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Ig mu chain C region

 IGHM_MOUSE              Reviewed;         454 AA.
P01872; P01873;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
22-NOV-2017, entry version 143.
RecName: Full=Ig mu chain C region;
Name=Ighm; Synonyms=Igh-6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
PROTEIN SEQUENCE (MYELOMA MOPC 104E).
TISSUE=Myeloma;
PubMed=111247; DOI=10.1073/pnas.76.6.2932;
Kehry M.R., Sibley C.H., Fuhrman J.S., Schilling J.W., Hood L.E.;
"Amino acid sequence of a mouse immunoglobulin mu chain.";
Proc. Natl. Acad. Sci. U.S.A. 76:2932-2936(1979).
[2]
SEQUENCE REVISION (MYELOMA MOPC 104E).
PubMed=6816276; DOI=10.1021/bi00265a006;
Kehry M.R., Fuhrman J.S., Schilling J.W., Rogers J., Sibley C.H.,
Hood L.E.;
"Complete amino acid sequence of a mouse mu chain: homology among
heavy chain constant region domains.";
Biochemistry 21:5415-5424(1982).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 409-454 (ISOFORM 2).
STRAIN=BALB/cJ; TISSUE=Myeloma;
PubMed=6771019; DOI=10.1016/0092-8674(80)90616-9;
Rogers J., Early P., Carter C., Calame K., Bond M., Hood L., Wall R.;
"Two mRNAs with different 3' ends encode membrane-bound and secreted
forms of immunoglobulin mu chain.";
Cell 20:303-312(1980).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (MYELOMA TEPC183).
STRAIN=BALB/cJ; TISSUE=Myeloma;
PubMed=6260591; DOI=10.1016/0378-1119(80)90017-7;
Auffray C., Rougeon F.;
"Nucleotide sequence of a cloned cDNA corresponding to secreted mu
chain of mouse immunoglobulin.";
Gene 12:77-86(1980).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=6255422; DOI=10.1093/nar/8.17.3933;
Kawakami T., Takahashi N., Honjo T.;
"Complete nucleotide sequence of mouse immunoglobulin mu gene and
comparison with other immunoglobulin heavy chain genes.";
Nucleic Acids Res. 8:3933-3945(1980).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=6795090; DOI=10.1016/0378-1119(81)90102-5;
Goldberg G.I., Vanin E.F., Zrolka A.M., Blattner F.R.;
"Sequence of the gene for the constant region of the mu chain of
Balb/c mouse immunoglobulin.";
Gene 15:33-42(1981).
[7]
GLYCOSYLATION AT ASN-45; ASN-210; ASN-242; ASN-257 AND ASN-280.
PubMed=12654314; DOI=10.1016/S0003-2697(02)00693-0;
Wang F., Nakouzi A., Angeletti R.H., Casadevall A.;
"Site-specific characterization of the N-linked oligosaccharides of a
murine immunoglobulin M by high-performance liquid
chromatography/electrospray mass spectrometry.";
Anal. Biochem. 314:266-280(2003).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 428-454, AND ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2).
STRAIN=BALB/cJ;
PubMed=6771020; DOI=10.1016/0092-8674(80)90617-0;
Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L.;
"Two mRNAs can be produced from a single immunoglobulin mu gene by
alternative RNA processing pathways.";
Cell 20:313-319(1980).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 103-217, STRUCTURE BY NMR OF
222-321, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-215; CYS-292 AND
CYS-453.
PubMed=23733956; DOI=10.1073/pnas.1300547110;
Muller R., Grawert M.A., Kern T., Madl T., Peschek J., Sattler M.,
Groll M., Buchner J.;
"High-resolution structures of the IgM Fc domains reveal principles of
its hexamer formation.";
Proc. Natl. Acad. Sci. U.S.A. 110:10183-10188(2013).
-!- FUNCTION: 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 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Immunoglobulin (Ig) molecules consist of two chains, one
heavy chain (which can be alpha, delta, epsilon, gamma or mu) and
one light chain (which can be kappa or lambda) each consisting of
a variable and a constant region. An IgM molecule contains thus a
mu heavy chain combined with either a kappa or a lambda light
chains (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-645833, EBI-645833;
P25918:Cd19; NbExp=3; IntAct=EBI-645833, EBI-644463;
P19437:Ms4a1; NbExp=3; IntAct=EBI-645833, EBI-10683749;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000305}.
Note=During differentiation, B-lymphocytes switch from expression
of membrane-bound IgM to secretion of IgM. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Secreted;
IsoId=P01872-1; Sequence=Displayed;
Name=2; Synonyms=Membrane-bound;
IsoId=P01872-2; Sequence=VSP_053388;
-----------------------------------------------------------------------
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EMBL; V00821; CAA24202.1; -; mRNA.
EMBL; V00827; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; J00443; AAB59650.1; -; Genomic_DNA.
EMBL; J00444; AAB59650.1; JOINED; Genomic_DNA.
EMBL; J00443; AAB59651.1; -; Genomic_DNA.
EMBL; J00444; AAB59651.1; JOINED; Genomic_DNA.
PIR; A02166; MHMS.
PIR; A02167; MHMSM.
UniGene; Mm.304472; -.
UniGene; Mm.313488; -.
UniGene; Mm.342177; -.
UniGene; Mm.428442; -.
UniGene; Mm.435580; -.
UniGene; Mm.436922; -.
UniGene; Mm.439101; -.
PDB; 4BA8; NMR; -; A=222-321.
PDB; 4JVU; X-ray; 1.30 A; A/B=103-217.
