PIGR_HUMAN
ID PIGR_HUMAN Reviewed; 764 AA.
AC P01833; Q68D81; Q8IZY7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Polymeric immunoglobulin receptor;
DE Short=PIgR;
DE Short=Poly-Ig receptor;
DE AltName: Full=Hepatocellular carcinoma-associated protein TB6;
DE Contains:
DE RecName: Full=Secretory component;
DE Flags: Precursor;
GN Name=PIGR;
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 [MRNA], AND VARIANT SER-365.
RX PubMed=1682231; DOI=10.1007/bf00201717;
RA Krajci P., Grzeschik K.H., Geurts van Kessel A.H., Olaisen B.,
RA Brandtzaeg P.;
RT "The human transmembrane secretory component (poly-Ig receptor): molecular
RT cloning, restriction fragment length polymorphism and chromosomal
RT sublocalization.";
RL Hum. Genet. 87:642-648(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-365.
RX PubMed=1355431; DOI=10.1002/eji.1830220920;
RA Krajci P., Kvale D., Tasken K., Brandtzaeg P.;
RT "Molecular cloning and exon-intron mapping of the gene encoding human
RT transmembrane secretory component (the poly-Ig receptor).";
RL Eur. J. Immunol. 22:2309-2315(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dong X., Pang X., Cheng W.;
RT "Cloning and characterization of hepatocellular carcinoma associated-
RT genes.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-365.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-764, AND VARIANT SER-365.
RX PubMed=2920039; DOI=10.1016/0006-291x(89)92790-3;
RA Krajci P., Solberg R., Sandberg M., Oyen O., Jahnsen T., Brandtzaeg P.;
RT "Molecular cloning of the human transmembrane secretory component (poly-Ig
RT receptor) and its mRNA expression in human tissues.";
RL Biochem. Biophys. Res. Commun. 158:783-789(1989).
RN [6]
RP PROTEIN SEQUENCE OF 19-577, VARIANT SER-365, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND
RP ASN-499.
RX PubMed=6526384;
RA Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M.,
RA Klingmueller D., Weber M.H., Hilschmann N.;
RT "The primary structure of human free secretory component and the
RT arrangement of disulfide bonds.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:1489-1495(1984).
RN [7]
RP PROTEIN SEQUENCE OF 19-577, AND VARIANT SER-365.
RX PubMed=1859628; DOI=10.1515/bchm3.1991.372.1.119;
RA Eiffert H., Quentin E., Wiederhold M., Hillemeir S., Decker J., Weber M.,
RA Hilschmann N.;
RT "Determination of the molecular structure of the human free secretory
RT component.";
RL Biol. Chem. Hoppe-Seyler 372:119-128(1991).
RN [8]
RP SUBUNIT (SECRETORY COMPONENT), SUBCELLULAR LOCATION (SECRETORY COMPONENT),
RP AND DISULFIDE BOND.
RX PubMed=8292260; DOI=10.1515/bchm3.1993.374.7-12.1023;
RA Fallgreen-Gebauer E., Gebauer W., Bastian A., Kratzin H.D., Eiffert H.,
RA Zimmermann B., Karas M., Hilschmann N.;
RT "The covalent linkage of secretory component to IgA. Structure of sIgA.";
RL Biol. Chem. Hoppe-Seyler 374:1023-1028(1993).
RN [9]
RP PROTEIN SEQUENCE OF 118-138; 212-230; 232-268; 273-288 AND 578-603.
RX PubMed=9237679; DOI=10.1016/s0014-5793(97)00629-7;
RA Hughes G.J., Frutiger S., Savoy L.-A., Reason A.J., Morris H.R.,
RA Jaton J.-C.;
RT "Human free secretory component is composed of the first 585 amino acid
RT residues of the polymeric immunoglobulin receptor.";
RL FEBS Lett. 410:443-446(1997).
RN [10]
RP FUNCTION (POLYMERIC IMMUNOGLOBULIN RECEPTOR), AND SUBCELLULAR LOCATION
RP (POLYMERIC IMMUNOGLOBULIN RECEPTOR).
RX PubMed=9379029;
RA Natvig I.B., Johansen F.E., Nordeng T.W., Haraldsen G., Brandtzaeg P.;
RT "Mechanism for enhanced external transfer of dimeric IgA over pentameric
RT IgM: studies of diffusion, binding to the human polymeric Ig receptor, and
RT epithelial transcytosis.";
RL J. Immunol. 159:4330-4340(1997).
RN [11]
RP FUNCTION (POLYMERIC IMMUNOGLOBULIN RECEPTOR), SUBUNIT, AND DOMAIN.
RX PubMed=10229845;
RA Roee M., Norderhaug I.N., Brandtzaeg P., Johansen F.E.;
RT "Fine specificity of ligand-binding domain 1 in the polymeric Ig receptor:
RT importance of the CDR2-containing region for IgM interaction.";
RL J. Immunol. 162:6046-6052(1999).
RN [12]
RP FUNCTION (SECRETORY COMPONENT), AND GLYCOSYLATION.
RX PubMed=12150896; DOI=10.1016/s1074-7613(02)00341-2;
RA Phalipon A., Cardona A., Kraehenbuhl J.P., Edelman L., Sansonetti P.J.,
RA Corthesy B.;
RT "Secretory component: a new role in secretory IgA-mediated immune exclusion
RT in vivo.";
RL Immunity 17:107-115(2002).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 AND
RP ASN-469.
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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469.
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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186; ASN-421;
RP ASN-469 AND ASN-499.
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 [16]
RP FUNCTION (SECRETORY COMPONENT), SUBCELLULAR LOCATION (SECRETORY COMPONENT),
RP SUBUNIT (SECRETORY COMPONENT), AND GLYCOSYLATION.
RX PubMed=16543244; DOI=10.1074/jbc.m512958200;
RA Perrier C., Sprenger N., Corthesy B.;
RT "Glycans on secretory component participate in innate protection against
RT mucosal pathogens.";
RL J. Biol. Chem. 281:14280-14287(2006).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135; ASN-186;
RP ASN-421; ASN-469 AND ASN-499.
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 [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421 AND ASN-469.
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 [19]
RP GLYCOSYLATION AT ASN-469.
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 [20]
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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP PROTEIN SEQUENCE OF 573-648, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-127, FUNCTION (POLYMERIC
RP IMMUNOGLOBULIN RECEPTOR), SUBUNIT, AND DOMAIN.
RX PubMed=15530357; DOI=10.1016/j.str.2004.09.006;
RA Hamburger A.E., West A.P. Jr., Bjorkman P.J.;
RT "Crystal structure of a polymeric immunoglobulin binding fragment of the
RT human polymeric immunoglobulin receptor.";
RL Structure 12:1925-1935(2004).
RN [24]
RP STRUCTURE BY NMR OF 353-458 AND 19-603, SUBUNIT (SECRETORY COMPONENT), AND
RP SUBCELLULAR LOCATION (SECRETORY COMPONENT).
RX PubMed=19079336; DOI=10.1038/mi.2008.68;
RA Bonner A., Almogren A., Furtado P.B., Kerr M.A., Perkins S.J.;
RT "Location of secretory component on the Fc edge of dimeric IgA1 reveals
RT insight into the role of secretory IgA1 in mucosal immunity.";
RL Mucosal Immunol. 2:74-84(2009).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 19-603 IN COMPLEX WITH
RP JCHAIN AND IGHA1 OR IGHA2, SUBUNIT (SECRETORY COMPONENT), SUBCELLULAR
RP LOCATION (SECRETORY COMPONENT), AND DISULFIDE BOND.
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: [Polymeric immunoglobulin receptor]: Mediates selective
CC transcytosis of polymeric IgA and IgM across mucosal epithelial cells.
CC Binds polymeric IgA and IgM at the basolateral surface of epithelial
CC cells. The complex is then transported across the cell to be secreted
CC at the apical surface. During this process, a cleavage occurs that
CC separates the extracellular (known as the secretory component) from the
CC transmembrane segment. {ECO:0000269|PubMed:10229845,
CC ECO:0000269|PubMed:15530357, ECO:0000269|PubMed:9379029}.
