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P01833 (PIGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polymeric immunoglobulin receptor

Short name=PIgR
Short name=Poly-Ig receptor
Alternative name(s):
Hepatocellular carcinoma-associated protein TB6

Cleaved into the following chain:

  1. Secretory component
Gene names
Name:PIGR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Secretory component: Secreted.

Post-translational modification

N-glycosylation is not necessary for Ig binding.

Sequence similarities

Contains 5 Ig-like V-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc receptor signaling pathway

Inferred from direct assay PubMed 22022593. Source: UniProt

detection of chemical stimulus involved in sensory perception of bitter taste

Inferred from direct assay PubMed 24248522. Source: UniProt

epidermal growth factor receptor signaling pathway

Inferred from direct assay PubMed 22022593. Source: UniProt

immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor

Inferred from direct assay PubMed 22022593. Source: UniProt

receptor clustering

Inferred from direct assay PubMed 22022593. Source: UniProt

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

   Cellular_componentextracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065PubMed 24248522. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.5. Source: ProtInc

plasma membrane

Inferred from direct assay PubMed 22022593. Source: UniProt

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionpolymeric immunoglobulin receptor activity

Inferred from direct assay PubMed 22022593. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.6 Ref.7
Chain19 – 764746Polymeric immunoglobulin receptor
PRO_0000014900
Chain19 – 603585Secretory component
PRO_0000014901

Regions

Topological domain19 – 638620Extracellular Potential
Transmembrane639 – 66123Helical; Potential
Topological domain662 – 764103Cytoplasmic Potential
Domain19 – 120102Ig-like V-type 1
Domain145 – 23793Ig-like V-type 2
Domain250 – 352103Ig-like V-type 3
Domain364 – 45895Ig-like V-type 4
Domain462 – 561100Ig-like V-type 5

Amino acid modifications

Modified residue6821Phosphoserine By similarity
Modified residue7351Phosphoserine By similarity
Glycosylation831N-linked (GlcNAc...) Ref.6 Ref.9 Ref.11 Ref.12
Glycosylation901N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10 Ref.11 Ref.12
Glycosylation1351N-linked (GlcNAc...) Ref.6 Ref.12
Glycosylation1861N-linked (GlcNAc...) Ref.6 Ref.11 Ref.12
Glycosylation4211N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Glycosylation4691N-linked (GlcNAc...) (complex) Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Glycosylation4991N-linked (GlcNAc...) Ref.6 Ref.11 Ref.12
Disulfide bond40 ↔ 110 Ref.6
Disulfide bond56 ↔ 64 Ref.6
Disulfide bond152 ↔ 220 Ref.6
Disulfide bond257 ↔ 325 Ref.6
Disulfide bond271 ↔ 279 Ref.6
Disulfide bond371 ↔ 441 Ref.6
Disulfide bond385 ↔ 395 Ref.6
Disulfide bond482 ↔ 544 Ref.6
Disulfide bond486 ↔ 520 Ref.6
Disulfide bond496 ↔ 503 Ref.6

Natural variations

Natural variant3651G → S. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs2275531 [ dbSNP | Ensembl ].
VAR_025283
Natural variant5551T → I.
Corresponds to variant rs7542760 [ dbSNP | Ensembl ].
VAR_032822
Natural variant5801A → V.
Corresponds to variant rs291102 [ dbSNP | Ensembl ].
VAR_003920

Experimental info

Sequence conflict1361D → Q AA sequence Ref.6
Sequence conflict1361D → Q AA sequence Ref.7
Sequence conflict1581N → D AA sequence Ref.6
Sequence conflict1581N → D AA sequence Ref.7
Sequence conflict208 – 2092NQ → DE AA sequence Ref.6
Sequence conflict208 – 2092NQ → DE AA sequence Ref.7
Sequence conflict2291Missing AA sequence Ref.6
Sequence conflict2291Missing AA sequence Ref.7
Sequence conflict2341D → N AA sequence Ref.6
Sequence conflict2341D → N AA sequence Ref.7
Sequence conflict2411E → Q AA sequence Ref.6
Sequence conflict2411E → Q AA sequence Ref.7
Sequence conflict2621E → Q AA sequence Ref.6
Sequence conflict2621E → Q AA sequence Ref.7
Sequence conflict2801D → N AA sequence Ref.6
Sequence conflict2801D → N AA sequence Ref.7
Sequence conflict3921N → D AA sequence Ref.6
Sequence conflict3921N → D AA sequence Ref.7
Sequence conflict5001N → D AA sequence Ref.6
Sequence conflict5001N → D AA sequence Ref.7

