PILRA_MOUSE
ID PILRA_MOUSE Reviewed; 302 AA.
AC Q2YFS3; Q8BYA6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Paired immunoglobulin-like type 2 receptor alpha;
DE AltName: Full=Cell surface receptor FDF03;
DE AltName: Full=Inhibitory receptor PILR-alpha;
DE Flags: Precursor;
GN Name=Pilra;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10903717; DOI=10.4049/jimmunol.165.3.1197;
RA Fournier N., Chalus L., Durand I., Garcia E., Pin J.J., Churakova T.,
RA Patel S., Zlot C., Gorman D., Zurawski S., Abrams J., Bates E.E.,
RA Garrone P.;
RT "FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is
RT expressed by human dendritic and myeloid cells.";
RL J. Immunol. 165:1197-1209(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Wilson M.D., McKinnel L., Danby A., Schnupf P., Hunt P., Martindale D.,
RA Koop B.F.;
RT "Comparative genomic analysis of the paired immunoglobin-like receptor
RT locus at 7q22: duplications, conversions, inversions and the birth of new
RT genes.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP INTERACTION WITH CD99.
RX PubMed=14970179; DOI=10.1084/jem.20031885;
RA Shiratori I., Ogasawara K., Saito T., Lanier L.L., Arase H.;
RT "Activation of natural killer cells and dendritic cells upon recognition of
RT a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.";
RL J. Exp. Med. 199:525-533(2004).
RN [5]
RP FUNCTION.
RX PubMed=21241660; DOI=10.1016/j.bbrc.2011.01.047;
RA Kogure A., Shiratori I., Wang J., Lanier L.L., Arase H.;
RT "PANP is a novel O-glycosylated PILRalpha ligand expressed in neural
RT tissues.";
RL Biochem. Biophys. Res. Commun. 405:428-433(2011).
CC -!- FUNCTION: Paired receptors consist of highly related activating and
CC inhibitory receptors and are widely involved in the regulation of the
CC immune system. Receptor for CD99 and PIANP.
CC {ECO:0000269|PubMed:21241660}.
CC -!- SUBUNIT: Interacts with CD99. {ECO:0000269|PubMed:14970179}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2YFS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2YFS3-2; Sequence=VSP_017505;
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC PTPN6 seems to bind predominantly to the first ITIM motif (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
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DR EMBL; AJ400844; CAC01617.1; -; mRNA.
DR EMBL; AY823670; AAX39494.1; -; Genomic_DNA.
DR EMBL; AK041413; BAC30935.1; -; mRNA.
DR CCDS; CCDS19780.1; -. [Q2YFS3-1]
DR RefSeq; NP_705730.1; NM_153510.3. [Q2YFS3-1]
DR AlphaFoldDB; Q2YFS3; -.
DR SMR; Q2YFS3; -.
DR IntAct; Q2YFS3; 1.
DR STRING; 10090.ENSMUSP00000050313; -.
DR GlyGen; Q2YFS3; 2 sites.
DR PhosphoSitePlus; Q2YFS3; -.
DR MaxQB; Q2YFS3; -.
DR PaxDb; Q2YFS3; -.
DR PRIDE; Q2YFS3; -.
DR ProteomicsDB; 287730; -. [Q2YFS3-1]
DR ProteomicsDB; 287731; -. [Q2YFS3-2]
DR ABCD; Q2YFS3; 19 sequenced antibodies.
DR DNASU; 231805; -.
DR Ensembl; ENSMUST00000058897; ENSMUSP00000050313; ENSMUSG00000046245. [Q2YFS3-1]
DR Ensembl; ENSMUST00000110980; ENSMUSP00000106608; ENSMUSG00000046245. [Q2YFS3-2]
DR GeneID; 231805; -.
DR KEGG; mmu:231805; -.
DR UCSC; uc009aea.2; mouse. [Q2YFS3-1]
DR UCSC; uc009aeb.2; mouse. [Q2YFS3-2]
DR CTD; 29992; -.
DR MGI; MGI:2450529; Pilra.
DR VEuPathDB; HostDB:ENSMUSG00000046245; -.
DR eggNOG; ENOG502SUHR; Eukaryota.
DR GeneTree; ENSGT00390000008831; -.
DR HOGENOM; CLU_070832_0_0_1; -.
DR InParanoid; Q2YFS3; -.
DR OMA; YENIGND; -.
DR OrthoDB; 1325787at2759; -.
DR PhylomeDB; Q2YFS3; -.
DR TreeFam; TF338478; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 231805; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q2YFS3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q2YFS3; protein.
DR Bgee; ENSMUSG00000046245; Expressed in granulocyte and 101 other tissues.
DR ExpressionAtlas; Q2YFS3; baseline and differential.
DR Genevisible; Q2YFS3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..302
FT /note="Paired immunoglobulin-like type 2 receptor alpha"
FT /id="PRO_0000226823"
FT TOPO_DOM 32..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 228..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..270
FT /note="ITIM motif 1"
FT MOTIF 294..299
FT /note="ITIM motif 2"
FT COMPBIAS 228..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..28
FT /note="MALLISLPGGTPAMAQILLLLSSACLHA -> MFCVVLSMFPVTVPCSGFRV
FT SPSFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017505"
SQ SEQUENCE 302 AA; 33064 MW; F5F38725B91A3FEC CRC64;
MALLISLPGG TPAMAQILLL LSSACLHAGN SERSNRKNGF GVNQPESCSG VQGGSIDIPF
SFYFPWKLAK DPQMSIAWRW KDFHGEFIYN SSLPFIHEHF KGRLILNWTQ GQTSGVLRIL
NLKESDQTRY FGRVFLQTTE GIQFWQSIPG TQLNVTNATC TPTTLPSTTA ATSAHTQNDI
TEVKSANIGG LDLQTTVGLA TAAAVFLVGV LGLIVFLWWK RRRQGQKTKA EIPAREPLET
SEKHESVGHE GQCMDPKENP KDNNIVYASI SLSSPTSPGT APNLPVHGNP QEETVYSIVK
AK
