A1AG8_MUSCR
ID A1AG8_MUSCR Reviewed; 207 AA.
AC P21352;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Alpha-1-acid glycoprotein 8;
DE Short=AGP 8;
DE AltName: Full=Orosomucoid-8;
DE Short=OMD 8;
DE Flags: Precursor;
GN Name=Orm8; Synonyms=Agp-8, Orm-8;
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}.
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DR EMBL; M34649; AAA37198.1; -; mRNA.
DR EMBL; M34646; AAB67844.1; -; mRNA.
DR PIR; C35425; C35425.
DR PIR; D35425; D35425.
DR AlphaFoldDB; P21352; -.
DR SMR; P21352; -.
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; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..207
FT /note="Alpha-1-acid glycoprotein 8"
FT /id="PRO_0000017866"
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 10
FT /note="L -> V"
FT VARIANT 24
FT /note="A -> V"
FT VARIANT 50
FT /note="A -> R"
FT VARIANT 98
FT /note="L -> V"
SQ SEQUENCE 207 AA; 23912 MW; 2BADBF5EF94E7EB7 CRC64;
MALHTVLIML SLLPMLEAQN PEHANITIGE PITNETLGWL SDKWFFMGAA FRKLEYRQAI
QMMQTEFFYL TTNLINDTIE LRESQTIGDQ CVYNSTHLGF QRENGTFSKY EGGVETFAHL
IVLRKHGAFM LAFDLNDEKK RGLSLYAKRP DMTLELREVF QKAVKHVGMD ESEIIFVDWK
KDKCGQQEKK QLELGKETKK DPEEGQA
