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Protein

Paired immunoglobulin-like type 2 receptor alpha

Gene

PILRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Paired immunoglobulin-like type 2 receptor alpha
Alternative name(s):
Cell surface receptor FDF03
Inhibitory receptor PILR-alpha
Gene namesi
Name:PILRA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:20396. PILRA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 197178ExtracellularSequence analysisAdd
BLAST
Transmembranei198 – 21821HelicalSequence analysisAdd
BLAST
Topological domaini219 – 30385CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi269 – 2691Y → F: Greatly diminishes interaction with PTPN6. 1 Publication

Organism-specific databases

PharmGKBiPA134873007.

Polymorphism and mutation databases

BioMutaiPILRA.
DMDMi296439272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 303284Paired immunoglobulin-like type 2 receptor alphaPRO_0000226821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...)1 Publication

Post-translational modificationi

According to PubMed:10660620, N- and O-glycosylated. According to PubMed:10903717, only N-glycosylated.3 Publications
Phosphorylated on tyrosine residues.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9UKJ1.
PRIDEiQ9UKJ1.

PTM databases

iPTMnetiQ9UKJ1.
PhosphoSiteiQ9UKJ1.

Expressioni

Tissue specificityi

Predominantly detected in hemopoietic tissues and is expressed by monocytes, macrophages, and granulocytes, but not by lymphocytes. Also strongly expressed by dendritic cells (DC); preferentially by CD14+/CD1a- DC derived from CD34+ progenitors. Also expressed by CD11c+ blood and tonsil DC, but not by CD11c- DC precursors.1 Publication

Gene expression databases

BgeeiQ9UKJ1.
CleanExiHS_PILRA.
ExpressionAtlasiQ9UKJ1. baseline and differential.
GenevisibleiQ9UKJ1. HS.

Organism-specific databases

HPAiHPA051219.

Interactioni

Subunit structurei

Monomer. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon tyrosine phosphorylation. Interacts with herpes simplex virus 1 glycoprotein B; functions as an entry coreceptor for this virus.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
gBP064363EBI-965833,EBI-1771271From a different organism.
PTPN6P293505EBI-965833,EBI-78260

GO - Molecular functioni

Protein-protein interaction databases

BioGridi119017. 14 interactions.
IntActiQ9UKJ1. 5 interactions.
MINTiMINT-8020036.
STRINGi9606.ENSP00000198536.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Beta strandi39 – 446Combined sources
Beta strandi49 – 568Combined sources
Beta strandi68 – 7710Combined sources
Beta strandi79 – 835Combined sources
Turni84 – 874Combined sources
Helixi91 – 933Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi106 – 1127Combined sources
Helixi117 – 1193Combined sources
Beta strandi121 – 13111Combined sources
Turni132 – 1343Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi145 – 1506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WUZX-ray1.30A32-150[»]
3WV0X-ray2.30A/B32-150[»]
4NFBX-ray1.60A32-150[»]
ProteinModelPortaliQ9UKJ1.
SMRiQ9UKJ1. Positions 32-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 150119Ig-like V-typeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi267 – 2726ITIM motif 1
Motifi296 – 3016ITIM motif 2

Domaini

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IW80. Eukaryota.
ENOG41114MH. LUCA.
GeneTreeiENSGT00390000008831.
HOGENOMiHOG000035130.
HOVERGENiHBG082142.
InParanoidiQ9UKJ1.
KOiK15411.
OMAiAREPFQN.
PhylomeDBiQ9UKJ1.
TreeFamiTF338478.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UKJ1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRPLLLPLL PLLLPPAFLQ PSGSTGSGPS YLYGVTQPKH LSASMGGSVE
60 70 80 90 100
IPFSFYYPWE LATAPDVRIS WRRGHFHRQS FYSTRPPSIH KDYVNRLFLN
110 120 130 140 150
WTEGQKSGFL RISNLQKQDQ SVYFCRVELD TRSSGRQQWQ SIEGTKLSIT
160 170 180 190 200
QAVTTTTQRP SSMTTTWRLS STTTTTGLRV TQGKRRSDSW HISLETAVGV
210 220 230 240 250
AVAVTVLGIM ILGLICLLRW RRRKGQQRTK ATTPAREPFQ NTEEPYENIR
260 270 280 290 300
NEGQNTDPKL NPKDDGIVYA SLALSSSTSP RAPPSHRPLK SPQNETLYSV

