IGJ_MOUSE
ID IGJ_MOUSE Reviewed; 159 AA.
AC P01592;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Immunoglobulin J chain {ECO:0000312|MGI:MGI:96493};
DE Flags: Precursor;
GN Name=Jchain {ECO:0000312|MGI:MGI:96493}; Synonyms=Igj;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3079912; DOI=10.1073/pnas.83.2.456;
RA Matsuuchi L., Cann G.M., Koshland M.E.;
RT "Immunoglobulin J chain gene from the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:456-460(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/10;
RX PubMed=1517233; DOI=10.1016/s0021-9258(19)37143-1;
RA Randall T.D., Brewer J.W., Corley R.B.;
RT "Direct evidence that J chain regulates the polymeric structure of IgM in
RT antibody-secreting B cells.";
RL J. Biol. Chem. 267:18002-18007(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-159.
RX PubMed=6815655; DOI=10.1073/pnas.79.21.6656;
RA Cann G.M., Zaritsky A., Koshland M.E.;
RT "Primary structure of the immunoglobulin J chain from the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6656-6660(1982).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Serves to link two monomer units of either IgM or IgA. In the
CC case of IgM, the J chain-joined dimer is a nucleating unit for the IgM
CC pentamer, and in the case of IgA it induces dimers and/or larger
CC polymers. It also helps to bind these immunoglobulins to secretory
CC component. {ECO:0000269|PubMed:1517233}.
CC -!- SUBUNIT: Part of the secretory IgA (sIgA) complex that consists of two,
CC four or five IgA monomers, and two additional non-Ig polypeptides,
CC namely the JCHAIN and the secretory component (the proteoytic product
CC of PIGR). {ECO:0000250|UniProtKB:P01591}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}.
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DR EMBL; M12557; AAA38674.1; -; Genomic_DNA.
DR EMBL; M12555; AAA38674.1; JOINED; Genomic_DNA.
DR EMBL; M12556; AAA38674.1; JOINED; Genomic_DNA.
DR EMBL; J00544; AAA38673.1; ALT_SEQ; mRNA.
DR EMBL; M90766; AAA37918.1; -; mRNA.
DR CCDS; CCDS19401.1; -.
DR PIR; A25963; JIMS.
DR RefSeq; NP_690052.2; NM_152839.3.
DR PDB; 7JG1; EM; 3.30 A; J=23-159.
DR PDB; 7JG2; EM; 3.30 A; J=23-159.
DR PDBsum; 7JG1; -.
DR PDBsum; 7JG2; -.
DR AlphaFoldDB; P01592; -.
DR SMR; P01592; -.
DR BioGRID; 200579; 1.
DR IntAct; P01592; 1.
DR MINT; P01592; -.
DR STRING; 10090.ENSMUSP00000084259; -.
DR GlyConnect; 694; 2 N-Linked glycans (1 site).
DR GlyGen; P01592; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; P01592; -.
DR PhosphoSitePlus; P01592; -.
DR CPTAC; non-CPTAC-3651; -.
DR CPTAC; non-CPTAC-3920; -.
DR EPD; P01592; -.
DR MaxQB; P01592; -.
DR PaxDb; P01592; -.
DR PeptideAtlas; P01592; -.
DR PRIDE; P01592; -.
DR ProteomicsDB; 269385; -.
DR Antibodypedia; 12875; 362 antibodies from 29 providers.
DR DNASU; 16069; -.
DR Ensembl; ENSMUST00000087033; ENSMUSP00000084259; ENSMUSG00000067149.
DR GeneID; 16069; -.
DR KEGG; mmu:16069; -.
DR UCSC; uc008xzu.2; mouse.
DR CTD; 3512; -.
DR MGI; MGI:96493; Jchain.
DR VEuPathDB; HostDB:ENSMUSG00000067149; -.
DR eggNOG; ENOG502RZF4; Eukaryota.
DR GeneTree; ENSGT00390000012791; -.
DR HOGENOM; CLU_1651635_0_0_1; -.
DR InParanoid; P01592; -.
DR OMA; DNKCKCV; -.
DR OrthoDB; 1400263at2759; -.
DR PhylomeDB; P01592; -.
DR TreeFam; TF335878; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR BioGRID-ORCS; 16069; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Jchain; mouse.
DR PRO; PR:P01592; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P01592; protein.
DR Bgee; ENSMUSG00000067149; Expressed in submandibular gland and 108 other tissues.
DR Genevisible; P01592; MM.
DR GO; GO:0071750; C:dimeric IgA immunoglobulin complex; IMP:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0071748; C:monomeric IgA immunoglobulin complex; ISO:MGI.
DR GO; GO:0071756; C:pentameric IgM immunoglobulin complex; ISO:MGI.
DR GO; GO:0071752; C:secretory dimeric IgA immunoglobulin complex; ISO:MGI.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; ISS:UniProtKB.
DR GO; GO:0003823; F:antigen binding; ISS:MGI.
DR GO; GO:0019862; F:IgA binding; IDA:UniProtKB.
DR GO; GO:0034987; F:immunoglobulin receptor binding; ISO:MGI.
DR GO; GO:0042834; F:peptidoglycan binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0003094; P:glomerular filtration; ISO:MGI.
DR GO; GO:0006959; P:humoral immune response; ISS:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0060267; P:positive regulation of respiratory burst; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR InterPro; IPR024110; Ig_J.
DR PANTHER; PTHR10070; PTHR10070; 1.
DR Pfam; PF15097; Ig_J_chain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT CHAIN 22..159
FT /note="Immunoglobulin J chain"
FT /id="PRO_0000021486"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 34..123
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 36
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 90
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 93..113
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 131..156
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT CONFLICT 17
FT /note="A -> V (in Ref. 1; AAA38674)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="R -> K (in Ref. 1; AAA38674)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> L (in Ref. 3; AAA38673)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="LR -> PG (in Ref. 3; AAA38673)"
FT /evidence="ECO:0000305"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7JG1"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 53..66
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:7JG1"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:7JG1"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7JG2"
SQ SEQUENCE 159 AA; 18014 MW; B75269C634470384 CRC64;
MKTHLLLWGV LAIFVKAVLV TGDDEATILA DNKCMCTRVT SRIIPSTEDP NEDIVERNIR
IVVPLNNREN ISDPTSPLRR NFVYHLSDVC KKCDPVEVEL EDQVVTATQS NICNEDDGVP
ETCYMYDRNK CYTTMVPLRY HGETKMVQAA LTPDSCYPD
