A1AG1_MUSCR
ID A1AG1_MUSCR Reviewed; 207 AA.
AC P21350;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Agp-1, Orm-1;
OS Mus caroli (Ryukyu mouse) (Ricefield mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10089;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2354997; DOI=10.1016/s0021-9258(18)86931-9;
RA Prowse K.R., Baumann H.;
RT "Molecular characterization and acute phase expression of the multiple Mus
RT caroli alpha 1-acid glycoprotein (AGP) genes. Differences in glucocorticoid
RT stimulation and regulatory elements between the rat and mouse AGP genes.";
RL J. Biol. Chem. 265:10201-10209(1990).
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 -!- DOMAIN: Contains a beta-barrel that binds various ligands in its
CC interior. {ECO:0000250}.
CC -!- MISCELLANEOUS: Eight genes coding for different forms of alpha-1-AGP
CC are present in mus carolis.
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; M34648; AAA37195.1; -; mRNA.
DR EMBL; M34647; AAA37197.1; -; mRNA.
DR PIR; B35425; B35425.
DR AlphaFoldDB; P21350; -.
DR SMR; P21350; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acute phase; Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..207
FT /note="Alpha-1-acid glycoprotein 1"
FT /id="PRO_0000017865"
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: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 DISULFID 91..184
FT /evidence="ECO:0000250"
FT VARIANT 38
FT /note="S -> G"
SQ SEQUENCE 207 AA; 23896 MW; A196EE6676F4D4C0 CRC64;
MALHMILVML SLLPLLEAQN PEHVNITIGE PITNETLSWL SDKWFFIGAA VLNPDYRQEI
QKMQMVFFNI TPNLINDTME LREYHTIDDH CVYNSTHLGI QRENGTLSKY VGGVKIFADL
IVLRKHGAFM LAFDLKDEKK RGLSLNAKRP DITPELREVF QKAVKHVGMD ESEIIFVDWK
KDKCGQQEKK QLELEKETKK DPEEGQA
