A1AG1_HUMAN
ID A1AG1_HUMAN Reviewed; 201 AA.
AC P02763; B7ZKQ5; Q5T539; Q5U067; Q8TC16;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 219.
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=AGP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-38.
RX PubMed=2409529; DOI=10.1093/nar/13.11.3941;
RA Dente L., Ciliberto G., Cortese R.;
RT "Structure of the human alpha 1-acid glycoprotein gene: sequence homology
RT with other human acute phase protein genes.";
RL Nucleic Acids Res. 13:3941-3952(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-38.
RX PubMed=3770479; DOI=10.1016/0378-1119(86)90051-x;
RA Board P.G., Jones I.M., Bentley A.K.;
RT "Molecular cloning and nucleotide sequence of human alpha 1 acid
RT glycoprotein cDNA.";
RL Gene 44:127-131(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-38.
RX PubMed=2822385; DOI=10.1002/j.1460-2075.1987.tb02503.x;
RA Dente L., Pizza M.G., Metspalu A., Cortese R.;
RT "Structure and expression of the genes coding for human alpha 1-acid
RT glycoprotein.";
RL EMBO J. 6:2289-2296(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-38.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-38.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS CYS-167 AND MET-174.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 [9]
RP PROTEIN SEQUENCE OF 19-129, AND PYROGLUTAMATE FORMATION AT GLN-19.
RX PubMed=4711474; DOI=10.1021/bi00738a026;
RA Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T.,
RA Ishiguro M., Nanno S.;
RT "Structure of alpha 1-acid glycoprotein. The complete amino acid sequence,
RT multiple amino acid substitutions, and homology with the immunoglobulins.";
RL Biochemistry 12:2711-2724(1973).
RN [10]
RP PROTEIN SEQUENCE OF 129-201.
RX PubMed=4561179; DOI=10.1021/bi00770a022;
RA Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W.,
RA Schmid K.;
RT "Isolation and partial characterization of the cyanogen bromide fragments
RT of alpha 1-acid glycoprotein and the elucidation of the amino acid sequence
RT of the carboxyl-terminal cyanogen bromide fragment.";
RL Biochemistry 11:3817-3829(1972).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=4603214; DOI=10.1021/bi00710a006;
RA Schmid K., Buergi W., Collins J.H., Nanno S.;
RT "The disulfide bonds of alpha1-acid glycoprotein.";
RL Biochemistry 13:2694-2697(1974).
RN [12]
RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
RX PubMed=1567356; DOI=10.1042/bj2830105;
RA Treuheit M.J., Costello C.E., Halsall H.B.;
RT "Analysis of the five glycosylation sites of human alpha 1-acid
RT glycoprotein.";
RL Biochem. J. 283:105-112(1992).
RN [13]
RP GLYCOSYLATION AT ASN-33.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [14]
RP GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15253437; DOI=10.1021/pr034112b;
RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT "A new strategy for identification of N-glycosylated proteins and
RT unambiguous assignment of their glycosylation sites using HILIC enrichment
RT and partial deglycosylation.";
RL J. Proteome Res. 3:556-566(2004).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND
RP ASN-103.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND
RP ASN-103.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [18]
RP FUNCTION.
RX PubMed=17008009; DOI=10.1016/j.bbagen.2006.08.015;
RA Fitos I., Visy J., Zsila F., Mady G., Simonyi M.;
RT "Selective binding of imatinib to the genetic variants of human alpha1-acid
RT glycoprotein.";
RL Biochim. Biophys. Acta 1760:1704-1712(2006).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [20]
RP FUNCTION.
RX PubMed=17321687; DOI=10.1016/j.bbagen.2007.01.009;
RA Zsila F., Iwao Y.;
RT "The drug binding site of human alpha1-acid glycoprotein: insight from
RT induced circular dichroism and electronic absorption spectra.";
RL Biochim. Biophys. Acta 1770:797-809(2007).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-72, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [23]
RP GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, AND DISULFIDE
RP BONDS.
