MILR1_MOUSE
ID MILR1_MOUSE Reviewed; 246 AA.
AC Q3TB92; B2RTB7; B7ZP18; D6RUW9; Q3TC23; Q3TDY5; Q3U5M7; Q3U9F5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Allergin-1;
DE AltName: Full=Allergy inhibitory receptor 1;
DE AltName: Full=Mast cell antigen 32;
DE Short=MCA-32;
DE Short=Mast cell Ag-32;
DE AltName: Full=Mast cell immunoglobulin-like receptor 1;
DE Flags: Precursor;
GN Name=Milr1; Synonyms=Gm885, Mca32;
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), FUNCTION, DISRUPTION PHENOTYPE,
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PTPN6; PTPN11 AND INPP5D,
RP TISSUE SPECIFICITY, GLYCOSYLATION, PHOSPHORYLATION AT TYR-216 AND TYR-241,
RP AND MUTAGENESIS OF TYR-216 AND TYR-241.
RX PubMed=20526344; DOI=10.1038/ni.1886;
RA Hitomi K., Tahara-Hanaoka S., Someya S., Fujiki A., Tada H., Sugiyama T.,
RA Shibayama S., Shibuya K., Shibuya A.;
RT "An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-
RT mediated immediate hypersensitivity reactions.";
RL Nat. Immunol. 11:601-607(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND TYR-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Immunoglobulin-like receptor which plays an inhibitory role
CC in degranulation of mast cells. Negatively regulates IgE-mediated mast
CC cell activation and suppresses the type I immediate hypersensitivity
CC reaction. {ECO:0000269|PubMed:20526344}.
CC -!- SUBUNIT: Monomer (Probable). Interacts (tyrosine-phosphorylated) with
CC PTPN6, PTPN11 and INPP5D. {ECO:0000269|PubMed:20526344, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20526344};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20526344}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TB92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TB92-2; Sequence=VSP_028742;
CC -!- TISSUE SPECIFICITY: Expressed in myeloid cells (dendritic cells,
CC macrophages and neutrophils but not in T-cells, B-cells or natural
CC killer cells) and mast cells (at protein level).
CC {ECO:0000269|PubMed:20526344}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20526344}.
CC -!- DISRUPTION PHENOTYPE: Enhanced IgE-mediated, mast cell-dependent
CC passive systemic anaphylaxis. No effect on differentiation of
CC hematopoietic cells, including mast cells.
CC {ECO:0000269|PubMed:20526344}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB542953; BAJ08254.1; -; mRNA.
DR EMBL; AK136488; BAE23003.1; -; mRNA.
DR EMBL; AK151814; BAE30712.1; -; mRNA.
DR EMBL; AK153506; BAE32051.1; ALT_INIT; mRNA.
DR EMBL; AK169925; BAE41463.1; -; mRNA.
DR EMBL; AK170947; BAE42134.1; -; mRNA.
DR EMBL; AK171381; BAE42422.1; -; mRNA.
DR EMBL; BC139224; AAI39225.1; -; mRNA.
DR EMBL; BC139225; AAI39226.1; -; mRNA.
DR EMBL; BC145580; AAI45581.1; -; mRNA.
DR CCDS; CCDS25560.1; -. [Q3TB92-1]
DR CCDS; CCDS70335.1; -. [Q3TB92-2]
DR RefSeq; NP_001028607.1; NM_001033435.3. [Q3TB92-1]
DR RefSeq; NP_001258301.1; NM_001271372.1.
DR RefSeq; NP_001258302.1; NM_001271373.1.
DR RefSeq; NP_001258303.1; NM_001271374.1. [Q3TB92-2]
DR RefSeq; NP_001258304.1; NM_001271375.1. [Q3TB92-2]
DR RefSeq; XP_006533711.1; XM_006533648.3. [Q3TB92-1]
DR RefSeq; XP_006533712.1; XM_006533649.3. [Q3TB92-2]
DR RefSeq; XP_011247406.1; XM_011249104.2. [Q3TB92-1]
DR AlphaFoldDB; Q3TB92; -.
DR SMR; Q3TB92; -.
DR DIP; DIP-62112N; -.
