A1AG3_MOUSE
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 25-MAY-2022, entry version 117.
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 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}.
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DR EMBL; S38219; AAB22378.2; -; Genomic_DNA.
DR CCDS; CCDS18252.1; -.
DR AlphaFoldDB; Q63805; -.
DR SMR; Q63805; -.
DR STRING; 10090.ENSMUSP00000006687; -.
DR GlyGen; Q63805; 3 sites.
DR iPTMnet; Q63805; -.
DR PhosphoSitePlus; Q63805; -.
DR MaxQB; Q63805; -.
DR PaxDb; Q63805; -.
DR PeptideAtlas; Q63805; -.
DR PRIDE; Q63805; -.
DR ProteomicsDB; 296424; -.
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 Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR001500; A1A_glycop.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036899; AGP; 1.
DR PRINTS; PR00708; A1AGLPROTEIN.
DR SUPFAM; SSF50814; SSF50814; 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
