IGJ_EQUAS
ID IGJ_EQUAS Reviewed; 158 AA.
AC P0DUB2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=Immunoglobulin J chain {ECO:0000303|PubMed:32251747};
DE AltName: Full=Joining chain of multimeric IgA and IgM;
DE Flags: Precursor;
GN Name=JCHAIN;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=26373886; DOI=10.1038/srep14106;
RA Huang J., Zhao Y., Bai D., Shiraigol W., Li B., Yang L., Wu J., Bao W.,
RA Ren X., Jin B., Zhao Q., Li A., Bao S., Bao W., Xing Z., An A., Gao Y.,
RA Wei R., Bao Y., Bao T., Han H., Bai H., Bao Y., Zhang Y., Daidiikhuu D.,
RA Zhao W., Liu S., Ding J., Ye W., Ding F., Sun Z., Shi Y., Zhang Y.,
RA Meng H., Dugarjaviin M.;
RT "Donkey genome and insight into the imprinting of fast karyotype
RT evolution.";
RL Sci. Rep. 5:14106-14106(2015).
RN [2]
RP PROTEIN SEQUENCE OF 45-59 AND 135-144, IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION AT ASN-72, AND SUBCELLULAR LOCATION.
RX PubMed=32251747; DOI=10.1016/j.ijbiomac.2020.03.253;
RA Gnanesh Kumar B.S., Rawal A.;
RT "Sequence characterization and N-glycoproteomics of secretory
RT immunoglobulin A from donkey milk.";
RL Int. J. Biol. Macromol. 155:605-613(2020).
RN [3]
RP PROTEIN SEQUENCE OF 45-59; 82-94 AND 135-144, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21645650; DOI=10.1016/j.jprot.2011.05.036;
RA Cunsolo V., Muccilli V., Fasoli E., Saletti R., Righetti P.G., Foti S.;
RT "Poppea's bath liquor: the secret proteome of she-donkey's milk.";
RL J. Proteomics 74:2083-2099(2011).
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:0000250|UniProtKB:P01591}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21645650,
CC ECO:0000269|PubMed:32251747}.
CC -!- PTM: N-glycosylated. N-glycans attached to Asn-72 varies from
CC truncated, differentially fucosylated to sialylated (NeuGc) complex
CC types: Man3GlcNAc2; GlcNAc2Man3GlcNAc2(Fuc); Gal1GlcNAc1Man3GlcNAc2;
CC GlcNAc2Man3GlcNAc2; GlcNAc1Man3GlcNAc2; GlcNAc1Man2GlcNAc2 and
CC NeuGc1Gal1GlcNAc2Man3GlcNAc2. {ECO:0000269|PubMed:32251747}.
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DR RefSeq; XP_014702706.1; XM_014847220.1.
DR AlphaFoldDB; P0DUB2; -.
DR SMR; P0DUB2; -.
DR GeneID; 106835097; -.
DR KEGG; eai:106835097; -.
DR CTD; 3512; -.
DR OMA; DNKCKCV; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR024110; Ig_J.
DR PANTHER; PTHR10070; PTHR10070; 1.
DR Pfam; PF15097; Ig_J_chain; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P01591, ECO:0000255"
FT CHAIN 23..158
FT /note="Immunoglobulin J chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451037"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT DISULFID 36..122
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 38
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 92
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 95..115
FT /evidence="ECO:0000250|UniProtKB:P01591"
FT DISULFID 130..155
FT /evidence="ECO:0000250|UniProtKB:P01591"
SQ SEQUENCE 158 AA; 17838 MW; 4F7BEE2772D7EDA2 CRC64;
MKNHLFFWGV LAIFVQAVLV TAGDEGERIV LADNKCKCVR VTSRIIPSPE NPNEDILERH
IRIIIPVNSR ENISDPTSPV RTKFVYHLSD LCKKCDPVEV ELDNQVVTAS QSNICDEDSE
TCYAYDRNKC YTNRVPLTYG GQTKIVETAL TPDSCYPD
