IGJ_HUMAN
ID IGJ_HUMAN Reviewed; 159 AA.
AC P01591;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Immunoglobulin J chain;
DE AltName: Full=Joining chain of multimeric IgA and IgM {ECO:0000312|HGNC:HGNC:5713};
DE Flags: Precursor;
GN Name=JCHAIN {ECO:0000312|HGNC:HGNC:5713}; Synonyms=IGCJ, IGJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 23-159, AND PYROGLUTAMATE FORMATION AT
RP GLN-23.
RX PubMed=407930; DOI=10.1021/bi00635a002;
RA Mole J.E., Bhown A.S., Bennett J.C.;
RT "Primary structure of human J chain: alignment of peptides from chemical
RT and enzymatic hydrolyses.";
RL Biochemistry 16:3507-3513(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-159.
RX PubMed=2984306; DOI=10.1084/jem.161.4.832;
RA Max E.E., Korsmeyer S.J.;
RT "Human J chain gene. Structure and expression in B lymphoid cells.";
RL J. Exp. Med. 161:832-849(1985).
RN [4]
RP PROTEIN SEQUENCE OF 23-50, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-23.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [5]
RP DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1472500; DOI=10.1021/bi00165a014;
RA Frutiger S., Hughes G.J., Paquet N., Luethy R., Jaton J.-C.;
RT "Disulfide bond assignment in human J chain and its covalent pairing with
RT immunoglobulin M.";
RL Biochemistry 31:12643-12647(1992).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP GLYCOSYLATION AT ASN-71.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 23-159 IN COMPLEX WITH
RP PIGR AND IGHA1 OR IGHA2, AND SUBUNIT.
RX PubMed=32029686; DOI=10.1126/science.aaz5807;
RA Kumar N., Arthur C.P., Ciferri C., Matsumoto M.L.;
RT "Structure of the secretory immunoglobulin A core.";
RL Science 367:1008-1014(2020).
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:0000250|UniProtKB:P01592}.
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:0000269|PubMed:32029686}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01592}.
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DR EMBL; AK312014; BAG34952.1; -; mRNA.
DR EMBL; M12759; AAA58902.1; -; Genomic_DNA.
DR EMBL; M12378; AAA58902.1; JOINED; Genomic_DNA.
DR CCDS; CCDS3545.1; -.
DR PIR; A01859; JIHU.
DR RefSeq; NP_653247.1; NM_144646.3.
DR RefSeq; XP_006714274.1; XM_006714211.2.
DR RefSeq; XP_006714275.1; XM_006714212.2.
DR RefSeq; XP_011530227.1; XM_011531925.1.
DR RefSeq; XP_011530228.1; XM_011531926.1.
DR PDB; 6KXS; EM; 3.40 A; J=24-159.
DR PDB; 6LX3; EM; 3.15 A; J=1-159.
DR PDB; 6LXW; EM; 3.27 A; J=1-159.
DR PDB; 6UE7; EM; 2.90 A; D=23-159.
DR PDB; 6UE8; EM; 3.00 A; D=23-159.
DR PDB; 6UE9; EM; 2.90 A; D=23-159.
DR PDB; 6UEA; EM; 3.00 A; D=23-159.
DR PDB; 7K0C; EM; 3.30 A; D=23-159.
DR PDBsum; 6KXS; -.
DR PDBsum; 6LX3; -.
DR PDBsum; 6LXW; -.
DR PDBsum; 6UE7; -.
DR PDBsum; 6UE8; -.
DR PDBsum; 6UE9; -.
DR PDBsum; 6UEA; -.
DR PDBsum; 7K0C; -.
DR AlphaFoldDB; P01591; -.
DR SMR; P01591; -.
DR BioGRID; 109732; 75.
DR IntAct; P01591; 25.
DR MINT; P01591; -.
DR STRING; 9606.ENSP00000254801; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 277; 86 N-Linked glycans (2 sites).
DR GlyGen; P01591; 5 sites, 89 N-linked glycans (1 site), 2 O-linked glycans (2 sites).
