Reviewed, UniProtKB/Swiss-Prot P01833 (PIGR_HUMAN)

Names and origin

Protein names

Recommended name:
    Polymeric immunoglobulin receptor
      Short name=Poly-Ig receptor
      Short name=PIgR
Alternative name(s):
    Hepatocellular carcinoma-associated protein TB6
Cleaved into the following chain:
    1- Recommended name:
            Secretory component

Gene names

Name:

PIGR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	764 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.5 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SGK1	O00141	1	EBI-1052371,EBI-1042854

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.6 Ref.7

Chain

19 – 764

746

Polymeric immunoglobulin receptor

PRO_0000014900

Chain

19 – 603

585

Secretory component

PRO_0000014901

Regions

Topological domain

19 – 638

620

Extracellular Potential

Transmembrane

639 – 661

23

Potential

Topological domain

662 – 764

103

Cytoplasmic Potential

Domain

19 – 120

102

Ig-like V-type 1

Domain

145 – 237

93

Ig-like V-type 2

Domain

250 – 352

103

Ig-like V-type 3

Domain

364 – 458

95

Ig-like V-type 4

Domain

462 – 561

100

Ig-like V-type 5

Amino acid modifications

Modified residue

682

1

Phosphoserine By similarity

Modified residue

734

1

Phosphoserine By similarity

Glycosylation

83

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.11 Ref.12

Glycosylation

90

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.11 Ref.12 Ref.10

Glycosylation

135

1

N-linked (GlcNAc...) Ref.6 Ref.12

Glycosylation

186

1

N-linked (GlcNAc...) Ref.6 Ref.11 Ref.12

Glycosylation

421

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.11 Ref.12 Ref.10 Ref.14

Glycosylation

469

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.11 Ref.12 Ref.10 Ref.14

Glycosylation

499

1

N-linked (GlcNAc...) Ref.6 Ref.11 Ref.12

Disulfide bond

40 ↔ 110

Ref.6

Disulfide bond

56 ↔ 64

Ref.6

Disulfide bond

152 ↔ 220

Ref.6

Disulfide bond

257 ↔ 325

Ref.6

Disulfide bond

271 ↔ 279

Ref.6

Disulfide bond

371 ↔ 441

Ref.6

Disulfide bond

385 ↔ 395

Ref.6

Disulfide bond

482 ↔ 544

Ref.6

Disulfide bond

486 ↔ 520

Ref.6

Disulfide bond

496 ↔ 503

Ref.6

Natural variations

Natural variant

365

1

G → S: dbSNP rs2275531. Ref.6 Ref.7 Ref.1 Ref.2 Ref.4 Ref.5

VAR_025283

Natural variant

555

1

T → I: dbSNP rs7542760.

VAR_032822

Natural variant

580

1

A → V: dbSNP rs291102.

VAR_003920

Experimental info

Sequence conflict

136

1

D → Q Ref.6

Sequence conflict

136

1

D → Q Ref.7

Sequence conflict

158

1

N → D Ref.6

Sequence conflict

158

1

N → D Ref.7

Sequence conflict

208 – 209

2

NQ → DE Ref.6

Sequence conflict

208 – 209

2

NQ → DE Ref.7

Sequence conflict

229

1

Missing Ref.6

Sequence conflict

229

1

Missing Ref.7

Sequence conflict

234

1

D → N Ref.6

Sequence conflict

234

1

D → N Ref.7

Sequence conflict

241

1

E → Q Ref.6

Sequence conflict

241

1

E → Q Ref.7

Sequence conflict

262

1

E → Q Ref.6

Sequence conflict

262

1

E → Q Ref.7

Sequence conflict

280

1

D → N Ref.6

Sequence conflict

280

1

D → N Ref.7

Sequence conflict

392

1

N → D Ref.6

Sequence conflict

392

1

N → D Ref.7

Sequence conflict

500

1

N → D Ref.6

Sequence conflict

500

1

N → D Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

764

Helix Strand Turn

Details...

Beta strand

26 – 31

6

Beta strand

36 – 41

6

Helix

46 – 50

5

Beta strand

53 – 57

5

Beta strand

65 – 72

8

Turn

76 – 81

6

Beta strand

82 – 87

6

Turn

88 – 91

4

Beta strand

92 – 97

6

Helix

102 – 104

3

Beta strand

106 – 113

8

Helix

115 – 117

3

Beta strand

120 – 127

8

Sequences

	Sequence		Length	Mass (Da)
	P01833-1 [UniParc]. Last modified June 26, 2007. Version 4. Checksum: 927461F4EB3B05C7	FASTA	764	83,284
	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

References

	« Hide 'large scale' referencesShow '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: 1682231] [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: 1355431] [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: 17974005] [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: 2920039] [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: 6526384] [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: 1859628] [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: 9237679] [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: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 AND ASN-469, MASS SPECTROMETRY. 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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469, MASS SPECTROMETRY. 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: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186; ASN-421; ASN-469 AND ASN-499, MASS SPECTROMETRY. 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: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND ASN-499, MASS SPECTROMETRY. Tissue: Milk.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421 AND ASN-469, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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: 15530357] [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 , 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.

IPI

IPI00004573.

PIR

QRHUGS. A46537.

RefSeq

NP_002635.2.

UniGene

Hs.497589

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

SMR

P01833. Positions 23-249.

ModBase

Search...

Protein-protein interaction databases

IntAct

P01833. 1 interaction.

STRING

P01833.

PTM databases

GlycoSuiteDB

P01833.

PhosphoSite

P01833.

Proteomic databases

PeptideAtlas

P01833.

PRIDE

P01833.

Genome annotation databases

Ensembl

ENST00000356495; ENSP00000348888; ENSG00000162896; Homo sapiens. [Genome view]

GeneID

5284.

KEGG

hsa:5284.

UCSC

uc001hez.1. human.

Organism-specific databases

CTD

5284.

GeneCards

GC01M205168.

H-InvDB

HIX0028583.

HGNC

HGNC:8968. PIGR.

HPA

CAB009454.
HPA006154.
HPA012012.

MIM

173880. gene.

PharmGKB

PA33300.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18559.

HOGENOM

HBG279174.

HOVERGEN

P01833.

InParanoid

P01833.

OMA

YWCGVKQ.

OrthoDB

EOG93N9XV.

PhylomeDB

P01833.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Gene expression databases

ArrayExpress

P01833.

Bgee

P01833.

CleanEx

HS_PIGR.

Genevestigator

P01833.

GermOnline

ENSG00000162896. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 4 hits.

Pfam

PF07686. V-set. 5 hits.
[Graphical view]

SMART

SM00409. IG. 5 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

20420.

SOURCE

Search...

Entry information

Entry name

PIGR_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.