMed=6771019; DOI=10.1016/0092-8674(80)90616-9;
RA Rogers J., Early P., Carter C., Calame K., Bond M., Hood L., Wall R.;
RT "Two mRNAs with different 3' ends encode membrane-bound and secreted forms
RT of immunoglobulin mu chain.";
RL Cell 20:303-312(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (MYELOMA TEPC183).
RC STRAIN=BALB/cJ; TISSUE=Myeloma;
RX PubMed=6260591; DOI=10.1016/0378-1119(80)90017-7;
RA Auffray C., Rougeon F.;
RT "Nucleotide sequence of a cloned cDNA corresponding to secreted mu chain of
RT mouse immunoglobulin.";
RL Gene 12:77-86(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=6255422; DOI=10.1093/nar/8.17.3933;
RA Kawakami T., Takahashi N., Honjo T.;
RT "Complete nucleotide sequence of mouse immunoglobulin mu gene and
RT comparison with other immunoglobulin heavy chain genes.";
RL Nucleic Acids Res. 8:3933-3945(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=6795090; DOI=10.1016/0378-1119(81)90102-5;
RA Goldberg G.I., Vanin E.F., Zrolka A.M., Blattner F.R.;
RT "Sequence of the gene for the constant region of the mu chain of Balb/c
RT mouse immunoglobulin.";
RL Gene 15:33-42(1981).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 428-454, AND ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RX PubMed=6771020; DOI=10.1016/0092-8674(80)90617-0;
RA Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L.;
RT "Two mRNAs can be produced from a single immunoglobulin mu gene by
RT alternative RNA processing pathways.";
RL Cell 20:313-319(1980).
RN [8]
RP PROTEIN SEQUENCE OF 97-108 (MU' CHAIN), IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF ASN-96, AND PROCESSING CLEAVAGE.
RX PubMed=29323348; DOI=10.1038/s41598-017-19003-4;
RA Klaus T., Stalinska K., Czaplicki D., Mak P., Skupien-Rabian B.,
RA Kedracka-Krok S., Wiatrowska K., Bzowska M., Machula M., Bereta J.;
RT "Mouse Antibody of IgM Class is Prone to Non-Enzymatic Cleavage between CH1
RT and CH2 Domains.";
RL Sci. Rep. 8:519-519(2018).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=2415657; DOI=10.1084/jem.162.6.1862;
RA Marks R., Bosma M.J.;
RT "Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack
RT variable regions.";
RL J. Exp. Med. 162:1862-1877(1985).
RN [10]
RP GLYCOSYLATION AT ASN-45; ASN-210; ASN-242; ASN-257 AND ASN-280.
RX PubMed=12654314; DOI=10.1016/s0003-2697(02)00693-0;
RA Wang F., Nakouzi A., Angeletti R.H., Casadevall A.;
RT "Site-specific characterization of the N-linked oligosaccharides of a
RT murine immunoglobulin M by high-performance liquid
RT chromatography/electrospray mass spectrometry.";
RL Anal. Biochem. 314:266-280(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 103-217, STRUCTURE BY NMR OF
RP 222-321, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-215; CYS-292 AND CYS-453.
RX PubMed=23733956; DOI=10.1073/pnas.1300547110;
RA Muller R., Grawert M.A., Kern T., Madl T., Peschek J., Sattler M.,
RA Groll M., Buchner J.;
RT "High-resolution structures of the IgM Fc domains reveal principles of its
RT hexamer formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10183-10188(2013).
CC -!- FUNCTION: IgM antibodies play an important role in primary defense
CC mechanisms. They have been shown to be involved in early recognition of
CC external invaders like bacteria and viruses, cellular waste and
CC modified self, as well as in recognition and elimination of
CC precancerous and cancerous lesions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Immunoglobulin (Ig) molecules consist of two chains, one heavy
CC chain (which can be alpha, delta, epsilon, gamma or mu) and one light
CC chain (which can be kappa or lambda) each consisting of a variable and
CC a constant region. An IgM molecule contains thus a mu heavy chain
CC combined with either a kappa or a lambda light chains (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P01872; P01872: Ighm; NbExp=9; IntAct=EBI-645833, EBI-645833;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000305}. Note=During
CC differentiation, B-lymphocytes switch from expression of membrane-bound
CC IgM to secretion of IgM. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Secreted;
CC IsoId=P01872-1; Sequence=Displayed;
CC Name=2; Synonyms=Membrane-bound;
CC IsoId=P01872-2; Sequence=VSP_053388;
CC -!- TISSUE SPECIFICITY: Mu' chain is expressed in bone marrow.
CC {ECO:0000269|PubMed:2415657}.
CC -!- PTM: Cleaved by a non-enzymatic process after Asn-96, yielding a
CC glycosylated protein of 55 kDa. The process is induced by other
CC proteins, and requires neutral or alkaline pH.
CC {ECO:0000269|PubMed:29323348}.
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DR EMBL; V00821; CAA24202.1; -; mRNA.
DR EMBL; V00827; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; J00443; AAB59650.1; -; Genomic_DNA.
DR EMBL; J00444; AAB59650.1; JOINED; Genomic_DNA.
DR EMBL; J00443; AAB59651.1; -; Genomic_DNA.
DR EMBL; J00444; AAB59651.1; JOINED; Genomic_DNA.
DR PIR; A02166; MHMS.
DR PIR; A02167; MHMSM.
DR PDB; 4BA8; NMR; -; A=222-321.
DR PDB; 4JVU; X-ray; 1.30 A; A/B=103-217.
DR PDB; 4JVW; X-ray; 2.00 A; A/B/C/D=324-436.
DR PDBsum; 4BA8; -.
DR PDBsum; 4JVU; -.
DR PDBsum; 4JVW; -.