RX PubMed=18823996; DOI=10.1016/j.jmb.2008.09.020;
RA Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A.;
RT "The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid)
RT solved by UV RIP reveals the broad drug-binding activity of this human
RT plasma lipocalin.";
RL J. Mol. Biol. 384:393-405(2008).
RN [25]
RP VARIANTS GLN-38 AND MET-174.
RX PubMed=9050929; DOI=10.1007/s004390050378;
RA Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., Irizawa Y.;
RT "Human orosomucoid polymorphism: molecular basis of the three common ORM1
RT alleles, ORM1*F1, ORM1*F2, and ORM1*S.";
RL Hum. Genet. 99:393-398(1997).
CC -!- FUNCTION: Functions as transport protein in the blood stream. Binds
CC various ligands in the interior of its beta-barrel domain. Also binds
CC synthetic drugs and influences their distribution and availability in
CC the body. Appears to function in modulating the activity of the immune
CC system during the acute-phase reaction. {ECO:0000269|PubMed:17008009,
CC ECO:0000269|PubMed:17321687}.
CC -!- INTERACTION:
CC P02763; P05121: SERPINE1; NbExp=4; IntAct=EBI-976767, EBI-953978;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, interleukin-1
CC and interleukin-6, It increases 5- to 50-fold upon inflammation.
CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its
CC interior. {ECO:0000269|PubMed:18823996}.
CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4
CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
CC {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437,
CC ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
CC -!- POLYMORPHISM: Three common alleles of ORM1 are known. ORM1*F1 has Gln-
CC 38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg-38/Val-174.
CC The sequence shown is that of allele ORM1*S.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X02544; CAA26397.1; -; mRNA.
DR EMBL; M13692; AAA35515.1; -; mRNA.
DR EMBL; X05779; CAA29229.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05780; CAA29229.1; JOINED; Genomic_DNA.
DR EMBL; X05781; CAA29229.1; JOINED; Genomic_DNA.
DR EMBL; X05782; CAA29229.1; JOINED; Genomic_DNA.
DR EMBL; X05783; CAA29229.1; JOINED; Genomic_DNA.
DR EMBL; X05784; CAA29229.1; JOINED; Genomic_DNA.
DR EMBL; X06676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X06680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT019790; AAV38593.1; -; mRNA.
DR EMBL; AK312035; BAG34972.1; -; mRNA.
DR EMBL; AL356796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87416.1; -; Genomic_DNA.
DR EMBL; BC104818; AAI04819.1; -; mRNA.
DR EMBL; BC104820; AAI04821.1; -; mRNA.
DR EMBL; BC143313; AAI43314.1; -; mRNA.
DR EMBL; BC143314; AAI43315.1; -; mRNA.
DR EMBL; BC026238; AAH26238.1; -; mRNA.
DR CCDS; CCDS6803.1; -.
DR PIR; A28346; OMHU1.
DR RefSeq; NP_000598.2; NM_000607.2.
DR PDB; 3KQ0; X-ray; 1.80 A; A=19-201.
DR PDBsum; 3KQ0; -.
DR AlphaFoldDB; P02763; -.
DR BioGRID; 111046; 78.
DR IntAct; P02763; 17.
DR MINT; P02763; -.
DR STRING; 9606.ENSP00000259396; -.
DR BindingDB; P02763; -.
DR ChEMBL; CHEMBL4285; -.
DR DrugBank; DB12001; Abemaciclib.
DR DrugBank; DB05812; Abiraterone.
DR DrugBank; DB11703; Acalabrutinib.
DR DrugBank; DB01418; Acenocoumarol.
DR DrugBank; DB01426; Ajmaline.
DR DrugBank; DB00802; Alfentanil.
DR DrugBank; DB00346; Alfuzosin.
DR DrugBank; DB00404; Alprazolam.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00276; Amsacrine.
DR DrugBank; DB01429; Aprindine.