Secondary structure

........................ 764
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01833 [UniParc].

Last modified June 26, 2007. Version 4.
Checksum: 927461F4EB3B05C7

FASTA76483,284
        10         20         30         40         50         60 
MLLFVLTCLL AVFPAISTKS PIFGPEEVNS VEGNSVSITC YYPPTSVNRH TRKYWCRQGA 

        70         80         90        100        110        120 
RGGCITLISS EGYVSSKYAG RANLTNFPEN GTFVVNIAQL SQDDSGRYKC GLGINSRGLS 

       130        140        150        160        170        180 
FDVSLEVSQG PGLLNDTKVY TVDLGRTVTI NCPFKTENAQ KRKSLYKQIG LYPVLVIDSS 

       190        200        210        220        230        240 
GYVNPNYTGR IRLDIQGTGQ LLFSVVINQL RLSDAGQYLC QAGDDSNSNK KNADLQVLKP 

       250        260        270        280        290        300 
EPELVYEDLR GSVTFHCALG PEVANVAKFL CRQSSGENCD VVVNTLGKRA PAFEGRILLN 

       310        320        330        340        350        360 
PQDKDGSFSV VITGLRKEDA GRYLCGAHSD GQLQEGSPIQ AWQLFVNEES TIPRSPTVVK 

       370        380        390        400        410        420 
GVAGGSVAVL CPYNRKESKS IKYWCLWEGA QNGRCPLLVD SEGWVKAQYE GRLSLLEEPG 

       430        440        450        460        470        480 
NGTFTVILNQ LTSRDAGFYW CLTNGDTLWR TTVEIKIIEG EPNLKVPGNV TAVLGETLKV 

       490        500        510        520        530        540 
PCHFPCKFSS YEKYWCKWNN TGCQALPSQD EGPSKAFVNC DENSRLVSLT LNLVTRADEG 

       550        560        570        580        590        600 
WYWCGVKQGH FYGETAAVYV AVEERKAAGS RDVSLAKADA APDEKVLDSG FREIENKAIQ 

       610        620        630        640        650        660 
DPRLFAEEKA VADTRDQADG SRASVDSGSS EEQGGSSRAL VSTLVPLGLV LAVGAVAVGV 

       670        680        690        700        710        720 
ARARHRKNVD RVSIRSYRTD ISMSDFENSR EFGANDNMGA SSITQETSLG GKEEFVATTE 

