SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01833

- PIGR_HUMAN

UniProt

P01833 - PIGR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Polymeric immunoglobulin receptor
Gene
PIGR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. polymeric immunoglobulin receptor activity Source: UniProt
Complete GO annotation...

GO - Biological processi

  1. Fc receptor signaling pathway Source: UniProt
  2. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProt
  3. epidermal growth factor receptor signaling pathway Source: UniProt
  4. immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor Source: UniProt
  5. receptor clustering Source: UniProt
  6. retina homeostasis Source: UniProt
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:PIGR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8968. PIGR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 638620Extracellular Reviewed prediction
Add
BLAST
Transmembranei639 – 66123Helical; Reviewed prediction
Add
BLAST
Topological domaini662 – 764103Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: UniProt
  5. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 Publications
Add
BLAST
Chaini19 – 764746Polymeric immunoglobulin receptor
PRO_0000014900Add
BLAST
Chaini19 – 603585Secretory component
PRO_0000014901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 1101 Publication
Disulfide bondi56 ↔ 641 Publication
Glycosylationi83 – 831N-linked (GlcNAc...)4 Publications
Glycosylationi90 – 901N-linked (GlcNAc...)5 Publications
Glycosylationi135 – 1351N-linked (GlcNAc...)2 Publications
Disulfide bondi152 ↔ 2201 Publication
Glycosylationi186 – 1861N-linked (GlcNAc...)3 Publications
Disulfide bondi257 ↔ 3251 Publication
Disulfide bondi271 ↔ 2791 Publication
Disulfide bondi371 ↔ 4411 Publication
Disulfide bondi385 ↔ 3951 Publication
Glycosylationi421 – 4211N-linked (GlcNAc...)6 Publications
Glycosylationi469 – 4691N-linked (GlcNAc...) (complex)7 Publications
Disulfide bondi482 ↔ 5441 Publication
Disulfide bondi486 ↔ 5201 Publication
Disulfide bondi496 ↔ 5031 Publication
Glycosylationi499 – 4991N-linked (GlcNAc...)3 Publications
Modified residuei682 – 6821Phosphoserine By similarity
Modified residuei735 – 7351Phosphoserine By similarity

Post-translational modificationi

N-glycosylation is not necessary for Ig binding.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01833.
PeptideAtlasiP01833.
PRIDEiP01833.

PTM databases

PhosphoSiteiP01833.
UniCarbKBiP01833.

Expressioni

Gene expression databases

BgeeiP01833.
CleanExiHS_PIGR.
GenevestigatoriP01833.

Organism-specific databases

HPAiCAB009454.
HPA006154.
HPA012012.

Interactioni

Protein-protein interaction databases

BioGridi111302. 7 interactions.
IntActiP01833. 4 interactions.
STRINGi9606.ENSP00000348888.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 316
Beta strandi36 – 416
Helixi46 – 505
Beta strandi53 – 575
Beta strandi65 – 728
Turni76 – 816
Beta strandi82 – 876
Turni88 – 914
Beta strandi92 – 976
Helixi102 – 1043
Beta strandi106 – 1138
Helixi115 – 1173
Beta strandi120 – 1278

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP01833.
SMRiP01833. Positions 20-241, 247-327, 356-441.

Miscellaneous databases

EvolutionaryTraceiP01833.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 120102Ig-like V-type 1
Add
BLAST
Domaini145 – 23793Ig-like V-type 2
Add
BLAST
Domaini250 – 352103Ig-like V-type 3
Add
BLAST
Domaini364 – 45895Ig-like V-type 4
Add
BLAST
Domaini462 – 561100Ig-like V-type 5
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46873.
HOGENOMiHOG000115545.
HOVERGENiHBG008199.
InParanoidiP01833.
KOiK13073.
OMAiYWCGVKQ.
OrthoDBiEOG7PCJG8.
PhylomeDBiP01833.
TreeFamiTF334441.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 5 hits.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01833-1 [UniParc]FASTAAdd to Basket

« Hide

MLLFVLTCLL AVFPAISTKS PIFGPEEVNS VEGNSVSITC YYPPTSVNRH    50
TRKYWCRQGA RGGCITLISS EGYVSSKYAG RANLTNFPEN GTFVVNIAQL 100
SQDDSGRYKC GLGINSRGLS FDVSLEVSQG PGLLNDTKVY TVDLGRTVTI 150
NCPFKTENAQ KRKSLYKQIG LYPVLVIDSS GYVNPNYTGR IRLDIQGTGQ 200
LLFSVVINQL RLSDAGQYLC QAGDDSNSNK KNADLQVLKP EPELVYEDLR 250
GSVTFHCALG PEVANVAKFL CRQSSGENCD VVVNTLGKRA PAFEGRILLN 300
PQDKDGSFSV VITGLRKEDA GRYLCGAHSD GQLQEGSPIQ AWQLFVNEES 350
TIPRSPTVVK GVAGGSVAVL CPYNRKESKS IKYWCLWEGA QNGRCPLLVD 400
SEGWVKAQYE GRLSLLEEPG NGTFTVILNQ LTSRDAGFYW CLTNGDTLWR 450
TTVEIKIIEG EPNLKVPGNV TAVLGETLKV PCHFPCKFSS YEKYWCKWNN 500
TGCQALPSQD EGPSKAFVNC DENSRLVSLT LNLVTRADEG WYWCGVKQGH 550
FYGETAAVYV AVEERKAAGS RDVSLAKADA APDEKVLDSG FREIENKAIQ 600
DPRLFAEEKA VADTRDQADG SRASVDSGSS EEQGGSSRAL VSTLVPLGLV 650
LAVGAVAVGV ARARHRKNVD RVSIRSYRTD ISMSDFENSR EFGANDNMGA 700
SSITQETSLG GKEEFVATTE STTETKEPKK AKRSSKEEAE MAYKDFLLQS 750
STVAAEAQDG PQEA 764
Length:764
Mass (Da):83,284
Last modified:June 26, 2007 - v4
Checksum:i927461F4EB3B05C7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti365 – 3651G → S.6 Publications
Corresponds to variant rs2275531 [ dbSNP | Ensembl ].
VAR_025283
Natural varianti555 – 5551T → I.
Corresponds to variant rs7542760 [ dbSNP | Ensembl ].
VAR_032822
Natural varianti580 – 5801A → V.
Corresponds to variant rs291102 [ dbSNP | Ensembl ].
VAR_003920

