PIGR_PIG
ID PIGR_PIG Reviewed; 102 AA.
AC Q29244;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Polymeric immunoglobulin receptor;
DE Short=PIgR;
DE Short=Poly-Ig receptor;
DE Flags: Fragment;
GN Name=PIGR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
CC -!- FUNCTION: Mediates selective transcytosis of polymeric IgA and IgM
CC across mucosal epithelial cells. Binds polymeric IgA and IgM at the
CC basolateral surface of epithelial cells. The complex is then
CC transported across the cell to be secreted at the apical surface.
CC During this process, a cleavage occurs that separates the extracellular
CC (known as the secretory component) from the transmembrane segment (By
CC similarity). Through its N-linked glycans ensures anchoring of
CC secretory IgA (sIgA) molecules to mucus lining the epithelial surface
CC to neutralize extracellular pathogens. On its own (free form) may act
CC as a non-specific microbial scavenger to prevent pathogen interaction
CC with epithelial cells (By similarity). {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBUNIT: Interacts (mainly via CDR1-like domain) with dimeric IgA.
CC Interacts (mainly via CDR2-like domain) with pentameric IgM (By
CC similarity). Either free or part of the secretory IgA (sIgA) complex
CC that consists of two, four or five IgA monomers, and two additional
CC non-Ig polypeptides, namely the JCHAIN and the secretory component (the
CC proteolytic product of PIGR). Free secretory component interacts with
CC bacterial antigens toxA of C. difficile and eae of E. coli (By
CC similarity). {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01833};
CC Single-pass type I membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:P01833}.
CC -!- PTM: N-glycosylated. N-glycosylation is required for anchoring IgA
CC molecules to mucus, but is not necessary for Ig binding.
CC {ECO:0000250|UniProtKB:P01833}.
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DR EMBL; F14851; CAA23294.1; -; mRNA.
DR STRING; 9823.ENSSSCP00000016593; -.
DR PaxDb; Q29244; -.
DR PeptideAtlas; Q29244; -.
DR PRIDE; Q29244; -.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Secreted; Transmembrane.
FT CHAIN <1..>102
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000072702"
FT NON_TER 1
FT NON_TER 102
SQ SEQUENCE 102 AA; 11206 MW; 82C915264B1508E8 CRC64;
DLQVLKPEPE LIYGDLRGSV TFDCALGQEM ANVAKFLCQL KNGKTCNVVI NTLGKKAQDF
EGRILLTPKE NSHFSVHITG LRKEDAGHYL CGXHPDGEPK EG
