PIGR_RABIT
ID PIGR_RABIT Reviewed; 773 AA.
AC P01832;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 128.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6322002; DOI=10.1038/308037a0;
RA Mostov K.E., Friedlander M., Blobel G.;
RT "The receptor for transepithelial transport of IgA and IgM contains
RT multiple immunoglobulin-like domains.";
RL Nature 308:37-43(1984).
RN [2]
RP PROTEIN SEQUENCE OF 87-114 AND 410-428, GLYCOSYLATION AT ASN-88 (VARIANT
RP ASN-88), GLYCOSYLATION AT ASN-108 AND ASN-418, VARIANTS, AND POLYMORPHISM.
RX PubMed=3131339; DOI=10.1016/s0021-9258(18)68450-9;
RA Frutiger S., Hughes G.J., Hanly W.C., Jaton J.-C.;
RT "Rabbit secretory components of different allotypes vary in their
RT carbohydrate content and their sites of N-linked glycosylation.";
RL J. Biol. Chem. 263:8120-8125(1988).
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}.
CC -!- POLYMORPHISM: Three allotypes are known: allotype T61, allotype T62 and
CC allotype T63. The sequence shown is that of allotype T62.
CC {ECO:0000269|PubMed:3131339}.
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DR EMBL; X00412; CAA25118.1; -; mRNA.
DR PIR; A02111; QRRBG.
DR RefSeq; NP_001164516.1; NM_001171045.1.
DR AlphaFoldDB; P01832; -.
DR SMR; P01832; -.
DR STRING; 9986.ENSOCUP00000012314; -.
DR iPTMnet; P01832; -.
DR PRIDE; P01832; -.
DR GeneID; 100328593; -.
DR KEGG; ocu:100328593; -.
DR CTD; 5284; -.
DR eggNOG; ENOG502QPKT; Eukaryota.
DR InParanoid; P01832; -.
DR OrthoDB; 570521at2759; -.
DR Proteomes; UP000001811; 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; IDA: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; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT CHAIN 19..773
FT /note="Polymeric immunoglobulin receptor"
FT /id="PRO_0000014904"
FT CHAIN 19..615
FT /note="Secretory component"
FT /id="PRO_0000014905"
FT TOPO_DOM 19..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..131
FT /note="Ig-like V-type 1; required for binding to polymeric
FT IgA and IgM"
FT /evidence="ECO:0000250|UniProtKB:P01833"
FT DOMAIN 138..232
FT /note="Ig-like V-type 2"
FT DOMAIN 233..340
FT /note="Ig-like V-type 3"
FT DOMAIN 352..455
FT /note="Ig-like V-type 4"
FT DOMAIN 461..557
FT /note="Ig-like V-type 5"
FT REGION 619..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15083"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70570"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; in variant N-88"
FT /evidence="ECO:0000269|PubMed:3131339"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3131339"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3131339"
FT DISULFID 46..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 260..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 369..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 478..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 88
FT /note="K -> N (in allotype T61)"
FT VARIANT 94
FT /note="D -> E (in allotype T61)"
FT VARIANT 101..108
FT /note="TVDQLTQN -> YLNRLSQS (in allotype T61)"
FT VARIANT 110
FT /note="S -> T (in allotype T63)"
SQ SEQUENCE 773 AA; 83887 MW; DF2C44D2F1193C65 CRC64;
MALFLLTCLL AVFSAATAQS SLLGPSSIFG PGEVNVLEGD SVSITCYYPT TSVTRHSRKF
WCREEESGRC VTLASTGYTS QEYSGRGKLT DFPDKGEFVV TVDQLTQNDS GSYKCGVGVN
GRGLDFGVNV LVSQKPEPDD VVYKQYESYT VTITCPFTYA TRQLKKSFYK VEDGELVLII
DSSSKEAKDP RYKGRITLQI QSTTAKEFTV TIKHLQLNDA GQYVCQSGSD PTAEEQNVDL
RLLTPGLLYG NLGGSVTFEC ALDSEDANAV ASLRQVRGGN VVIDSQGTID PAFEGRILFT
KAENGHFSVV IAGLRKEDTG NYLCGVQSNG QSGDGPTQLR QLFVNEEIDV SRSPPVLKGF
PGGSVTIRCP YNPKRSDSHL QLYLWEGSQT RHLLVDSGEG LVQKDYTGRL ALFEEPGNGT
FSVVLNQLTA EDEGFYWCVS DDDESLTTSV KLQIVDGEPS PTIDKFTAVQ GEPVEITCHF
PCKYFSSEKY WCKWNDHGCE DLPTKLSSSG DLVKCNNNLV LTLTLDSVSE DDEGWYWCGA
KDGHEFEEVA AVRVELTEPA KVAVEPAKVP VDPAKAAPAP AEEKAKARCP VPRRRQWYPL
SRKLRTSCPE PRLLAEEVAV QSAEDPASGS RASVDASSAS GQSGSAKVLI STLVPLGLVL
AAGAMAVAIA RARHRRNVDR VSIGSYRTDI SMSDLENSRE FGAIDNPSAC PDARETALGG
KDELATATES TVEIEEPKKA KRSSKEEADL AYSAFLLQSN TIAAEHQDGP KEA