DR AlphaFoldDB; P01872; -.
DR SMR; P01872; -.
DR IntAct; P01872; 6.
DR MINT; P01872; -.
DR CarbonylDB; P01872; -.
DR GlyConnect; 2379; 8 N-Linked glycans (1 site).
DR GlyGen; P01872; 6 sites, 7 N-linked glycans (1 site).
DR iPTMnet; P01872; -.
DR PhosphoSitePlus; P01872; -.
DR CPTAC; non-CPTAC-3919; -.
DR EPD; P01872; -.
DR jPOST; P01872; -.
DR MaxQB; P01872; -.
DR PeptideAtlas; P01872; -.
DR PRIDE; P01872; -.
DR ProteomicsDB; 269465; -. [P01872-1]
DR ProteomicsDB; 269466; -. [P01872-2]
DR MGI; MGI:96448; Ighm.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR ChiTaRS; Ighm; mouse.
DR PRO; PR:P01872; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01872; protein.
DR GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0071757; C:hexameric IgM immunoglobulin complex; ISO:MGI.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0071756; C:pentameric IgM immunoglobulin complex; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IPI:AgBase.
DR GO; GO:0042834; F:peptidoglycan binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR GO; GO:0042113; P:B cell activation; IDA:MGI.
DR GO; GO:0002344; P:B cell affinity maturation; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IDA:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:MGI.
DR GO; GO:0002637; P:regulation of immunoglobulin production; IMP:MGI.
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; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..454
FT /note="Immunoglobulin heavy constant mu"
FT /id="PRO_0000153623"
FT CHAIN 97..454
FT /note="Mu' chain"
FT /evidence="ECO:0000269|PubMed:29323348"
FT /id="PRO_0000443951"
FT REGION <1..104
FT /note="CH1"
FT REGION 105..216
FT /note="CH2"
FT REGION 217..323
FT /note="CH3"
FT REGION 324..454
FT /note="Important for oligomerization"
FT REGION 324..435
FT /note="CH4"
FT SITE 96..97
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:29323348"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12654314,
FT ECO:0000269|PubMed:6816276"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12654314,
FT ECO:0000269|PubMed:6816276"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12654314,
FT ECO:0000269|PubMed:6816276"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12654314"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12654314,
FT ECO:0000269|PubMed:6816276"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6816276"
FT DISULFID 13
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000305|PubMed:23733956"
FT DISULFID 27..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:111247, ECO:0000269|PubMed:23733956"
FT DISULFID 135..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23733956"
FT DISULFID 215
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23733956"
FT DISULFID 245..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23733956"
FT DISULFID 292
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000305|PubMed:23733956"
FT DISULFID 352..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23733956"
FT DISULFID 453
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000305|PubMed:23733956"
FT VAR_SEQ 435..454
FT /note="GKPTLYNVSLIMSDTGGTCY -> EGEVNAEEEGFENLWTTASTFIVLFLLS
FT LFYSTTVTLFKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:6771019"
FT /id="VSP_053388"
FT VARIANT 77
FT /note="S -> N (in MOPC 104E)"
FT VARIANT 100
FT /note="H -> Q (in MOPC 104E)"
FT VARIANT 225
FT /note="T -> N (in TEPC183 and MOPC 104E)"
FT VARIANT 257
FT /note="N -> S (in TEPC183)"
FT VARIANT 257
FT /note="N -> T (in MOPC 104E)"
FT VARIANT 367
FT /note="L -> K (in TEPC183 and MOPC 104E; requires 2
FT nucleotide substitutions)"
FT MUTAGEN 96
FT /note="N->A: Abolishes formation of 55 kDa cleavage
FT product."
FT /evidence="ECO:0000269|PubMed:29323348"
FT MUTAGEN 215
FT /note="C->S: Impairs dimerization."
FT /evidence="ECO:0000269|PubMed:23733956"
FT MUTAGEN 292
FT /note="C->S: Impairs dimerization."
FT /evidence="ECO:0000269|PubMed:23733956"
FT MUTAGEN 453
FT /note="C->S: Impairs dimerization and oligomerization."
FT /evidence="ECO:0000269|PubMed:23733956"
FT NON_TER 1
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:4JVU"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4JVU"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4BA8"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:4BA8"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4BA8"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:4JVW"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4JVW"
FT STRAND 345..360
FT /evidence="ECO:0007829|PDB:4JVW"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4JVW"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4JVW"
FT STRAND 393..402
FT /evidence="ECO:0007829|PDB:4JVW"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:4JVW"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:4JVW"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:4JVW"
SQ SEQUENCE 454 AA; 49972 MW; EBCCA6E8569AEEC5 CRC64;
SQSFPNVFPL VSCESPLSDK NLVAMGCLAR DFLPSTISFT WNYQNNTEVI QGIRTFPTLR
TGGKYLATSQ VLLSPKSILE GSDEYLVCKI HYGGKNRDLH VPIPAVAEMN PNVNVFVPPR
DGFSGPAPRK SKLICEATNF TPKPITVSWL KDGKLVESGF TTDPVTIENK GSTPQTYKVI
STLTISEIDW LNLNVYTCRV DHRGLTFLKN VSSTCAASPS TDILTFTIPP SFADIFLSKS
ANLTCLVSNL ATYETLNISW ASQSGEPLET KIKIMESHPN GTFSAKGVAS VCVEDWNNRK
EFVCTVTHRD LPSPQKKFIS KPNEVHKHPP AVYLLPPARE QLNLRESATV TCLVKGFSPA
DISVQWLQRG QLLPQEKYVT SAPMPEPGAP GFYFTHSILT VTEEEWNSGE TYTCVVGHEA
LPHLVTERTV DKSTGKPTLY NVSLIMSDTG GTCY
