A1AG2_MOUSE
ID A1AG2_MOUSE Reviewed; 207 AA.
AC P07361;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-1-acid glycoprotein 2;
DE Short=AGP 2;
DE AltName: Full=Orosomucoid-2;
DE Short=OMD 2;
DE Flags: Precursor;
GN Name=Orm2; Synonyms=Agp-2, Orm-2;
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=BALB/cJ;
RX PubMed=3676251; DOI=10.1021/bi00391a006;
RA Cooper R., Eckley D.M., Papaconstantinou J.;
RT "Nucleotide sequence of the mouse alpha 1-acid glycoprotein gene 1.";
RL Biochemistry 26:5244-5250(1987).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 70-207.
RX PubMed=3003086; DOI=10.1016/s0021-9258(17)36019-2;
RA Cooper R., Papaconstantinou J.;
RT "Evidence for the existence of multiple alpha 1-acid glycoprotein genes in
RT the mouse.";
RL J. Biol. Chem. 261:1849-1853(1986).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-76.
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).
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 -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, interleukin-1
CC and interleukin-6, It increases 5- to 50-fold upon inflammation.
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; M17376; AAA37193.1; -; Genomic_DNA.
DR EMBL; M27009; AAA37196.1; -; mRNA.
DR EMBL; BC057985; AAH57985.1; -; mRNA.
DR EMBL; M12566; AAA91744.1; -; mRNA.
DR CCDS; CCDS18253.1; -.
DR PIR; A29294; OMMS1.
DR RefSeq; NP_035146.1; NM_011016.2.
DR AlphaFoldDB; P07361; -.
DR SMR; P07361; -.
DR STRING; 10090.ENSMUSP00000074810; -.
DR GlyGen; P07361; 5 sites.
DR iPTMnet; P07361; -.
DR PhosphoSitePlus; P07361; -.
DR CPTAC; non-CPTAC-3307; -.
DR CPTAC; non-CPTAC-3368; -.
DR MaxQB; P07361; -.
DR PaxDb; P07361; -.
DR PeptideAtlas; P07361; -.
DR PRIDE; P07361; -.
DR ProteomicsDB; 285693; -.
DR DNASU; 18406; -.
DR Ensembl; ENSMUST00000075341; ENSMUSP00000074810; ENSMUSG00000061540.
DR GeneID; 18406; -.
DR KEGG; mmu:18406; -.
DR UCSC; uc008tga.1; mouse.
DR CTD; 5005; -.
DR MGI; MGI:97444; Orm2.
DR VEuPathDB; HostDB:ENSMUSG00000061540; -.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR GeneTree; ENSGT00390000012130; -.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; P07361; -.
DR OMA; PEHANII; -.
DR OrthoDB; 1257041at2759; -.
DR PhylomeDB; P07361; -.
DR TreeFam; TF343791; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18406; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Orm2; mouse.
DR PRO; PR:P07361; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P07361; protein.
DR Bgee; ENSMUSG00000061540; Expressed in left lobe of liver and 39 other tissues.
DR Genevisible; P07361; 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 CHAIN 19..207
FT /note="Alpha-1-acid glycoprotein 2"
FT /id="PRO_0000017863"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P19652"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..184
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23843 MW; 0FBCBEA99C558A6F CRC64;
MALHMILVMV SLLPLLEAQN PEHVNITIGD PITNETLSWL SDKWFFIGAA VLNPDYRQEI
QKTQMVFFNL TPNLINDTME LREYHTIDDH CVYNSTHLGI QRENGTLSKY VGGVKIFADL
IVLKMHGAFM LAFDLKDEKK RGLSLNAKRP DITPELREVF QKAVTHVGMD ESEIIFVDWK
KDRCSQQEKQ QLELEKETKK DPEEGQA
