ID   Q91X23_MOUSE            Unreviewed;       207 AA.
AC   Q91X23;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Alpha-1-acid glycoprotein {ECO:0000256|PIRNR:PIRNR036899};
GN   Name=Orm1 {ECO:0000313|EMBL:AAH12725.1, ECO:0000313|MGI:MGI:97443};
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 {ECO:0000313|EMBL:AAH12725.1};
RN   [1] {ECO:0000313|EMBL:AAH12725.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH12725.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AAH12725.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|EMBL:CAJ18605.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a 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.
CC       {ECO:0000256|ARBA:ARBA00043849}.
CC   -!- FUNCTION: Functions as transport protein in the blood stream.
CC       {ECO:0000256|PIRNR:PIRNR036899}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|PIRNR:PIRNR036899}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000256|ARBA:ARBA00006889, ECO:0000256|PIRNR:PIRNR036899}.
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DR   EMBL; BC012725; AAH12725.1; -; mRNA.
DR   EMBL; CT010399; CAJ18605.1; -; mRNA.
DR   PIR; B26300; B26300.
DR   AlphaFoldDB; Q91X23; -.
DR   SMR; Q91X23; -.
DR   PeptideAtlas; Q91X23; -.
DR   AGR; MGI:97443; -.
DR   MGI; MGI:97443; Orm1.
DR   ChiTaRS; Orm1; mouse.
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   CDD; cd19451; lipocalin_AGP-like; 1.
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   PANTHER; PTHR11967; ALPHA-1-ACID GLYCOPROTEIN; 1.
DR   PANTHER; PTHR11967:SF2; ALPHA-1-ACID GLYCOPROTEIN 1; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036899; AGP; 1.
DR   PRINTS; PR00708; A1AGLPROTEIN.
DR   SUPFAM; SSF50814; Lipocalins; 1.
PE   2: Evidence at transcript level;
KW   Acute phase {ECO:0000256|ARBA:ARBA00022486};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR036899-50};
KW   Glycoprotein {ECO:0000256|PIRSR:PIRSR036899-51};
KW   Pyrrolidone carboxylic acid {ECO:0000256|PIRSR:PIRSR036899-51};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036899};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|PIRNR:PIRNR036899}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..207
FT                   /note="Alpha-1-acid glycoprotein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014312446"
FT   DOMAIN          42..180
FT                   /note="Lipocalin/cytosolic fatty-acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF00061"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036899-51"
FT   DISULFID        91..184
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036899-50"
SQ   SEQUENCE   207 AA;  23867 MW;  34CA3AF52D088863 CRC64;
     MALHTVLIIL SLLPMLEAQN PEHANFTIGE PITNETLSWL SDKWFFMGAA FRKLEYRQAI
     QTMQSEFFYL TTNLINDTIE LRESQTIGDQ CVYNSTHLGF QRENGTFSKY EGGVETFAHL
     IVLRKHGAFM LAFDLKDEKK RGLSLYAKRP DITPELQEVF QKAVTHVGMD ESEIIFVDWK
     KDRCGQQEKK QLELGKETKK DPEEGQA
//