DR STRING; 10090.ENSMUSP00000083538; -.
DR GlyGen; Q3TB92; 1 site.
DR iPTMnet; Q3TB92; -.
DR PhosphoSitePlus; Q3TB92; -.
DR EPD; Q3TB92; -.
DR MaxQB; Q3TB92; -.
DR PaxDb; Q3TB92; -.
DR PeptideAtlas; Q3TB92; -.
DR PRIDE; Q3TB92; -.
DR ProteomicsDB; 290081; -. [Q3TB92-1]
DR ProteomicsDB; 290082; -. [Q3TB92-2]
DR Antibodypedia; 68852; 110 antibodies from 14 providers.
DR Ensembl; ENSMUST00000086353; ENSMUSP00000083538; ENSMUSG00000040528. [Q3TB92-1]
DR Ensembl; ENSMUST00000147326; ENSMUSP00000138742; ENSMUSG00000040528. [Q3TB92-1]
DR Ensembl; ENSMUST00000182908; ENSMUSP00000138678; ENSMUSG00000040528. [Q3TB92-2]
DR Ensembl; ENSMUST00000183111; ENSMUSP00000138513; ENSMUSG00000040528. [Q3TB92-2]
DR GeneID; 380732; -.
DR KEGG; mmu:380732; -.
DR UCSC; uc007lzj.2; mouse. [Q3TB92-1]
DR UCSC; uc007lzl.2; mouse. [Q3TB92-2]
DR CTD; 284021; -.
DR MGI; MGI:2685731; Milr1.
DR VEuPathDB; HostDB:ENSMUSG00000040528; -.
DR eggNOG; ENOG502S5BW; Eukaryota.
DR GeneTree; ENSGT01050000244988; -.
DR InParanoid; Q3TB92; -.
DR OMA; ENVCKDQ; -.
DR OrthoDB; 1405395at2759; -.
DR BioGRID-ORCS; 380732; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q3TB92; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3TB92; protein.
DR Bgee; ENSMUSG00000040528; Expressed in granulocyte and 77 other tissues.
DR ExpressionAtlas; Q3TB92; baseline and differential.
DR Genevisible; Q3TB92; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0043303; P:mast cell degranulation; IMP:UniProtKB.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR029626; Allergin-1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR11481:SF58; PTHR11481:SF58; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..246
FT /note="Allergin-1"
FT /id="PRO_0000307365"
FT TOPO_DOM 34..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..131
FT /note="Ig-like C2-type"
FT MOTIF 214..219
FT /note="ITIM motif"
FT MOTIF 239..244
FT /note="ITIM motif"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20526344,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20526344,
FT ECO:0007744|PubMed:19144319"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 140..178
FT /note="KDESCPSCRLSLLLPGLLLGILVIVLVLAYLIHLKYKKG -> R (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028742"
FT MUTAGEN 216
FT /note="Y->F: Abolishes interaction with PTPN6 and PTPN11.
FT Loss of function; when associated with F-241."
FT /evidence="ECO:0000269|PubMed:20526344"
FT MUTAGEN 241
FT /note="Y->F: Abolishes interaction with PTPN6 and PTPN11.
FT Loss of function; when associated with F-216."
FT /evidence="ECO:0000269|PubMed:20526344"
FT CONFLICT 13
FT /note="V -> F (in Ref. 2; BAE32051)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="D -> E (in Ref. 2; BAE30712)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..141
FT /note="KD -> N (in Ref. 2; BAE42422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 27366 MW; 38B4E4EE9E229B49 CRC64;
MGDGDSPMCL SAVSFKGIRC WLDKLLLWAL TISITLQNAA VDCTRVENNE LPSPNLNSSM
NVVRMGQNVS LSCSTKNTSV DITYSLFWGT KYLESKRRRG GAVDFHLRIS NANESGPYKC
KVNVSNLMKY SQDFNFTMAK DESCPSCRLS LLLPGLLLGI LVIVLVLAYL IHLKYKKGKK
TQREDQSKGS GDAPAQDELY VNACKTQTEQ PQEIHYATPV FKEMAPMEEE GGTDGKADYI
YSELTH
