A1AG1_MOUSE
ID A1AG1_MOUSE Reviewed; 207 AA.
AC Q60590;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alpha-1-acid glycoprotein 1;
DE Short=AGP 1;
DE AltName: Full=Orosomucoid-1;
DE Short=OMD 1;
DE Flags: Precursor;
GN Name=Orm1; Synonyms=Agp1, Orm-1;
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].
RX PubMed=2475311; DOI=10.1089/dna.1.1989.8.245;
RA Lee S.C., Chang C.J., Lee Y.M., Lei H.Y., Lai M.Y., Chen D.S.;
RT "Molecular cloning of cDNAs corresponding to two genes of alpha 1-acid
RT glycoprotein and characterization of two alleles of AGP-1 in the mouse.";
RL DNA 8:245-251(1989).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-34; ASN-76 AND ASN-94.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94 AND ASN-104.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; M27008; AAA37194.1; -; mRNA.
DR CCDS; CCDS18251.1; -.
DR PIR; A32476; A32476.
DR RefSeq; NP_032794.1; NM_008768.2.
DR AlphaFoldDB; Q60590; -.
DR SMR; Q60590; -.
DR BioGRID; 201978; 3.
DR STRING; 10090.ENSMUSP00000030044; -.
DR GlyConnect; 798; 4 N-Linked glycans (1 site).
DR GlyGen; Q60590; 5 sites, 7 N-linked glycans (1 site).
DR iPTMnet; Q60590; -.
DR PhosphoSitePlus; Q60590; -.
DR CPTAC; non-CPTAC-3308; -.
DR jPOST; Q60590; -.
DR MaxQB; Q60590; -.
DR PaxDb; Q60590; -.
DR PeptideAtlas; Q60590; -.
DR PRIDE; Q60590; -.
DR ProteomicsDB; 285692; -.
DR DNASU; 18405; -.
DR Ensembl; ENSMUST00000030044; ENSMUSP00000030044; ENSMUSG00000039196.
DR GeneID; 18405; -.
DR KEGG; mmu:18405; -.
DR UCSC; uc008tfx.1; mouse.
DR CTD; 5004; -.
DR MGI; MGI:97443; Orm1.
DR VEuPathDB; HostDB:ENSMUSG00000039196; -.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR GeneTree; ENSGT00390000012130; -.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; Q60590; -.
DR OMA; KTFMLAF; -.
DR OrthoDB; 1257041at2759; -.
DR PhylomeDB; Q60590; -.
DR TreeFam; TF343791; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18405; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Orm1; mouse.
DR PRO; PR:Q60590; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60590; protein.
DR Bgee; ENSMUSG00000039196; Expressed in left lobe of liver and 92 other tissues.
DR Genevisible; Q60590; MM.
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 1: Evidence at protein level;
KW Acute phase; Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..207
FT /note="Alpha-1-acid glycoprotein 1"
FT /id="PRO_0000017862"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02763"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 91..184
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23895 MW; 34CA38BE40BC1863 CRC64;
MALHTVLIIL SLLPMLEAQN PEHANFTIGE PITNETLSWL SDKWFFMGAA FRKLEYRQAI
QTMQSEFFYL TTNLINDTIE LRESQTIGDQ CVYNSTHLGF QRENGTFSKY EGGVETFAHL
IVLRKHGAFM LAFDLKDEKK RGLSLYAKRP DITPELREVF QKAVTHVGMD ESEIIFVDWK
KDRCGQQEKK QLELGKETKK DPEEGQA
