A1AG_RAT
ID A1AG_RAT Reviewed; 205 AA.
AC P02764;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-1-acid glycoprotein;
DE AltName: Full=Orosomucoid;
DE Short=OMD;
DE Flags: Precursor;
GN Name=Orm1;
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].
RX PubMed=6270146; DOI=10.1016/s0021-9258(19)68577-7;
RA Ricca G.A., Taylor J.M.;
RT "Nucleotide sequence of rat alpha 1-acid glycoprotein messenger RNA.";
RL J. Biol. Chem. 256:11199-11202(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2943986; DOI=10.1128/mcb.5.12.3634-3639.1985;
RA Liao Y.C.J., Taylor J.M., Vannice J.L., Clawson G.A., Smuckler E.A.;
RT "Structure of the rat alpha 1-acid glycoprotein gene.";
RL Mol. Cell. Biol. 5:3634-3639(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3838547; DOI=10.1016/s0021-9258(18)89278-x;
RA Reinke R., Feigelson P.;
RT "Rat alpha 1-acid glycoprotein. Gene sequence and regulation by
RT glucocorticoids in transfected L-cells.";
RL J. Biol. Chem. 260:4397-4403(1985).
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 {ECO:0000250}.
CC -!- INDUCTION: Alpha-1-AGP is synthesized in the liver, the synthesis being
CC controlled by glucocorticoids, interleukin-1 and interleukin-6, it
CC 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}.
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DR EMBL; J00696; AAA40699.1; -; mRNA.
DR EMBL; V01216; CAA24527.1; -; mRNA.
DR EMBL; M11329; AAA40700.1; -; Genomic_DNA.
DR EMBL; M10614; AAA40701.1; -; Genomic_DNA.
DR PIR; A93069; OMRT1.
DR RefSeq; NP_445740.1; NM_053288.2.
DR AlphaFoldDB; P02764; -.
DR SMR; P02764; -.
DR STRING; 10116.ENSRNOP00000010454; -.
DR ChEMBL; CHEMBL3709434; -.
DR GlyConnect; 18; 10 N-Linked glycans.
DR GlyGen; P02764; 7 sites, 14 N-linked glycans (1 site).
DR iPTMnet; P02764; -.
DR PhosphoSitePlus; P02764; -.
DR PaxDb; P02764; -.
DR PRIDE; P02764; -.
DR GeneID; 24614; -.
DR KEGG; rno:24614; -.
DR UCSC; RGD:67390; rat.
DR CTD; 5004; -.
DR RGD; 67390; Orm1.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; P02764; -.
DR OrthoDB; 1257041at2759; -.
DR PhylomeDB; P02764; -.
DR TreeFam; TF343791; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P02764; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P02764; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0036094; F:small molecule binding; IDA:RGD.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEP:RGD.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IEP:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 2: Evidence at transcript level;
KW Acute phase; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..205
FT /note="Alpha-1-acid glycoprotein"
FT /id="PRO_0000017868"
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:0000255"
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 CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..183
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 23575 MW; E363A742C2B2DE06 CRC64;
MALHMVLVVL SLLPLLEAQN PEPANITLGI PITNETLKWL SDKWFYMGAA FRDPVFKQAV
QTIQTEYFYL TPNLINDTIE LREFQTTDDQ CVYNFTHLGV QRENGTLSKC AGAVKIFAHL
IVLKKHGTFM LAFNLTDENR GLSFYAKKPD LSPELRKIFQ QAVKDVGMDE SEIVFVDWTK
DKCSEQQKQQ LELEKETKKE TKKDP