DR iPTMnet; P01591; -.
DR PhosphoSitePlus; P01591; -.
DR BioMuta; JCHAIN; -.
DR SWISS-2DPAGE; P01591; -.
DR CPTAC; CPTAC-659; -.
DR jPOST; P01591; -.
DR MassIVE; P01591; -.
DR MaxQB; P01591; -.
DR PaxDb; P01591; -.
DR PeptideAtlas; P01591; -.
DR PRIDE; P01591; -.
DR ProteomicsDB; 51394; -.
DR Antibodypedia; 12875; 362 antibodies from 29 providers.
DR DNASU; 3512; -.
DR Ensembl; ENST00000254801.9; ENSP00000254801.4; ENSG00000132465.12.
DR Ensembl; ENST00000510437.5; ENSP00000426687.1; ENSG00000132465.12.
DR GeneID; 3512; -.
DR KEGG; hsa:3512; -.
DR MANE-Select; ENST00000254801.9; ENSP00000254801.4; NM_144646.4; NP_653247.1.
DR UCSC; uc003hfn.5; human.
DR CTD; 3512; -.
DR DisGeNET; 3512; -.
DR GeneCards; JCHAIN; -.
DR HGNC; HGNC:5713; JCHAIN.
DR HPA; ENSG00000132465; Tissue enhanced (breast, intestine, stomach).
DR MIM; 147790; gene.
DR neXtProt; NX_P01591; -.
DR OpenTargets; ENSG00000132465; -.
DR PharmGKB; PA29733; -.
DR VEuPathDB; HostDB:ENSG00000132465; -.
DR eggNOG; ENOG502RZF4; Eukaryota.
DR GeneTree; ENSGT00390000012791; -.
DR HOGENOM; CLU_1651635_0_0_1; -.
DR InParanoid; P01591; -.
DR OMA; DNKCKCV; -.
DR OrthoDB; 1400263at2759; -.
DR PhylomeDB; P01591; -.
DR TreeFam; TF335878; -.
DR PathwayCommons; P01591; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR SignaLink; P01591; -.
DR BioGRID-ORCS; 3512; 4 hits in 1066 CRISPR screens.
DR ChiTaRS; JCHAIN; human.
DR GeneWiki; IGJ; -.
DR GenomeRNAi; 3512; -.
DR Pharos; P01591; Tbio.
DR PRO; PR:P01591; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P01591; protein.
DR Bgee; ENSG00000132465; Expressed in rectum and 151 other tissues.
DR ExpressionAtlas; P01591; baseline and differential.
DR Genevisible; P01591; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0071750; C:dimeric IgA immunoglobulin complex; IMP:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071752; C:secretory dimeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0019862; F:IgA binding; IMP:UniProtKB.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0060267; P:positive regulation of respiratory burst; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:25946035"
FT CHAIN 23..159
FT /note="Immunoglobulin J chain"
FT /id="PRO_0000084174"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:25946035,
FT ECO:0000269|PubMed:407930"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT /id="CAR_000167"
FT DISULFID 35..123
FT /evidence="ECO:0000269|PubMed:1472500"
FT DISULFID 37
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:1472500"
FT DISULFID 91
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:1472500"
FT DISULFID 94..114
FT /evidence="ECO:0000269|PubMed:1472500"
FT DISULFID 131..156
FT /evidence="ECO:0000269|PubMed:1472500"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6UE7"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 55..67
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6UE9"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6UE7"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6UE8"
SQ SEQUENCE 159 AA; 18099 MW; B7835C02CCC0CB05 CRC64;
MKNHLLFWGV LAVFIKAVHV KAQEDERIVL VDNKCKCARI TSRIIRSSED PNEDIVERNI
RIIVPLNNRE NISDPTSPLR TRFVYHLSDL CKKCDPTEVE LDNQIVTATQ SNICDEDSAT
ETCYTYDRNK CYTAVVPLVY GGETKMVETA LTPDACYPD