CC -!- FUNCTION: [Secretory component]: Through its N-linked glycans ensures
CC anchoring of secretory IgA (sIgA) molecules to mucus lining the
CC epithelial surface to neutralize extracellular pathogens
CC (PubMed:12150896). On its own (free form) may act as a non-specific
CC microbial scavenger to prevent pathogen interaction with epithelial
CC cells (PubMed:16543244). {ECO:0000269|PubMed:12150896,
CC ECO:0000269|PubMed:16543244}.
CC -!- SUBUNIT: Interacts (mainly via CDR1-like domain) with dimeric IgA
CC (PubMed:15530357). Interacts (mainly via CDR2-like domain) with
CC pentameric IgM (PubMed:10229845). {ECO:0000269|PubMed:10229845,
CC ECO:0000269|PubMed:15530357}.
CC -!- SUBUNIT: [Secretory component]: Either free or part of the secretory
CC IgA (sIgA) complex that consists of two, four or five IgA monomers, and
CC two additional non-Ig polypeptides, namely the JCHAIN and the secretory
CC component (the proteolytic product of PIGR) (PubMed:8292260,
CC PubMed:19079336, PubMed:32029686, PubMed:16543244). Free secretory
CC component interacts with bacterial antigens toxA of C. difficile and
CC eae of E. coli (PubMed:16543244). {ECO:0000269|PubMed:16543244,
CC ECO:0000269|PubMed:19079336, ECO:0000269|PubMed:32029686,
CC ECO:0000269|PubMed:8292260}.
CC -!- SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell
CC membrane {ECO:0000269|PubMed:9379029}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secretory component]: Secreted
CC {ECO:0000269|PubMed:16543244, ECO:0000269|PubMed:19079336,
CC ECO:0000269|PubMed:8292260}.
CC -!- DOMAIN: The Ig-like V-type 1/D1 domain contains three complementarity
CC determining region-like loops CDR1-3, which mediate interaction with
CC IgA and IgM. {ECO:0000269|PubMed:10229845,
CC ECO:0000269|PubMed:15530357}.
CC -!- PTM: N-glycosylated. N-glycosylation is required for anchoring IgA
CC molecules to mucus, but is not necessary for Ig binding.
CC {ECO:0000269|PubMed:12150896, ECO:0000269|PubMed:15084671,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16543244,
CC ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:6526384}.
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DR EMBL; S62403; AAB20203.1; -; mRNA.
DR EMBL; S43449; AAB23176.1; -; Genomic_DNA.
DR EMBL; S43437; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43441; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43442; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43443; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43444; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43445; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43446; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43447; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; S43448; AAB23176.1; JOINED; Genomic_DNA.
DR EMBL; AF272149; AAN65630.1; -; mRNA.
DR EMBL; CR749533; CAH18339.1; -; mRNA.
DR EMBL; M24559; AAA36102.1; -; mRNA.
DR CCDS; CCDS1474.1; -.
DR PIR; A46537; QRHUGS.
DR RefSeq; NP_002635.2; NM_002644.3.
DR RefSeq; XP_011507931.1; XM_011509629.1.
DR PDB; 1XED; X-ray; 1.90 A; A/B/C/D/E/F=19-127.
DR PDB; 2OCW; X-ray; -; A=19-603.
DR PDB; 3CHN; Other; 1.00 A; J=353-458, S=19-603.
DR PDB; 3CM9; Other; 1.00 A; J=353-458, S=19-603.
DR PDB; 5D4K; X-ray; 2.60 A; A/B=19-565.
DR PDB; 6KXS; EM; 3.40 A; P=19-565.
DR PDB; 6LX3; EM; 3.15 A; P=1-565.
DR PDB; 6LXW; EM; 3.27 A; P=1-565.
DR PDB; 6UE7; EM; 2.90 A; C=19-603.
DR PDB; 6UE8; EM; 3.00 A; C=19-603.
DR PDB; 6UE9; EM; 2.90 A; C=19-603.
