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Protein

Ig mu chain C region

Gene

Ighm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • antigen binding Source: MGI
  • identical protein binding Source: IntAct
  • immunoglobulin receptor binding Source: AgBase
  • transmembrane signaling receptor activity Source: MGI

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • antigen processing and presentation Source: MGI
  • B cell receptor signaling pathway Source: MGI
  • complement activation, classical pathway Source: GO_Central
  • defense response to Gram-negative bacterium Source: MGI
  • early endosome to late endosome transport Source: MGI
  • humoral immune response mediated by circulating immunoglobulin Source: MGI
  • immunoglobulin mediated immune response Source: MGI
  • innate immune response Source: GO_Central
  • phagocytosis, engulfment Source: GO_Central
  • phagocytosis, recognition Source: GO_Central
  • positive regulation of B cell activation Source: MGI
  • positive regulation of B cell proliferation Source: MGI
  • positive regulation of endocytosis Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig mu chain C region
Gene namesi
Name:Ighm
Synonyms:Igh-6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96448. Ighm.

Subcellular locationi

Isoform 1 :
  • Secreted Curated

  • Note: During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM.Curated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151C → S: Impairs dimerization. 1 Publication
Mutagenesisi292 – 2921C → S: Impairs dimerization. 1 Publication
Mutagenesisi453 – 4531C → S: Impairs dimerization and oligomerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 454›454Ig mu chain C regionPRO_0000153623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi13 – 13Interchain (with light chain)1 Publication
Disulfide bondi27 ↔ 88PROSITE-ProRule annotation2 Publications
Glycosylationi45 – 451N-linked (GlcNAc...)2 Publications
Disulfide bondi135 ↔ 198PROSITE-ProRule annotation1 Publication
Glycosylationi210 – 2101N-linked (GlcNAc...)2 Publications
Disulfide bondi215 – 215Interchain (with heavy chain)PROSITE-ProRule annotation1 Publication
Glycosylationi242 – 2421N-linked (GlcNAc...)2 Publications
Disulfide bondi245 ↔ 304PROSITE-ProRule annotation1 Publication
Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
Glycosylationi280 – 2801N-linked (GlcNAc...)2 Publications
Disulfide bondi292 – 292Interchain (with heavy chain)1 Publication
Disulfide bondi352 ↔ 414PROSITE-ProRule annotation1 Publication
Glycosylationi441 – 4411N-linked (GlcNAc...)1 Publication
Disulfide bondi453 – 453Interchain (with heavy chain)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01872.
MaxQBiP01872.
PeptideAtlasiP01872.
PRIDEiP01872.

Expressioni

Gene expression databases

CleanExiMM_IGH-6.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-645833,EBI-645833
Cd19P259183EBI-645833,EBI-644463
Ms4a1P194373EBI-645833,EBI-10683749

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • immunoglobulin receptor binding Source: AgBase

Protein-protein interaction databases

IntActiP01872. 5 interactions.

Structurei

Secondary structure

1
454
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi112 – 1176Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi130 – 14314Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi177 – 18610Combined sources
Helixi187 – 1915Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi205 – 2117Combined sources
Beta strandi224 – 2285Combined sources
Helixi232 – 2387Combined sources
Beta strandi239 – 24810Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 2917Combined sources
Helixi293 – 2975Combined sources
Beta strandi302 – 3076Combined sources
Beta strandi309 – 3135Combined sources
Beta strandi315 – 3195Combined sources
Beta strandi331 – 3355Combined sources
Helixi339 – 3424Combined sources
Beta strandi345 – 36016Combined sources
Beta strandi363 – 3686Combined sources
Helixi375 – 3773Combined sources
Beta strandi393 – 40210Combined sources
Helixi403 – 4075Combined sources
Beta strandi412 – 4176Combined sources
Beta strandi424 – 4318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BA8NMR-A222-321[»]
4JVUX-ray1.30A/B103-217[»]
4JVWX-ray2.00A/B/C/D324-436[»]
ProteinModelPortaliP01872.
SMRiP01872. Positions 1-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni‹1 – 104›104CH1Add
BLAST
Regioni105 – 216112CH2Add
BLAST
Regioni217 – 323107CH3Add
BLAST
Regioni324 – 454131Important for oligomerizationAdd
BLAST
Regioni324 – 435112CH4Add
BLAST

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG005814.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 4 hits.
[Graphical view]
SMARTiSM00407. IGc1. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS00290. IG_MHC. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P01872-1) [UniParc]FASTAAdd to basket

Also known as: Secreted

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
SQSFPNVFPL VSCESPLSDK NLVAMGCLAR DFLPSTISFT WNYQNNTEVI
60 70 80 90 100
QGIRTFPTLR TGGKYLATSQ VLLSPKSILE GSDEYLVCKI HYGGKNRDLH
110 120 130 140 150
VPIPAVAEMN PNVNVFVPPR DGFSGPAPRK SKLICEATNF TPKPITVSWL
160 170 180 190 200
KDGKLVESGF TTDPVTIENK GSTPQTYKVI STLTISEIDW LNLNVYTCRV
210 220 230 240 250
DHRGLTFLKN VSSTCAASPS TDILTFTIPP SFADIFLSKS ANLTCLVSNL
260 270 280 290 300
ATYETLNISW ASQSGEPLET KIKIMESHPN GTFSAKGVAS VCVEDWNNRK
310 320 330 340 350
EFVCTVTHRD LPSPQKKFIS KPNEVHKHPP AVYLLPPARE QLNLRESATV
360 370 380 390 400
TCLVKGFSPA DISVQWLQRG QLLPQEKYVT SAPMPEPGAP GFYFTHSILT
410 420 430 440 450
VTEEEWNSGE TYTCVVGHEA LPHLVTERTV DKSTGKPTLY NVSLIMSDTG