       730        740        750        760 
STTETKEPKK AKRSSKEEAE MAYKDFLLQS STVAAEAQDG PQEA 

« Hide

References

« Hide 'large scale' references
[1]"The human transmembrane secretory component (poly-Ig receptor): molecular cloning, restriction fragment length polymorphism and chromosomal sublocalization."
Krajci P., Grzeschik K.H., Geurts van Kessel A.H., Olaisen B., Brandtzaeg P.
Hum. Genet. 87:642-648(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-365.
[2]"Molecular cloning and exon-intron mapping of the gene encoding human transmembrane secretory component (the poly-Ig receptor)."
Krajci P., Kvale D., Tasken K., Brandtzaeg P.
Eur. J. Immunol. 22:2309-2315(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-365.
[3]"Cloning and characterization of hepatocellular carcinoma associated-genes."
Dong X., Pang X., Cheng W.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-365.
Tissue: Small intestine.
[5]"Molecular cloning of the human transmembrane secretory component (poly-Ig receptor) and its mRNA expression in human tissues."
Krajci P., Solberg R., Sandberg M., Oyen O., Jahnsen T., Brandtzaeg P.
Biochem. Biophys. Res. Commun. 158:783-789(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-764, VARIANT SER-365.
[6]"The primary structure of human free secretory component and the arrangement of disulfide bonds."
Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M., Klingmueller D., Weber M.H., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 365:1489-1495(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-577, VARIANT SER-365, DISULFIDE BONDS, GLYCOSYLATION AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND ASN-499.
[7]"Determination of the molecular structure of the human free secretory component."
Eiffert H., Quentin E., Wiederhold M., Hillemeir S., Decker J., Weber M., Hilschmann N.
Biol. Chem. Hoppe-Seyler 372:119-128(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-577, VARIANT SER-365.
[8]"Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor."
Hughes G.J., Frutiger S., Savoy L.-A., Reason A.J., Morris H.R., Jaton J.-C.
FEBS Lett. 410:443-446(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 118-138; 212-230; 232-268; 273-288 AND 578-603.
[9]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 AND ASN-469.
Tissue: Bile.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469.
Tissue: Plasma.
[11]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186; ASN-421; ASN-469 AND ASN-499.
Tissue: Saliva.
[12]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND ASN-499.
Tissue: Milk.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421 AND ASN-469.
Tissue: Liver.
[14]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-469.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Crystal structure of a polymeric immunoglobulin binding fragment of the human polymeric immunoglobulin receptor."
Hamburger A.E., West A.P. Jr., Bjorkman P.J.
Structure 12:1925-1935(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-127.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S62403 mRNA. Translation: AAB20203.1.
S43449 expand/collapse EMBL AC list , S43437, S43441, S43442, S43443, S43444, S43445, S43446, S43447, S43448 Genomic DNA. Translation: AAB23176.1.
AF272149 mRNA. Translation: AAN65630.1.
CR749533 mRNA. Translation: CAH18339.1.
M24559 mRNA. Translation: AAA36102.1.
PIRQRHUGS. A46537.
RefSeqNP_002635.2. NM_002644.3.
UniGeneHs.497589.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEDX-ray1.90A/B/C/D/E/F19-127[»]
2OCWX-ray-A19-603[»]
3CHNOther1.00J353-458[»]
S19-603[»]
3CM9Other1.00J353-458[»]
S19-603[»]
ProteinModelPortalP01833.
SMRP01833. Positions 20-225, 356-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111302. 7 interactions.
IntActP01833. 4 interactions.
STRING9606.ENSP00000348888.

PTM databases

PhosphoSiteP01833.
UniCarbKBP01833.

Polymorphism databases

DMDM150421625.

Proteomic databases

PaxDbP01833.
PeptideAtlasP01833.
PRIDEP01833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356495; ENSP00000348888; ENSG00000162896.
GeneID5284.
KEGGhsa:5284.
UCSCuc001hez.3. human.

Organism-specific databases

CTD5284.
GeneCardsGC01M207101.
H-InvDBHIX0028583.
HGNCHGNC:8968. PIGR.
HPACAB009454.
HPA006154.
HPA012012.
MIM173880. gene.
neXtProtNX_P01833.
PharmGKBPA33300.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46873.
HOGENOMHOG000115545.
HOVERGENHBG008199.
InParanoidP01833.
KOK13073.
OMAYWCGVKQ.
OrthoDBEOG7PCJG8.
PhylomeDBP01833.
TreeFamTF334441.

Gene expression databases

BgeeP01833.
CleanExHS_PIGR.
GenevestigatorP01833.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07686. V-set. 5 hits.
[Graphical view]
SMARTSM00409. IG. 5 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIGR. human.
EvolutionaryTraceP01833.
GeneWikiPolymeric_immunoglobulin_receptor.
GenomeRNAi5284.
NextBio20420.
PROP01833.
SOURCESearch...

Entry information

Entry namePIGR_HUMAN
AccessionPrimary (citable) accession number: P01833
Secondary accession number(s): Q68D81, Q8IZY7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM