PILB2_MOUSE
ID PILB2_MOUSE Reviewed; 225 AA.
AC Q2YFS1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Paired immunoglobulin-like type 2 receptor beta-2;
DE AltName: Full=Activating receptor PILR-beta-2;
DE Flags: Precursor;
GN Name=Pilrb2;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
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).
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. PILRB2 is probably a cellular signaling activating
CC receptor that associates with ITAM-bearing adapter molecules on the
CC cell surface.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY823670; AAX39496.1; -; Genomic_DNA.
DR EMBL; AK036467; BAC29442.1; -; mRNA.
DR CCDS; CCDS51676.1; -.
DR RefSeq; NP_001020103.1; NM_001024932.2.
DR AlphaFoldDB; Q2YFS1; -.
DR SMR; Q2YFS1; -.
DR STRING; 10090.ENSMUSP00000131233; -.
DR GlyGen; Q2YFS1; 3 sites.
DR MaxQB; Q2YFS1; -.
DR PaxDb; Q2YFS1; -.
DR PRIDE; Q2YFS1; -.
DR ProteomicsDB; 289896; -.
DR Ensembl; ENSMUST00000164886; ENSMUSP00000131233; ENSMUSG00000066682.
DR GeneID; 545812; -.
DR UCSC; uc009aee.1; mouse.
DR CTD; 545812; -.
DR MGI; MGI:2450535; Pilrb2.
DR VEuPathDB; HostDB:ENSMUSG00000066682; -.
DR eggNOG; ENOG502SUHR; Eukaryota.
DR GeneTree; ENSGT00390000008831; -.
DR InParanoid; Q2YFS1; -.
DR OMA; VIISWRW; -.
DR OrthoDB; 1325787at2759; -.
DR PhylomeDB; Q2YFS1; -.
DR TreeFam; TF338478; -.
DR BioGRID-ORCS; 545812; 1 hit in 42 CRISPR screens.
DR PRO; PR:Q2YFS1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q2YFS1; protein.
DR Bgee; ENSMUSG00000066682; Expressed in granulocyte and 37 other tissues.
DR ExpressionAtlas; Q2YFS1; baseline and differential.
DR Genevisible; Q2YFS1; 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 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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..225
FT /note="Paired immunoglobulin-like type 2 receptor beta-2"
FT /id="PRO_0000226825"
FT TOPO_DOM 32..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 225 AA; 25513 MW; 512E40AD9E7E803B CRC64;
MALLISLPGE TPAMAQILLL LSSACLHAGN SARSNGGNDF GVNQPERCSG VQGGSIDIPF
SFYFPWKLAK DPQMSIAWRW KDFFGHFIYN SSMPFIHEHF KGRLILNWTQ GQTSGVLRIL
NFKESDQTWY FCRVFLQTTE GIKFWQSLPG TQLTLTQALN TTMRSPFIVT SEFTTAGLEH
TRDKRNPSLM NLGAMVTMLL AKVVVIILVY GWMIFLRWKQ RPDPA
