PIGR_RAT
ID PIGR_RAT Reviewed; 769 AA.
AC P15083;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 152.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2776882; DOI=10.1016/0014-5793(89)81034-8;
RA Banting G., Brake B., Braghetta P., Luzio J.P., Stanley K.K.;
RT "Intracellular targeting signals of polymeric immunoglobulin receptors are
RT highly conserved between species.";
RL FEBS Lett. 254:177-183(1989).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678; SER-687 AND SER-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; X15741; CAA33758.1; -; mRNA.
DR PIR; S05407; QRRTGS.
DR RefSeq; NP_036855.3; NM_012723.4.
DR AlphaFoldDB; P15083; -.
DR SMR; P15083; -.
DR CORUM; P15083; -.
DR STRING; 10116.ENSRNOP00000005853; -.
DR GlyGen; P15083; 4 sites.
DR iPTMnet; P15083; -.
DR PhosphoSitePlus; P15083; -.
DR PaxDb; P15083; -.
DR PRIDE; P15083; -.
DR GeneID; 25046; -.
DR KEGG; rno:25046; -.
DR UCSC; RGD:3328; rat.
DR CTD; 5284; -.
DR RGD; 3328; Pigr.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR InParanoid; P15083; -.
DR OrthoDB; 570521at2759; -.
DR PhylomeDB; P15083; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P15083; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
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:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:RGD.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:RGD.
DR GO; GO:0001792; F:polymeric immunoglobulin receptor activity; ISO:RGD.
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:RGD.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0038093; P:Fc receptor signaling pathway; ISO:RGD.
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:RGD.
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; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT CHAIN 19..769
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000014906"
FT CHAIN 19..611
FT /note="Secretory component"
FT /id="PRO_0000014907"
FT TOPO_DOM 19..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..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 135..237
FT /note="Ig-like V-type 2"
FT DOMAIN 240..341
FT /note="Ig-like V-type 3"
FT DOMAIN 353..457
FT /note="Ig-like V-type 4"
FT DOMAIN 463..563
FT /note="Ig-like V-type 5"
FT REGION 569..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
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 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"
SQ SEQUENCE 769 AA; 84798 MW; 5F849303400255A7 CRC64;
MRLSLFALLV TVFSGVSTQS PIFGPQDVSS IEGNSVSITC YYPDTSVNRH TRKYWCRQGA
NGYCATLISS NGYLSKEYSG RASLINFPEN STFVINIAHL TQEDTGSYKC GLGTTNRGLF
FDVSLEVSQV PEFPNDTHVY TKDIGRTVTI ECRFKEGNAH SKKSLCKKRG EACEVVIDST
EYVDPSYKDR AILFMKGTSR DIFYVNISHL IPSDAGLYVC QAGEGPSADK NNADLQVLEP
EPELLYKDLR SSVTFECDLG REVANDAKYL CRKNKETCDV IINTLGKRDP AFEGRILLTP
RDDNGRFSVL ITGLRKEDAG HYQCGAHSSG LPQEGWPVQA WQLFVNEEST IPNSRSVVKG
VTGGSVAIVC PYNPKESSSL KYWCHWEADE NGRCPVLVGT QALVQEGYEG RLALFDQPGS
GAYTVILNQL TTQDSGFYWC LTDGDSRWRT TIELQVAEAT KKPDLEVTPQ NATAVIGETF
TISCHYPCKF YSQEKYWCKW SNDGCHILPS HDEGARQSSV SCDQSSQIVS MTLNPVKKED
EGWYWCGVKE GQVYGETTAI YVAVEERTRG SPHINPTDAN ARAKDAPEEE AMESSVREDE
NKANLDPRLF ADEREIQNAG DQAQENRASG NAGSAGGQSG SSKVLFSTLV PLGLVLAVGA
VAVWVARVRH RKNVDRMSIS SYRTDISMGD FRNSRDLGGN DNMGATPDTQ ETVLEGKDEI
ETTTECTTEP EESKKAKRSS KEEADMAYSA FLFQSSTIAA QVHDGPQEA