LKA
Length:303
Mass (Da):34,005
Last modified:May 18, 2010 - v3
Checksum:i77BD068C63274A40
GO
Isoform 2 (identifier: Q9UKJ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-303: DDGIVYASLA...NETLYSVLKA → LHLTQSTSQP...GLTNGQPSQD

Show »
Length:299
Mass (Da):33,646
Checksum:iB93981138065A130
GO
Isoform 3 (identifier: Q9UKJ1-3) [UniParc]FASTAAdd to basket

Also known as: FDF03-deltaTM

The sequence of this isoform differs from the canonical sequence as follows:
     152-224: Missing.

Show »
Length:230
Mass (Da):25,936
Checksum:i0A24E0FDC626C715
GO
Isoform 4 (identifier: Q9UKJ1-4) [UniParc]FASTAAdd to basket

Also known as: FDF03-M14

The sequence of this isoform differs from the canonical sequence as follows:
     152-303: AVTTTTQRPS...NETLYSVLKA → GNPSKTQRSHMRISGMKDKIQIPS

Show »
Length:175
Mass (Da):19,898
Checksum:i0F604AF3464B59EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921D → E in CAC01615 (PubMed:10903717).Curated
Sequence conflicti281 – 2811R → K in AAD52964 (PubMed:10660620).Curated
Isoform 4 (identifier: Q9UKJ1-4)
Sequence conflicti168 – 1681K → R in CAC01615 (PubMed:10903717).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781R → G.3 Publications
Corresponds to variant rs1859788 [ dbSNP | Ensembl ].
VAR_060361
Natural varianti279 – 2791S → L.
Corresponds to variant rs34266222 [ dbSNP | Ensembl ].
VAR_056062

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 303152AVTTT…SVLKA → GNPSKTQRSHMRISGMKDKI QIPS in isoform 4. 1 PublicationVSP_017500Add
BLAST
Alternative sequencei152 – 22473Missing in isoform 3. 1 PublicationVSP_017501Add
BLAST
Alternative sequencei264 – 30340DDGIV…SVLKA → LHLTQSTSQPPSPQEPPERD PVLCLKGLTNGQPSQD in isoform 2. 1 PublicationVSP_017502Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161080 mRNA. Translation: AAD52964.1.
AJ400841 mRNA. Translation: CAC01613.1.
AJ400842 mRNA. Translation: CAC01614.1.
AJ400843 mRNA. Translation: CAC01615.1.
AC005071 Genomic DNA. No translation available.
BC017812 mRNA. Translation: AAH17812.1.
CCDSiCCDS47660.1. [Q9UKJ1-4]
CCDS5691.1. [Q9UKJ1-1]
CCDS5692.1. [Q9UKJ1-3]
RefSeqiNP_038467.2. NM_013439.2. [Q9UKJ1-1]
NP_840056.1. NM_178272.1. [Q9UKJ1-3]
NP_840057.1. NM_178273.1. [Q9UKJ1-4]
UniGeneiHs.444407.