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361D → Q AA sequence 1 Publication
Sequence conflicti136 – 1361D → Q AA sequence 1 Publication
Sequence conflicti158 – 1581N → D AA sequence 1 Publication
Sequence conflicti158 – 1581N → D AA sequence 1 Publication
Sequence conflicti208 – 2092NQ → DE AA sequence 1 Publication
Sequence conflicti208 – 2092NQ → DE AA sequence 1 Publication
Sequence conflicti229 – 2291Missing AA sequence 1 Publication
Sequence conflicti229 – 2291Missing AA sequence 1 Publication
Sequence conflicti234 – 2341D → N AA sequence 1 Publication
Sequence conflicti234 – 2341D → N AA sequence 1 Publication
Sequence conflicti241 – 2411E → Q AA sequence 1 Publication
Sequence conflicti241 – 2411E → Q AA sequence 1 Publication
Sequence conflicti262 – 2621E → Q AA sequence 1 Publication
Sequence conflicti262 – 2621E → Q AA sequence 1 Publication
Sequence conflicti280 – 2801D → N AA sequence 1 Publication
Sequence conflicti280 – 2801D → N AA sequence 1 Publication
Sequence conflicti392 – 3921N → D AA sequence 1 Publication
Sequence conflicti392 – 3921N → D AA sequence 1 Publication
Sequence conflicti500 – 5001N → D AA sequence 1 Publication
Sequence conflicti500 – 5001N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S62403 mRNA. Translation: AAB20203.1.
S43449
, 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.
CCDSiCCDS1474.1.
PIRiA46537. QRHUGS.
RefSeqiNP_002635.2. NM_002644.3.
UniGeneiHs.497589.

Genome annotation databases

EnsembliENST00000356495; ENSP00000348888; ENSG00000162896.
GeneIDi5284.
KEGGihsa:5284.
UCSCiuc001hez.3. human.

Polymorphism databases

DMDMi150421625.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S62403 mRNA. Translation: AAB20203.1 .
S43449
, 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 .
CCDSi CCDS1474.1.
PIRi A46537. QRHUGS.
RefSeqi NP_002635.2. NM_002644.3.
UniGenei Hs.497589.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XED X-ray 1.90 A/B/C/D/E/F 19-127 [» ]
2OCW X-ray - A 19-603 [» ]
3CHN Other 1.00 J 353-458 [» ]
S 19-603 [» ]
3CM9 Other 1.00 J 353-458 [» ]
S 19-603 [» ]
ProteinModelPortali P01833.
SMRi P01833. Positions 20-241, 247-327, 356-441.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111302. 7 interactions.
IntActi P01833. 4 interactions.
STRINGi 9606.ENSP00000348888.

PTM databases

PhosphoSitei P01833.
UniCarbKBi P01833.

Polymorphism databases

DMDMi 150421625.

Proteomic databases

PaxDbi P01833.
PeptideAtlasi P01833.
PRIDEi P01833.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356495 ; ENSP00000348888 ; ENSG00000162896 .
GeneIDi 5284.
KEGGi hsa:5284.
UCSCi uc001hez.3. human.

Organism-specific databases

CTDi 5284.
GeneCardsi GC01M207101.
H-InvDB HIX0028583.
HGNCi HGNC:8968. PIGR.
HPAi CAB009454.
HPA006154.
HPA012012.
MIMi 173880. gene.
neXtProti NX_P01833.
PharmGKBi PA33300.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46873.
HOGENOMi HOG000115545.
HOVERGENi HBG008199.
InParanoidi P01833.
KOi K13073.
OMAi YWCGVKQ.
OrthoDBi EOG7PCJG8.
PhylomeDBi P01833.
TreeFami TF334441.

Miscellaneous databases

ChiTaRSi PIGR. human.
EvolutionaryTracei P01833.
GeneWikii Polymeric_immunoglobulin_receptor.
GenomeRNAii 5284.
NextBioi 20420.
PROi P01833.
SOURCEi Search...

Gene expression databases

Bgeei P01833.
CleanExi HS_PIGR.
Genevestigatori P01833.

Family and domain databases

Gene3Di 2.60.40.10. 5 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view ]
Pfami PF07686. V-set. 5 hits.
[Graphical view ]
SMARTi SM00409. IG. 5 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: GLYCOSYLATION AT ASN-469.
  15. 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.

Entry informationi

Entry nameiPIGR_HUMAN
AccessioniPrimary (citable) accession number: P01833
Secondary accession number(s): Q68D81, Q8IZY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi