A1AG_RABIT
ID A1AG_RABIT Reviewed; 201 AA.
AC P25227;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alpha-1-acid glycoprotein;
DE AltName: Full=Orosomucoid;
DE Short=OMD;
DE Flags: Precursor;
GN Name=ORM1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1859410; DOI=10.1016/0006-291x(91)90136-u;
RA Ray B.K., Ray A.;
RT "Molecular cloning and nucleotide sequence of complementary DNA encoding
RT rabbit alpha 1-acid glycoprotein.";
RL Biochem. Biophys. Res. Commun. 178:507-513(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1534658; DOI=10.1016/s0006-291x(05)80956-8;
RA Ray B.K., Ray A.;
RT "Cloning and structural characterization of a rabbit genomic DNA for alpha
RT 1 acid glycoprotein.";
RL Biochem. Biophys. Res. Commun. 185:69-77(1992).
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 -!- 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; X58727; CAA41559.1; -; mRNA.
DR EMBL; M93344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JH0617; JH0617.
DR RefSeq; NP_001095165.1; NM_001101695.1.
DR AlphaFoldDB; P25227; -.
DR SMR; P25227; -.
DR STRING; 9986.ENSOCUP00000003988; -.
DR GeneID; 100009268; -.
DR KEGG; ocu:100009268; -.
DR CTD; 5004; -.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; P25227; -.
DR OMA; KTFMLAF; -.
DR OrthoDB; 1257041at2759; -.
DR TreeFam; TF343791; -.
DR Proteomes; UP000001811; Unplaced.
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; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..201
FT /note="Alpha-1-acid glycoprotein"
FT /id="PRO_0000017867"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..183
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 23028 MW; 97DC40E41C7DAC4D CRC64;
MALPWALAVL SLLPLLHAQD PACANFSTSP ITNATLDQLS HKWFFTASAF RNPKYKQLVQ
HTQAAFFYFT AIKEEDTLLL REYITTNNTC FYNSSIVRVQ RENGTLSKHD GIRNSVADLL
LLRDPGSFLL VFFAGKEQDK GMSFYTDKPK ASPEQLEEFY EALTCLGMNK TEVVYTDWTK
DLCEPLEKQH EEERKKEKAE S