Genome annotation databases

EnsembliENST00000198536; ENSP00000198536; ENSG00000085514. [Q9UKJ1-1]
ENST00000350573; ENSP00000340109; ENSG00000085514. [Q9UKJ1-3]
ENST00000394000; ENSP00000377569; ENSG00000085514. [Q9UKJ1-4]
GeneIDi29992.
KEGGihsa:29992.
UCSCiuc003uuo.1. human. [Q9UKJ1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161080 mRNA. Translation: AAD52964.1.
AJ400841 mRNA. Translation: CAC01613.1.
AJ400842 mRNA. Translation: CAC01614.1.
AJ400843 mRNA. Translation: CAC01615.1.
AC005071 Genomic DNA. No translation available.
BC017812 mRNA. Translation: AAH17812.1.
CCDSiCCDS47660.1. [Q9UKJ1-4]
CCDS5691.1. [Q9UKJ1-1]
CCDS5692.1. [Q9UKJ1-3]
RefSeqiNP_038467.2. NM_013439.2. [Q9UKJ1-1]
NP_840056.1. NM_178272.1. [Q9UKJ1-3]
NP_840057.1. NM_178273.1. [Q9UKJ1-4]
UniGeneiHs.444407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WUZX-ray1.30A32-150[»]
3WV0X-ray2.30A/B32-150[»]
4NFBX-ray1.60A32-150[»]
ProteinModelPortaliQ9UKJ1.
SMRiQ9UKJ1. Positions 32-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119017. 14 interactions.
IntActiQ9UKJ1. 5 interactions.
MINTiMINT-8020036.
STRINGi9606.ENSP00000198536.

PTM databases

iPTMnetiQ9UKJ1.
PhosphoSiteiQ9UKJ1.

Polymorphism and mutation databases

BioMutaiPILRA.
DMDMi296439272.

Proteomic databases

PaxDbiQ9UKJ1.
PRIDEiQ9UKJ1.

Protocols and materials databases

DNASUi29992.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000198536; ENSP00000198536; ENSG00000085514. [Q9UKJ1-1]
ENST00000350573; ENSP00000340109; ENSG00000085514. [Q9UKJ1-3]
ENST00000394000; ENSP00000377569; ENSG00000085514. [Q9UKJ1-4]
GeneIDi29992.
KEGGihsa:29992.
UCSCiuc003uuo.1. human. [Q9UKJ1-1]

Organism-specific databases

CTDi29992.
GeneCardsiPILRA.
HGNCiHGNC:20396. PILRA.
HPAiHPA051219.
MIMi605341. gene.
neXtProtiNX_Q9UKJ1.
PharmGKBiPA134873007.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IW80. Eukaryota.
ENOG41114MH. LUCA.
GeneTreeiENSGT00390000008831.
HOGENOMiHOG000035130.
HOVERGENiHBG082142.
InParanoidiQ9UKJ1.
KOiK15411.
OMAiAREPFQN.
PhylomeDBiQ9UKJ1.
TreeFamiTF338478.

Miscellaneous databases

ChiTaRSiPILRA. human.
GenomeRNAii29992.
PROiQ9UKJ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKJ1.
CleanExiHS_PILRA.
ExpressionAtlasiQ9UKJ1. baseline and differential.
GenevisibleiQ9UKJ1. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta."
    Mousseau D.D., Banville D., L'Abbe D., Bouchard P., Shen S.H.
    J. Biol. Chem. 275:4467-4474(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTPN6, GLYCOSYLATION, PHOSPHORYLATION, MUTAGENESIS OF TYR-269, VARIANT GLY-78.
  2. "FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells."
    Fournier N., Chalus L., Durand I., Garcia E., Pin J.J., Churakova T., Patel S., Zlot C., Gorman D., Zurawski S., Abrams J., Bates E.E., Garrone P.
    J. Immunol. 165:1197-1209(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PTPN6 AND PTPN11, GLYCOSYLATION, PHOSPHORYLATION, VARIANT GLY-78.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLY-78.
    Tissue: Lung.
  5. "PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B."
    Satoh T., Arii J., Suenaga T., Wang J., Kogure A., Uehori J., Arase N., Shiratori I., Tanaka S., Kawaguchi Y., Spear P.G., Lanier L.L., Arase H.
    Cell 132:935-944(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPES SIMPLEX VIRUS 1 GLYCOPROTEIN B, FUNCTION AS A CORECEPTOR FOR THE VIRUS.
  6. "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-100.
    Tissue: Liver.
  7. "PANP is a novel O-glycosylated PILRalpha ligand expressed in neural tissues."
    Kogure A., Shiratori I., Wang J., Lanier L.L., Arase H.
    Biochem. Biophys. Res. Commun. 405:428-433(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPILRA_HUMAN
AccessioniPrimary (citable) accession number: Q9UKJ1
Secondary accession number(s): Q8NHI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 127 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.