ID   MILR1_RAT               Reviewed;         248 AA.
AC   Q62875;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 95.
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=Mca32;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7499870;
RA   Pirozzi G., Terry R.W., Epstein D., Labow M.A.;
RT   "Identification and characterization of a novel surface antigen gene
RT   induced in mast cells activated through the high affinity IgE receptor.";
RL   J. Immunol. 155:5811-5818(1995).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts (tyrosine-phosphorylated) with PTPN6,
CC       PTPN11 and INPP5D. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7499870};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:7499870}.
CC   -!- TISSUE SPECIFICITY: Mast cell-specific. Expressed in primary and
CC       transformed mast cells. {ECO:0000269|PubMed:7499870}.
CC   -!- INDUCTION: Up-regulated in response to mast cell activation.
CC       {ECO:0000269|PubMed:7499870}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52339.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U39546; AAC52339.1; ALT_INIT; mRNA.
DR   RefSeq; NP_067596.1; NM_021585.1.
DR   AlphaFoldDB; Q62875; -.
DR   STRING; 10116.ENSRNOP00000048321; -.
DR   GlyGen; Q62875; 2 sites.
DR   iPTMnet; Q62875; -.
DR   PhosphoSitePlus; Q62875; -.
DR   PaxDb; Q62875; -.
DR   PRIDE; Q62875; -.
DR   GeneID; 59105; -.
DR   KEGG; rno:59105; -.
DR   UCSC; RGD:620488; rat.
DR   CTD; 284021; -.
DR   RGD; 620488; Milr1.
DR   InParanoid; Q62875; -.
DR   OrthoDB; 1405395at2759; -.
DR   PhylomeDB; Q62875; -.
DR   PRO; PR:Q62875; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0033004; P:negative regulation of mast cell activation; ISS: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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..248
FT                   /note="Allergin-1"
FT                   /id="PRO_0000307366"
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..248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..137
FT                   /note="Ig-like C2-type"
FT   MOTIF           216..221
FT                   /note="ITIM motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           241..246
FT                   /note="ITIM motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         218
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TB92"
FT   MOD_RES         243
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TB92"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   248 AA;  27459 MW;  47F1BC8906F51116 CRC64;
     MGDDDTPVCL SVASCKGVSC WLDKLLLWAL TLSITLRNTA VDCRRVDRNG LLSPNLNSSM
     SVVRMGQNVS LSCSSKNTSI DITYSLFLGK RYLESKRRRG GAVDFHLRIS NANESGPYKC
     KVNDSNSSKY SQNFNFTIIQ DESCSSCLLS LLLPGVLLGL ILPGLAFLIY LKYKKGCTGK
     TLKENESKGS GDAPTQGELY ANICETQKGS EQLQEIHYTT PVFKEVAPTE QEGLEDRKDD
     YIYSELTY