PIGR_BOVIN
ID PIGR_BOVIN Reviewed; 757 AA.
AC P81265;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Polymeric immunoglobulin receptor;
DE Short=PIgR;
DE Short=Poly-Ig receptor;
DE Contains:
DE RecName: Full=Secretory component;
DE Flags: Precursor;
GN Name=PIGR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Mammary gland, and Small intestine;
RX PubMed=7880445; DOI=10.1089/dna.1995.14.251;
RA Kulseth M.A., Krajci P., Myklebost O., Rogne S.;
RT "Cloning and characterization of two forms of bovine polymeric
RT immunoglobulin receptor cDNA.";
RL DNA Cell Biol. 14:251-256(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=7590352; DOI=10.1016/0378-1119(95)00520-g;
RA Verbeet M.P., Vermeer H., Warmerdam G.C., de Boer H.A., Lee S.H.;
RT "Cloning and characterization of the bovine polymeric immunoglobulin
RT receptor-encoding cDNA.";
RL Gene 164:329-333(1995).
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:0000250|UniProtKB:P01833}.
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. On its own
CC (free form) may act as a non-specific microbial scavenger to prevent
CC pathogen interaction with epithelial cells.
CC {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.
CC {ECO:0000250|UniProtKB:P01833}.
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). Free secretory component
CC interacts with bacterial antigens toxA of C. difficile and eae of E.
CC coli. {ECO:0000250|UniProtKB:P01833}.
CC -!- SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell
CC membrane {ECO:0000250|UniProtKB:P01833}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secretory component]: Secreted
CC {ECO:0000250|UniProtKB:P01833}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P81265-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P81265-2; Sequence=VSP_002547;
CC -!- TISSUE SPECIFICITY: Found in mammary gland, jejunum, lung, kidney and
CC small intestine.
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:0000250|UniProtKB:P01833}.
CC -!- PTM: In the absence of dimeric IgA, Ser-727 is phosphorylated which
CC allows PIGR to function normally.
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; L04797; AAC41620.1; -; mRNA.
DR EMBL; X81371; CAA57136.1; -; mRNA.
DR PIR; I45956; I45956.
DR PIR; S48841; S48841.
DR RefSeq; NP_776568.1; NM_174143.1.
DR AlphaFoldDB; P81265; -.
DR SMR; P81265; -.
DR STRING; 9913.ENSBTAP00000026377; -.
DR CarbonylDB; P81265; -.
DR PaxDb; P81265; -.
DR PeptideAtlas; P81265; -.
DR PRIDE; P81265; -.
DR GeneID; 281401; -.
DR KEGG; bta:281401; -.
DR CTD; 5284; -.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR InParanoid; P81265; -.
DR OrthoDB; 570521at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; ISS:UniProtKB.
DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; ISS: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; 4.
DR SMART; SM00409; IG; 5.
DR SMART; SM00406; IGv; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..757
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000014898"
FT CHAIN 19..599
FT /note="Secretory component"
FT /id="PRO_0000014899"
FT TOPO_DOM 19..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..126
FT /note="Ig-like V-type 1; required for binding to polymeric
FT IgA and IgM"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 145..237
FT /note="Ig-like V-type 2"
FT DOMAIN 250..341
FT /note="Ig-like V-type 3"
FT DOMAIN 353..457
FT /note="Ig-like V-type 4"
FT DOMAIN 461..560
FT /note="Ig-like V-type 5"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 56..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 257..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 370..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 384..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 481..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 485..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 495..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 129..346
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_002547"
FT VARIANT 29
FT /note="T -> S"
FT VARIANT 142
FT /note="V -> I"
FT VARIANT 404
FT /note="I -> M"
FT VARIANT 413
FT /note="A -> V"
FT VARIANT 435
FT /note="T -> A"
SQ SEQUENCE 757 AA; 82435 MW; DCED67FDD6A6E6C6 CRC64;
MSRLFLACLL AIFPVVSMKS PIFGPEEVTS VEGRSVSIKC YYPPTSVNRH TRKYWCRQGA
QGRCTTLISS EGYVSDDYVG RANLTNFPES GTFVVDISHL THKDSGRYKC GLGISSRGLN
FDVSLEVSQD PAQASHAHVY TVDLGRTVTI NCPFTRANSE KRKSLCKKTI QDCFQVVDST
GYVSNSYKDR AHISILGTNT LVFSVVINRV KLSDAGMYVC QAGDDAKADK INIDLQVLEP
EPELVYGDLR SSVTFDCSLG PEVANVPKFL CQKKNGGACN VVINTLGKKA QDFQGRIVSV
PKDNGVFSVH ITSLRKEDAG RYVCGAQPEG EPQDGWPVQA WQLFVNEETA IPASPSVVKG
VRGGSVTVSC PYNPKDANSA KYWCHWEEAQ NGRCPRLVES RGLIKEQYEG RLALLTEPGN
GTYTVILNQL TDQDTGFYWC VTDGDTRWIS TVELKVVQGE PSLKVPKNVT AWLGEPLKLS
CHFPCKFYSF EKYWCKWSNR GCSALPTQND GPSQAFVSCD QNSQVVSLNL DTVTKEDEGW
YWCGVKEGPR YGETAAVYVA VESRVKGSQG AKQVKAAPAG AAIQSRAGEI QNKALLDPSF
FAKESVKDAA GGPGAPADPG RPTGYSGSSK ALVSTLVPLA LVLVAGVVAI GVVRARHRKN
VDRISIRSYR TDISMSDFEN SRDFEGRDNM GASPEAQETS LGGKDEFATT TEDTVESKEP
KKAKRSSKEE ADEAFTTFLL QAKNLASAAT QNGPTEA