PDB; 4JVW; X-ray; 2.00 A; A/B/C/D=324-436.
PDBsum; 4BA8; -.
PDBsum; 4JVU; -.
PDBsum; 4JVW; -.
ProteinModelPortal; P01872; -.
SMR; P01872; -.
IntAct; P01872; 5.
iPTMnet; P01872; -.
PhosphoSitePlus; P01872; -.
EPD; P01872; -.
MaxQB; P01872; -.
PeptideAtlas; P01872; -.
PRIDE; P01872; -.
MGI; MGI:96448; Ighm.
HOVERGEN; HBG005814; -.
PRO; PR:P01872; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_IGH-6; -.
GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0042571; C:immunoglobulin complex, circulating; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0034987; F:immunoglobulin receptor binding; IPI:AgBase.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
GO; GO:0002344; P:B cell affinity maturation; IMP:MGI.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:MGI.
GO; GO:0016064; P:immunoglobulin mediated immune response; IDA:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
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; IDA:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0022604; P:regulation of cell morphogenesis; IMP:MGI.
GO; GO:0002637; P:regulation of immunoglobulin production; IMP:MGI.
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; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin C region; Immunoglobulin domain; Membrane;
Reference proteome; Secreted; Transmembrane; Transmembrane helix.
CHAIN <1 454 Ig mu chain C region.
/FTId=PRO_0000153623.
REGION <1 104 CH1.
REGION 105 216 CH2.
REGION 217 323 CH3.
REGION 324 454 Important for oligomerization.
REGION 324 435 CH4.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12654314,
ECO:0000269|PubMed:6816276}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12654314,
ECO:0000269|PubMed:6816276}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12654314,
ECO:0000269|PubMed:6816276}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12654314}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12654314,
ECO:0000269|PubMed:6816276}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6816276}.
DISULFID 13 13 Interchain (with light chain).
{ECO:0000305|PubMed:23733956}.
DISULFID 27 88 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:111247,
ECO:0000269|PubMed:23733956}.
DISULFID 135 198 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23733956}.
DISULFID 215 215 Interchain (with heavy chain).
{ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23733956}.
DISULFID 245 304 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23733956}.
DISULFID 292 292 Interchain (with heavy chain).
{ECO:0000305|PubMed:23733956}.
DISULFID 352 414 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23733956}.
DISULFID 453 453 Interchain (with heavy chain).
{ECO:0000305|PubMed:23733956}.
VAR_SEQ 435 454 GKPTLYNVSLIMSDTGGTCY -> EGEVNAEEEGFENLWTT
ASTFIVLFLLSLFYSTTVTLFKVK (in isoform 2).
{ECO:0000303|PubMed:6771019}.
/FTId=VSP_053388.
VARIANT 77 77 S -> N (in MOPC 104E).
VARIANT 100 100 H -> Q (in MOPC 104E).
VARIANT 225 225 T -> N (in TEPC183 and MOPC 104E).
VARIANT 257 257 N -> S (in TEPC183).
VARIANT 257 257 N -> T (in MOPC 104E).
VARIANT 367 367 L -> K (in TEPC183 and MOPC 104E;
requires 2 nucleotide substitutions).
MUTAGEN 215 215 C->S: Impairs dimerization.
{ECO:0000269|PubMed:23733956}.
MUTAGEN 292 292 C->S: Impairs dimerization.
{ECO:0000269|PubMed:23733956}.
MUTAGEN 453 453 C->S: Impairs dimerization and
oligomerization.
{ECO:0000269|PubMed:23733956}.
NON_TER 1 1
STRAND 112 117 {ECO:0000244|PDB:4JVU}.
STRAND 124 128 {ECO:0000244|PDB:4JVU}.
STRAND 130 143 {ECO:0000244|PDB:4JVU}.
STRAND 146 151 {ECO:0000244|PDB:4JVU}.
STRAND 158 162 {ECO:0000244|PDB:4JVU}.
STRAND 177 186 {ECO:0000244|PDB:4JVU}.
HELIX 187 191 {ECO:0000244|PDB:4JVU}.
STRAND 196 202 {ECO:0000244|PDB:4JVU}.
STRAND 205 211 {ECO:0000244|PDB:4JVU}.
STRAND 224 228 {ECO:0000244|PDB:4BA8}.
HELIX 232 238 {ECO:0000244|PDB:4BA8}.
STRAND 239 248 {ECO:0000244|PDB:4BA8}.
STRAND 257 262 {ECO:0000244|PDB:4BA8}.
STRAND 280 283 {ECO:0000244|PDB:4BA8}.
STRAND 285 291 {ECO:0000244|PDB:4BA8}.
HELIX 293 297 {ECO:0000244|PDB:4BA8}.
STRAND 302 307 {ECO:0000244|PDB:4BA8}.
STRAND 309 313 {ECO:0000244|PDB:4BA8}.
STRAND 315 319 {ECO:0000244|PDB:4BA8}.
STRAND 331 335 {ECO:0000244|PDB:4JVW}.
HELIX 339 342 {ECO:0000244|PDB:4JVW}.
STRAND 345 360 {ECO:0000244|PDB:4JVW}.
STRAND 363 368 {ECO:0000244|PDB:4JVW}.
HELIX 375 377 {ECO:0000244|PDB:4JVW}.
STRAND 393 402 {ECO:0000244|PDB:4JVW}.
HELIX 403 407 {ECO:0000244|PDB:4JVW}.
STRAND 412 417 {ECO:0000244|PDB:4JVW}.
STRAND 424 431 {ECO:0000244|PDB:4JVW}.
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


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