DR PDB; 6UEA; EM; 3.00 A; C=19-603.
DR PDB; 7K0C; EM; 3.30 A; C=19-603.
DR PDBsum; 1XED; -.
DR PDBsum; 2OCW; -.
DR PDBsum; 3CHN; -.
DR PDBsum; 3CM9; -.
DR PDBsum; 5D4K; -.
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; P01833; -.
DR SMR; P01833; -.
DR BioGRID; 111302; 155.
DR IntAct; P01833; 25.
DR STRING; 9606.ENSP00000348888; -.
DR ChEMBL; CHEMBL4295691; -.
DR GlyConnect; 550; 182 N-Linked glycans (7 sites), 8 O-Linked glycans (6 sites).
DR GlyGen; P01833; 12 sites, 138 N-linked glycans (8 sites), 5 O-linked glycans (5 sites).
DR iPTMnet; P01833; -.
DR PhosphoSitePlus; P01833; -.
DR BioMuta; PIGR; -.
DR DMDM; 150421625; -.
DR CPTAC; CPTAC-685; -.
DR jPOST; P01833; -.
DR MassIVE; P01833; -.
DR PaxDb; P01833; -.
DR PeptideAtlas; P01833; -.
DR PRIDE; P01833; -.
DR ProteomicsDB; 51489; -.
DR ABCD; P01833; 20 sequenced antibodies.
DR Antibodypedia; 1594; 528 antibodies from 34 providers.
DR DNASU; 5284; -.
DR Ensembl; ENST00000356495.5; ENSP00000348888.4; ENSG00000162896.6.
DR GeneID; 5284; -.
DR KEGG; hsa:5284; -.
DR MANE-Select; ENST00000356495.5; ENSP00000348888.4; NM_002644.4; NP_002635.2.
DR UCSC; uc001hez.4; human.
DR CTD; 5284; -.
DR DisGeNET; 5284; -.
DR GeneCards; PIGR; -.
DR HGNC; HGNC:8968; PIGR.
DR HPA; ENSG00000162896; Tissue enhanced (intestine, salivary gland).
DR MIM; 173880; gene.
DR neXtProt; NX_P01833; -.
DR OpenTargets; ENSG00000162896; -.
DR PharmGKB; PA33300; -.
DR VEuPathDB; HostDB:ENSG00000162896; -.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR GeneTree; ENSGT00940000161667; -.
DR HOGENOM; CLU_020923_0_0_1; -.
DR InParanoid; P01833; -.
DR OMA; GAQNGRC; -.
DR OrthoDB; 570521at2759; -.
DR PhylomeDB; P01833; -.
DR TreeFam; TF334441; -.
DR PathwayCommons; P01833; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P01833; -.
DR BioGRID-ORCS; 5284; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; PIGR; human.
DR EvolutionaryTrace; P01833; -.
DR GeneWiki; Polymeric_immunoglobulin_receptor; -.
DR GenomeRNAi; 5284; -.
DR Pharos; P01833; Tbio.
DR PRO; PR:P01833; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P01833; protein.
DR Bgee; ENSG00000162896; Expressed in parotid gland and 140 other tissues.
DR Genevisible; P01833; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0001792; F:polymeric immunoglobulin receptor activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; IDA:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 5.
DR SMART; SM00409; IG; 5.
