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 13-FEB-2019, entry version 160. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 RT chemical 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 RT followed 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 RT with 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., RA Thuluvath P.J., 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., RA Moore R.J., 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., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein 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 RT multiple 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., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Serves to link two monomer units of either IgM or IgA. CC In the case of IgM, the J chain-joined dimer is a nucleating unit CC for the IgM pentamer, and in the case of IgA it induces larger CC polymers. It also help to bind these immunoglobulins to secretory CC component. {ECO:0000250|UniProtKB:P01592}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01592}. 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; 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 UniGene; Hs.643431; -. DR ProteinModelPortal; P01591; -. DR BioGrid; 109732; 24. DR IntAct; P01591; 5. DR MINT; P01591; -. DR STRING; 9606.ENSP00000254801; -. DR GlyConnect; 277; -. DR iPTMnet; P01591; -. DR PhosphoSitePlus; P01591; -. DR UniCarbKB; P01591; -. DR BioMuta; JCHAIN; -. DR SWISS-2DPAGE; P01591; -. DR EPD; P01591; -. DR jPOST; P01591; -. DR MaxQB; P01591; -. DR PaxDb; P01591; -. DR PeptideAtlas; P01591; -. DR PRIDE; P01591; -. DR ProteomicsDB; 51394; -. DR Ensembl; ENST00000254801; ENSP00000254801; ENSG00000132465. DR Ensembl; ENST00000510437; ENSP00000426687; ENSG00000132465. DR Ensembl; ENST00000543780; ENSP00000440066; ENSG00000132465. DR GeneID; 3512; -. DR KEGG; hsa:3512; -. DR UCSC; uc003hfn.5; human. DR CTD; 3512; -. DR DisGeNET; 3512; -. DR EuPathDB; HostDB:ENSG00000132465.10; -. DR GeneCards; JCHAIN; -. DR HGNC; HGNC:5713; JCHAIN. DR HPA; CAB034436; -. DR HPA; HPA044132; -. DR MIM; 147790; gene. DR neXtProt; NX_P01591; -. DR OpenTargets; ENSG00000132465; -. DR PharmGKB; PA29733; -. DR eggNOG; ENOG410IYAZ; Eukaryota. DR eggNOG; ENOG410YX96; LUCA. DR GeneTree; ENSGT00390000012791; -. DR HOGENOM; HOG000113012; -. DR HOVERGEN; HBG006138; -. DR InParanoid; P01591; -. DR OMA; KCYTNRV; -. DR OrthoDB; 665362at2759; -. DR PhylomeDB; P01591; -. DR TreeFam; TF335878; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-2168880; Scavenging of heme from plasma. DR ChiTaRS; JCHAIN; human. DR GeneWiki; IGJ; -. DR GenomeRNAi; 3512; -. DR PRO; PR:P01591; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000132465; Expressed in 169 organ(s), highest expression level in caecum. 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; IBA:GO_Central. DR GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. 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:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0032461; P:positive regulation of protein oligomerization; IMP:UniProtKB. DR GO; GO:0060267; P:positive regulation of respiratory burst; IDA:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. 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. DR ProDom; PD021296; PD021296; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 22 {ECO:0000269|PubMed:25946035}. FT CHAIN 23 159 Immunoglobulin J chain. FT /FTId=PRO_0000084174. FT MOD_RES 23 23 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:25946035, FT ECO:0000269|PubMed:407930}. FT CARBOHYD 71 71 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT /FTId=CAR_000167. FT DISULFID 35 123 {ECO:0000269|PubMed:1472500}. FT DISULFID 37 37 Interchain (with heavy chain). FT {ECO:0000269|PubMed:1472500}. FT DISULFID 91 91 Interchain (with heavy chain). FT {ECO:0000269|PubMed:1472500}. FT DISULFID 94 114 {ECO:0000269|PubMed:1472500}. FT DISULFID 131 156 {ECO:0000269|PubMed:1472500}. SQ SEQUENCE 159 AA; 18099 MW; B7835C02CCC0CB05 CRC64; MKNHLLFWGV LAVFIKAVHV KAQEDERIVL VDNKCKCARI TSRIIRSSED PNEDIVERNI RIIVPLNNRE NISDPTSPLR TRFVYHLSDL CKKCDPTEVE LDNQIVTATQ SNICDEDSAT ETCYTYDRNK CYTAVVPLVY GGETKMVETA LTPDACYPD //