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   27-MAR-2024, entry version 148.
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 proteolytic product
CC       of PIGR). Part of the secretory IgM (sIgM) complex that consist of five
CC       IgM monomers, and two additional non-Ig polypeptides, namely the JCHAIN
CC       and the secretory component (the proteolytic product of PIGR). JCHAIN-
CC       containing IgM interacts (via CH4 domain) with FCRM (via Ig-like
CC       domain). {ECO:0000250|UniProtKB:P01591}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   EMDB; EMD-22309; -.
DR   EMDB; EMD-22310; -.
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   GlyCosmos; P01592; 1 site, 4 glycans.
DR   GlyGen; P01592; 2 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (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; 10090-ENSMUSP00000084259; -.
DR   PeptideAtlas; P01592; -.
DR   ProteomicsDB; 269385; -.
DR   Antibodypedia; 12875; 421 antibodies from 30 providers.
DR   DNASU; 16069; -.
DR   Ensembl; ENSMUST00000087033.6; ENSMUSP00000084259.4; ENSMUSG00000067149.7.
DR   GeneID; 16069; -.
DR   KEGG; mmu:16069; -.
DR   UCSC; uc008xzu.2; mouse.
DR   AGR; MGI:96493; -.
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; KCQCARV; -.
DR   OrthoDB; 5315827at2759; -.
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 76 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 cell types or tissues.
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; ISS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:Ensembl.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
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; IEA:Ensembl.
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; IMMUNOGLOBULIN J CHAIN; 1.
DR   PANTHER; PTHR10070:SF2; IMMUNOGLOBULIN J CHAIN; 1.
DR   Pfam; PF15097; Ig_J_chain; 1.
DR   Genevisible; P01592; MM.
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
//