GTCY
Length:454
Mass (Da):49,972
Last modified:February 1, 2005 - v2
Checksum:iEBCCA6E8569AEEC5
GO
Isoform 2 (identifier: P01872-2) [UniParc]FASTAAdd to basket

Also known as: Membrane-bound

The sequence of this isoform differs from the canonical sequence as follows:
     435-454: GKPTLYNVSLIMSDTGGTCY → EGEVNAEEEGFENLWTTASTFIVLFLLSLFYSTTVTLFKVK

Show »
Length:475
Mass (Da):52,527
Checksum:iF2163AD4517E1485
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771S → N in MOPC 104E.
Natural varianti100 – 1001H → Q in MOPC 104E.
Natural varianti225 – 2251T → N in TEPC183 and MOPC 104E.
Natural varianti257 – 2571N → S in TEPC183.
Natural varianti257 – 2571N → T in MOPC 104E.
Natural varianti367 – 3671L → K in TEPC183 and MOPC 104E; requires 2 nucleotide substitutions.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei435 – 45420GKPTL…GGTCY → EGEVNAEEEGFENLWTTAST FIVLFLLSLFYSTTVTLFKV K in isoform 2. 1 PublicationVSP_053388Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00821 mRNA. Translation: CAA24202.1.
V00827 mRNA. No translation available.
J00443, J00444 Genomic DNA. Translation: AAB59650.1.
J00443, J00444 Genomic DNA. Translation: AAB59651.1.
PIRiA02166. MHMS.
A02167. MHMSM.
UniGeneiMm.304472.
Mm.313488.
Mm.342177.
Mm.428442.
Mm.435580.
Mm.436922.
Mm.439101.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00821 mRNA. Translation: CAA24202.1.
V00827 mRNA. No translation available.
J00443, J00444 Genomic DNA. Translation: AAB59650.1.
J00443, J00444 Genomic DNA. Translation: AAB59651.1.
PIRiA02166. MHMS.
A02167. MHMSM.
UniGeneiMm.304472.
Mm.313488.
Mm.342177.
Mm.428442.
Mm.435580.
Mm.436922.
Mm.439101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BA8NMR-A222-321[»]
4JVUX-ray1.30A/B103-217[»]
4JVWX-ray2.00A/B/C/D324-436[»]
ProteinModelPortaliP01872.
SMRiP01872. Positions 1-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01872. 5 interactions.

Protein family/group databases

IMGTiSearch...
Search...
Search...
Search...
Search...
Search...

Proteomic databases

EPDiP01872.
MaxQBiP01872.
PeptideAtlasiP01872.
PRIDEiP01872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:96448. Ighm.

Phylogenomic databases

HOVERGENiHBG005814.

Enzyme and pathway databases

ReactomeiR-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

PROiP01872.
SOURCEiSearch...

Gene expression databases

CleanExiMM_IGH-6.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 4 hits.
[Graphical view]
SMARTiSM00407. IGc1. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS00290. IG_MHC. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: PROTEIN SEQUENCE (MYELOMA MOPC 104E).
    Tissue: Myeloma.
  2. "Complete amino acid sequence of a mouse mu chain: homology among heavy chain constant region domains."
    Kehry M.R., Fuhrman J.S., Schilling J.W., Rogers J., Sibley C.H., Hood L.E.
    Biochemistry 21:5415-5424(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION (MYELOMA MOPC 104E).
  3. "Two mRNAs with different 3' ends encode membrane-bound and secreted forms of immunoglobulin mu chain."
    Rogers J., Early P., Carter C., Calame K., Bond M., Hood L., Wall R.
    Cell 20:303-312(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 409-454 (ISOFORM 2).
    Strain: BALB/cJ.
    Tissue: Myeloma.
  4. "Nucleotide sequence of a cloned cDNA corresponding to secreted mu chain of mouse immunoglobulin."
    Auffray C., Rougeon F.
    Gene 12:77-86(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (MYELOMA TEPC183).
    Strain: BALB/cJ.
    Tissue: Myeloma.
  5. "Complete nucleotide sequence of mouse immunoglobulin mu gene and comparison with other immunoglobulin heavy chain genes."
    Kawakami T., Takahashi N., Honjo T.
    Nucleic Acids Res. 8:3933-3945(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  6. "Sequence of the gene for the constant region of the mu chain of Balb/c mouse immunoglobulin."
    Goldberg G.I., Vanin E.F., Zrolka A.M., Blattner F.R.
    Gene 15:33-42(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  7. "Site-specific characterization of the N-linked oligosaccharides of a murine immunoglobulin M by high-performance liquid chromatography/electrospray mass spectrometry."
    Wang F., Nakouzi A., Angeletti R.H., Casadevall A.
    Anal. Biochem. 314:266-280(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-45; ASN-210; ASN-242; ASN-257 AND ASN-280.
  8. "Two mRNAs can be produced from a single immunoglobulin mu gene by alternative RNA processing pathways."
    Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L.
    Cell 20:313-319(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 428-454, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
    Strain: BALB/cJ.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  10. "High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation."
    Muller R., Grawert M.A., Kern T., Madl T., Peschek J., Sattler M., Groll M., Buchner J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10183-10188(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 103-217, STRUCTURE BY NMR OF 222-321, DISULFIDE BONDS, MUTAGENESIS OF CYS-215; CYS-292 AND CYS-453.

Entry informationi

Entry nameiIGHM_MOUSE
AccessioniPrimary (citable) accession number: P01872
Secondary accession number(s): P01873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 2005
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.