PIGR_MOUSE
ID PIGR_MOUSE Reviewed; 771 AA.
AC O70570;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=7836758;
RA Piskurich J.F., Blanchard M.H., Youngman K.R., France J.A., Kaetzel C.S.;
RT "Molecular cloning of the mouse polymeric Ig receptor. Functional regions
RT of the molecule are conserved among five mammalian species.";
RL J. Immunol. 154:1735-1747(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9409786; DOI=10.1016/s0378-1119(97)00447-2;
RA Martin M.G., Gutierrez E.M., Lam J.T., Li T.W.H., Wang J.;
RT "Genomic cloning and structural analysis of the murine polymeric receptor
RT (pIgR) gene and promoter region.";
RL Gene 201:189-197(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129; TISSUE=Liver;
RX PubMed=10481312; DOI=10.1023/a:1008981312682;
RA de Groot N., van Kuik-Romeijn P., Lee S.H., de Boer H.A.;
RT "Over-expression of the murine polymeric immunoglobulin receptor gene in
RT the mammary gland of transgenic mice.";
RL Transgenic Res. 8:125-135(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND SER-742, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- 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: 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; U06431; AAA67440.1; -; mRNA.
DR EMBL; U83434; AAC53585.1; -; Genomic_DNA.
DR EMBL; U83427; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83428; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83429; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83430; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83431; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83432; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; U83433; AAC53585.1; JOINED; Genomic_DNA.
DR EMBL; Y16524; CAA76272.1; -; Genomic_DNA.
DR EMBL; Y16525; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16526; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16527; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16528; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16529; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16530; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16531; CAA76272.1; JOINED; Genomic_DNA.
DR EMBL; Y16532; CAA76272.1; JOINED; Genomic_DNA.
DR CCDS; CCDS15260.1; -.
DR RefSeq; NP_035212.2; NM_011082.3.
DR PDB; 4NOB; X-ray; 1.51 A; A=20-133.
DR PDB; 4NOF; X-ray; 1.65 A; A/B=133-245.
DR PDB; 7JG2; EM; 3.30 A; E=19-567.
DR PDBsum; 4NOB; -.
DR PDBsum; 4NOF; -.
DR PDBsum; 7JG2; -.
DR AlphaFoldDB; O70570; -.
DR SMR; O70570; -.
DR BioGRID; 202157; 2.
DR STRING; 10090.ENSMUSP00000027675; -.
DR GlyGen; O70570; 7 sites.
DR iPTMnet; O70570; -.
DR PhosphoSitePlus; O70570; -.
DR CPTAC; non-CPTAC-3738; -.
DR jPOST; O70570; -.
DR MaxQB; O70570; -.
DR PaxDb; O70570; -.
DR PeptideAtlas; O70570; -.
DR PRIDE; O70570; -.
DR ProteomicsDB; 288210; -.
DR ABCD; O70570; 4 sequenced antibodies.
DR Antibodypedia; 1594; 528 antibodies from 34 providers.
DR DNASU; 18703; -.
DR Ensembl; ENSMUST00000027675; ENSMUSP00000027675; ENSMUSG00000026417.
DR GeneID; 18703; -.
DR KEGG; mmu:18703; -.
DR UCSC; uc011wrk.1; mouse.
DR CTD; 5284; -.
DR MGI; MGI:103080; Pigr.
DR VEuPathDB; HostDB:ENSMUSG00000026417; -.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR GeneTree; ENSGT00940000161667; -.
DR HOGENOM; CLU_020923_0_0_1; -.
DR InParanoid; O70570; -.
DR OMA; GAQNGRC; -.
DR OrthoDB; 570521at2759; -.
DR PhylomeDB; O70570; -.
DR TreeFam; TF334441; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18703; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pigr; mouse.
DR PRO; PR:O70570; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O70570; protein.
DR Bgee; ENSMUSG00000026417; Expressed in ileal epithelium and 84 other tissues.
DR ExpressionAtlas; O70570; baseline and differential.
DR Genevisible; O70570; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0001792; F:polymeric immunoglobulin receptor activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0038093; P:Fc receptor signaling pathway; ISO:MGI.
DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
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; 3.
PE 1: Evidence at protein level;
KW 3D-structure; 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..771
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000014902"
FT CHAIN 19..611
FT /note="Secretory component"
FT /id="PRO_0000014903"
FT TOPO_DOM 19..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..120
FT /note="Ig-like V-type 1; required for binding to polymeric
FT IgA and IgM"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 135..237
FT /note="Ig-like V-type 2"
FT DOMAIN 245..351
FT /note="Ig-like V-type 3"
FT DOMAIN 352..457
FT /note="Ig-like V-type 4"
FT DOMAIN 463..563
FT /note="Ig-like V-type 5"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
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 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..110
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 370..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 484..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 159
FT /note="A -> V (in Ref. 1; AAA67440)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="V -> A (in Ref. 1; AAA67440)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="G -> R (in Ref. 1; AAA67440)"
FT /evidence="ECO:0000305"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4NOB"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4NOB"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4NOB"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4NOB"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4NOB"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4NOB"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:4NOB"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4NOF"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4NOF"
FT TURN 185..190
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4NOF"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:4NOF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:4NOF"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:7JG2"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:7JG2"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 418..429
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 493..500
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:7JG2"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 542..550
FT /evidence="ECO:0007829|PDB:7JG2"
FT STRAND 558..565
FT /evidence="ECO:0007829|PDB:7JG2"
SQ SEQUENCE 771 AA; 84999 MW; 78C81302EC710730 CRC64;
MRLYLFTLLV TVFSGVSTKS PIFGPQEVSS IEGDSVSITC YYPDTSVNRH TRKYWCRQGA
SGMCTTLISS NGYLSKEYSG RANLINFPEN NTFVINIEQL TQDDTGSYKC GLGTSNRGLS
FDVSLEVSQV PELPSDTHVY TKDIGRNVTI ECPFKRENAP SKKSLCKKTN QSCELVIDST
EKVNPSYIGR AKLFMKGTDL TVFYVNISHL THNDAGLYIC QAGEGPSADK KNVDLQVLAP
EPELLYKDLR SSVTFECDLG REVANEAKYL CRMNKETCDV IINTLGKRDP DFEGRILITP
KDDNGRFSVL ITGLRKEDAG HYQCGAHSSG LPQEGWPIQT WQLFVNEEST IPNRRSVVKG
VTGGSVAIAC PYNPKESSSL KYWCRWEGDG NGHCPVLVGT QAQVQEEYEG RLALFDQPGN
GTYTVILNQL TTEDAGFYWC LTNGDSRWRT TIELQVAEAT REPNLEVTPQ NATAVLGETF
TVSCHYPCKF YSQEKYWCKW SNKGCHILPS HDEGARQSSV SCDQSSQLVS MTLNPVSKED
EGWYWCGVKQ GQTYGETTAI YIAVEERTRG SSHVNPTDAN ARAKVALEEE VVDSSISEKE
NKAIPNPGPF ANEREIQNVG DQAQENRASG DAGSADGQSR SSSSKVLFST LVPLGLVLAV
GAIAVWVARV RHRKNVDRMS ISSYRTDISM ADFKNSRDLG GNDNMGASPD TQQTVIEGKD
EIVTTTECTA EPEESKKAKR SSKEEADMAY SAFLLQSSTI AAQVHDGPQE A