DR SMART; SM00406; IGv; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1859628,
FT ECO:0000269|PubMed:6526384"
FT CHAIN 19..764
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000014900"
FT CHAIN 19..603
FT /note="Secretory component"
FT /id="PRO_0000014901"
FT TOPO_DOM 19..638
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..120
FT /note="Ig-like V-type 1; required for binding to polymeric
FT IgA and IgM"
FT /evidence="ECO:0000269|PubMed:10229845,
FT ECO:0000269|PubMed:15530357"
FT DOMAIN 145..237
FT /note="Ig-like V-type 2"
FT DOMAIN 250..352
FT /note="Ig-like V-type 3"
FT DOMAIN 364..458
FT /note="Ig-like V-type 4"
FT DOMAIN 462..561
FT /note="Ig-like V-type 5"
FT REGION 609..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401,
FT ECO:0000269|PubMed:6526384"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401,
FT ECO:0000269|PubMed:6526384"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:6526384"
FT CARBOHYD 469
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, ECO:0000269|PubMed:6526384"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384"
FT DISULFID 40..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 56..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 152..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 257..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 271..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 371..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 385..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 482..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 486..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 496..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6526384"
FT DISULFID 503
FT /note="Interchain (with C-179 of IGHA2/constant region of
FT IgA2 heavy chain)"
FT /evidence="ECO:0000269|PubMed:32029686,
FT ECO:0000269|PubMed:8292260"
FT VARIANT 365
FT /note="G -> S (in dbSNP:rs2275531)"
FT /evidence="ECO:0000269|PubMed:1355431,
FT ECO:0000269|PubMed:1682231, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:1859628, ECO:0000269|PubMed:2920039,
FT ECO:0000269|PubMed:6526384"
FT /id="VAR_025283"
FT VARIANT 555
FT /note="T -> I (in dbSNP:rs7542760)"
FT /id="VAR_032822"
FT VARIANT 580
FT /note="A -> V (in dbSNP:rs291102)"
FT /id="VAR_003920"
FT CONFLICT 136
FT /note="D -> Q (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="N -> D (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="NQ -> DE (in Ref. 6; AA sequence and 7; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Missing (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="D -> N (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="E -> Q (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> Q (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> N (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="N -> D (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="N -> D (in Ref. 6; AA sequence and 7; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1XED"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1XED"
FT TURN 76..81
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1XED"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1XED"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1XED"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:1XED"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6UEA"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 163..178
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6UE7"
FT TURN 185..189
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5D4K"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6UE8"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:7K0C"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:5D4K"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:5D4K"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6LXW"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5D4K"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 421..430
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6UE9"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6UE8"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:5D4K"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:6UE8"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 525..533
FT /evidence="ECO:0007829|PDB:5D4K"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 540..548
FT /evidence="ECO:0007829|PDB:5D4K"
FT STRAND 551..565
FT /evidence="ECO:0007829|PDB:5D4K"
SQ SEQUENCE 764 AA; 83284 MW; 927461F4EB3B05C7 CRC64;
MLLFVLTCLL AVFPAISTKS PIFGPEEVNS VEGNSVSITC YYPPTSVNRH TRKYWCRQGA
RGGCITLISS EGYVSSKYAG RANLTNFPEN GTFVVNIAQL SQDDSGRYKC GLGINSRGLS
FDVSLEVSQG PGLLNDTKVY TVDLGRTVTI NCPFKTENAQ KRKSLYKQIG LYPVLVIDSS
GYVNPNYTGR IRLDIQGTGQ LLFSVVINQL RLSDAGQYLC QAGDDSNSNK KNADLQVLKP
EPELVYEDLR GSVTFHCALG PEVANVAKFL CRQSSGENCD VVVNTLGKRA PAFEGRILLN
PQDKDGSFSV VITGLRKEDA GRYLCGAHSD GQLQEGSPIQ AWQLFVNEES TIPRSPTVVK
GVAGGSVAVL CPYNRKESKS IKYWCLWEGA QNGRCPLLVD SEGWVKAQYE GRLSLLEEPG
NGTFTVILNQ LTSRDAGFYW CLTNGDTLWR TTVEIKIIEG EPNLKVPGNV TAVLGETLKV
PCHFPCKFSS YEKYWCKWNN TGCQALPSQD EGPSKAFVNC DENSRLVSLT LNLVTRADEG
WYWCGVKQGH FYGETAAVYV AVEERKAAGS RDVSLAKADA APDEKVLDSG FREIENKAIQ
DPRLFAEEKA VADTRDQADG SRASVDSGSS EEQGGSSRAL VSTLVPLGLV LAVGAVAVGV
ARARHRKNVD RVSIRSYRTD ISMSDFENSR EFGANDNMGA SSITQETSLG GKEEFVATTE
STTETKEPKK AKRSSKEEAE MAYKDFLLQS STVAAEAQDG PQEA
