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93  structures 303  species 0  interactions 5051  sequences 52  architectures

Family: UPAR_LY6 (PF00021)

Summary: u-PAR/Ly-6 domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "CD59 antigen". More...

CD59 antigen Edit Wikipedia article

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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "LU domain". More...

LU domain Edit Wikipedia article

u-PAR/Ly-6 domain
Identifiers
SymbolUPAR_LY6
PfamPF00021
InterProIPR001526
PROSITEPDOC00756
SCOP21erg / SCOPe / SUPFAM

CD59 antigen (also called 1F-5Ag, H19, HRF20, MACIF, MIRL, P-18 or protectin) inhibits formation of membrane attack complex (MAC), thus protecting cells from complement-mediated lysis. It has a signaling role, as a GPI anchored molecule, in T cell activation and appears to have some role in cell adhesion through CD2 (controversial). CD59 associates with C9, inhibiting incorporation into C5b-8 preventing terminal steps in polymerization of the (MAC) in plasma membranes. Genetic defects in GPI-anchor attachment that cause a reduction or loss of both CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal nocturnal hemoglobinuria (PNH).

A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved domain of about 100 amino-acid residues[1][2]. Among these proteins, U-PAR contains three tandem copies of the domain, while all the others are made up of a single domain.

As shown in the following schematic, this conserved domain contains 10 cysteine residues involved in five disulphide bonds - in U-PAR, the first copy of the domain lacks the fourth disulphide bond.

    +------+     +------------------------+                    +---+
    |      |     |                        |                    |   |
xCxxCxxxxxxCxxxxxCxxxxxCxxxxxxxxxxxxxxxxxxCxxxxCxxxxxxxxxxxxxxCCxxxCxxxxxxxx
 |                     |                       |              |
 +---------------------+                       +--------------+

'C': conserved cysteine involved in a disulphide bond.


CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/).

Subfamilies

Human proteins containing this domain

ARS; CD177; CD59; LY6D; LY6E; LY6H; LYNX1; LYPD2; LYPD3; LYPD4; LYPD5; LYPD6; PLAUR; PSCA; SLURP2; SLURP1; SPACA4; TEX101;

References

  1. ^ Patthy L, Blasi F, Behrendt N, Ploug M, Houen G, Dano K (1991). "The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator". J. Biol. Chem. 266 (12): 7842–7847. PMID 1850423.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Ploug M, Dano K, Kjalke M, Ronne E, Weidle U, Hoyer-Hansen G (1993). "Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored membrane proteins". J. Biol. Chem. 268 (23): 17539–17546. PMID 8394346.{{cite journal}}: CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR001526

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

u-PAR/Ly-6 domain Provide feedback

This extracellular disulphide bond rich domain is related to PF00087.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR016054

A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved domain of about 100 amino-acid residues [ PUBMED:1850423 , PUBMED:8394346 ]. Among these proteins, U-PAR contains three tandem copies of the domain, while all the others are made up of a single domain.

As shown in the following schematic, this conserved domain contains 10 cysteine residues involved in five disulphide bonds - in U-PAR, the first copy of the domain lacks the fourth disulphide bond.

     +------+     +------------------------+                    +---+
     |      |     |                        |                    |   |
 xCxxCxxxxxxCxxxxxCxxxxxCxxxxxxxxxxxxxxxxxxCxxxxCxxxxxxxxxxxxxxCCxxxCxxxxxxxx
  |                     |                       |              |
  +---------------------+                       +--------------+

'C': conserved cysteine involved in a disulphide bond.

This entry represents a three-fold repeated domain in urokinase-type plasminogen activator receptor (uPAR) that occurs singly in other GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2).

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan uPAR_Ly6_toxin (CL0117), which has the following description:

This superfamily contains snake toxins as well as extracellular cysteine rich domains.

The clan contains the following 10 members:

Activin_recp BAMBI DUF5746 ecTbetaR2 Ly-6_related PLA2_inh QVR Toxin_TOLIP UPAR_LY6 UPAR_LY6_2

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(27)
Full
(5051)
Representative proteomes UniProt
(8176)
RP15
(391)
RP35
(1307)
RP55
(3505)
RP75
(5064)
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HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(27)
Full
(5051)
Representative proteomes UniProt
(8176)
RP15
(391)
RP35
(1307)
RP55
(3505)
RP75
(5064)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(27)
Full
(5051)
Representative proteomes UniProt
(8176)
RP15
(391)
RP35
(1307)
RP55
(3505)
RP75
(5064)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL , Bateman A
Number in seed: 27
Number in full: 5051
Average length of the domain: 74.6 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 49.56 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 17.7 10.0
Trusted cut-off 17.7 10.0
Noise cut-off 17.6 9.9
Model length: 77
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Viroids Viroids Unclassified sequence Unclassified sequence

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the UPAR_LY6 domain has been found. There are 93 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A087WQT1 View 3D Structure Click here
A0A0G2L893 View 3D Structure Click here
A0A0R4IAR1 View 3D Structure Click here
A0A0R4IDA9 View 3D Structure Click here
A0A0R4IE63 View 3D Structure Click here
A0A0R4IEB6 View 3D Structure Click here
A0A0R4IGF8 View 3D Structure Click here
A0A0R4IQH2 View 3D Structure Click here
A0A0R4IR06 View 3D Structure Click here
A0A0R4IR51 View 3D Structure Click here
A0A0R4IW80 View 3D Structure Click here
A0A0R4IXU5 View 3D Structure Click here
A0A286Y9H8 View 3D Structure Click here
A0A2R8QI72 View 3D Structure Click here
A0A2R8QR51 View 3D Structure Click here
A0A2R8RYF0 View 3D Structure Click here
A0JNB3 View 3D Structure Click here
A2VE33 View 3D Structure Click here
A6NC86 View 3D Structure Click here
D3Z9W4 View 3D Structure Click here
D3ZCH9 View 3D Structure Click here
D3ZFP5 View 3D Structure Click here
D3ZGW9 View 3D Structure Click here
D3ZHB4 View 3D Structure Click here
D3ZNV7 View 3D Structure Click here
D3ZP75 View 3D Structure Click here
D3ZT54 View 3D Structure Click here
D3ZUR5 View 3D Structure Click here
D3ZZL5 View 3D Structure Click here
D4A499 View 3D Structure Click here
D4A6I7 View 3D Structure Click here
D4A7L8 View 3D Structure Click here
D4A9M5 View 3D Structure Click here
E7F0J8 View 3D Structure Click here
E7F2M5 View 3D Structure Click here
F1LNW6 View 3D Structure Click here
F7EWC5 View 3D Structure Click here
H3BJG9 View 3D Structure Click here
H3BQJ8 View 3D Structure Click here
M0R4W1 View 3D Structure Click here