ID A1AG3_MOUSE Reviewed; 206 AA. AC Q63805; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUL-2024, entry version 123. DE RecName: Full=Alpha-1-acid glycoprotein 3; DE Short=AGP 3; DE AltName: Full=Orosomucoid-3; DE Short=OMD 3; DE Flags: Precursor; GN Name=Orm3; Synonyms=Agp-3, Orm-3; 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=C57BL/6J; TISSUE=Lymphocyte; RX PubMed=1605854; DOI=10.1089/dna.1992.11.315; RA Chang C.J., Lai M.Y., Chen D.S., Lee S.C.; RT "Structure and expression of mouse alpha 1-acid glycoprotein gene-3 (AGP- RT 3)."; RL DNA Cell Biol. 11:315-320(1992). CC -!- FUNCTION: Functions as a transport protein in the blood stream. Binds CC various ligands in the interior of its beta-barrel domain (By CC similarity). Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its CC interior. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC {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; S38219; AAB22378.2; -; Genomic_DNA. DR CCDS; CCDS18252.1; -. DR AlphaFoldDB; Q63805; -. DR SMR; Q63805; -. DR STRING; 10090.ENSMUSP00000006687; -. DR GlyCosmos; Q63805; 3 sites, No reported glycans. DR GlyGen; Q63805; 3 sites. DR iPTMnet; Q63805; -. DR PhosphoSitePlus; Q63805; -. DR PaxDb; 10090-ENSMUSP00000006687; -. DR PeptideAtlas; Q63805; -. DR ProteomicsDB; 296424; -. DR AGR; MGI:97445; -. DR MGI; MGI:97445; Orm3. DR eggNOG; ENOG502S0Q2; Eukaryota. DR InParanoid; Q63805; -. DR Reactome; R-MMU-114608; Platelet degranulation. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR PRO; PR:Q63805; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q63805; Protein. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0036094; F:small molecule binding; ISO:MGI. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro. DR CDD; cd19451; lipocalin_AGP-like; 1. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR PANTHER; PTHR11967; ALPHA-1-ACID GLYCOPROTEIN; 1. DR PANTHER; PTHR11967:SF2; ALPHA-1-ACID GLYCOPROTEIN 1; 1. DR Pfam; PF00061; Lipocalin; 1. DR PIRSF; PIRSF036899; AGP; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR SUPFAM; SSF50814; Lipocalins; 1. PE 3: Inferred from homology; KW Acute phase; Disulfide bond; Glycoprotein; Reference proteome; Secreted; KW Signal; Transport. FT SIGNAL 1..18 FT /evidence="ECO:0000250" FT CHAIN 19..206 FT /note="Alpha-1-acid glycoprotein 3" FT /id="PRO_0000017864" FT REGION 187..206 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 75 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 90..183 FT /evidence="ECO:0000250" SQ SEQUENCE 206 AA; 24069 MW; 5E98D1958BE1F0AB CRC64; MELHTVLIML SLLPLLEAQN PEHAINIGDP ITNETLSWLS GKWFLIAVAD SDPDYRQEIQ KVQTIFFYLT LNKINDTMEL REYHTKDDHC VYNSNLLGFQ RENGTLFKYE GEVENPSHLR VLEKHGAIML FFDLKDEKKR GLSLSARRPD IPPELREVFQ KAVTHVGMDE SEIIFVDWKK DRCSEQEKKH LELEKETKKD PEESQA //