DR DrugBank; DB09229; Aranidipine.
DR DrugBank; DB00278; Argatroban.
DR DrugBank; DB09204; Arotinolol.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB01072; Atazanavir.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB06237; Avanafil.
DR DrugBank; DB16703; Belumosudil.
DR DrugBank; DB01086; Benzocaine.
DR DrugBank; DB01156; Bupropion.
DR DrugBank; DB00490; Buspirone.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB08907; Canagliflozin.
DR DrugBank; DB00608; Chloroquine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01190; Clindamycin.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB00080; Daptomycin.
DR DrugBank; DB01264; Darunavir.
DR DrugBank; DB11637; Delamanid.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB00343; Diltiazem.
DR DrugBank; DB00975; Dipyridamole.
DR DrugBank; DB00280; Disopyramide.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB00476; Duloxetine.
DR DrugBank; DB01126; Dutasteride.
DR DrugBank; DB00530; Erlotinib.
DR DrugBank; DB12235; Estetrol.
DR DrugBank; DB12466; Favipiravir.
DR DrugBank; DB00813; Fentanyl.
DR DrugBank; DB00950; Fexofenadine.
DR DrugBank; DB01195; Flecainide.
DR DrugBank; DB00472; Fluoxetine.
DR DrugBank; DB00317; Gefitinib.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB11575; Grazoprevir.
DR DrugBank; DB01611; Hydroxychloroquine.
DR DrugBank; DB09053; Ibrutinib.
DR DrugBank; DB00619; Imatinib.
DR DrugBank; DB09262; Imidafenacin.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB00808; Indapamide.
DR DrugBank; DB00332; Ipratropium.
DR DrugBank; DB01029; Irbesartan.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB08820; Ivacaftor.
DR DrugBank; DB00598; Labetalol.
DR DrugBank; DB09236; Lacidipine.
DR DrugBank; DB00281; Lidocaine.
DR DrugBank; DB01627; Lincomycin.
DR DrugBank; DB01601; Lopinavir.
DR DrugBank; DB12674; Lurbinectedin.
DR DrugBank; DB08932; Macitentan.
DR DrugBank; DB00934; Maprotiline.
DR DrugBank; DB06234; Maribavir.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB01233; Metoclopramide.
DR DrugBank; DB08893; Mirabegron.
DR DrugBank; DB01203; Nadolol.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB11828; Neratinib.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB04821; Nomifensine.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB01062; Oxybutynin.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB14582; Patisiran.
DR DrugBank; DB01359; Penbutolol.
DR DrugBank; DB12978; Pexidartinib.
DR DrugBank; DB00946; Phenprocoumon.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB08860; Pitavastatin.
DR DrugBank; DB11642; Pitolisant.
DR DrugBank; DB00457; Prazosin.
DR DrugBank; DB00396; Progesterone.
DR DrugBank; DB00571; Propranolol.
DR DrugBank; DB00908; Quinidine.
DR DrugBank; DB00481; Raloxifene.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB11853; Relugolix.
DR DrugBank; DB00409; Remoxipride.
DR DrugBank; DB01045; Rifampicin.
DR DrugBank; DB08931; Riociguat.
DR DrugBank; DB14840; Ripretinib.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB00503; Ritonavir.
DR DrugBank; DB00938; Salmeterol.
DR DrugBank; DB01232; Saquinavir.
DR DrugBank; DB11689; Selumetinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB01591; Solifenacin.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00864; Tacrolimus.
DR DrugBank; DB00706; Tamsulosin.
DR DrugBank; DB05521; Telaprevir.
DR DrugBank; DB00853; Temozolomide.
DR DrugBank; DB15133; Tepotinib.
DR DrugBank; DB00857; Terbinafine.
DR DrugBank; DB01041; Thalidomide.
DR DrugBank; DB01685; Topiroxostat.
DR DrugBank; DB08867; Ulipristal.
DR DrugBank; DB00512; Vancomycin.
DR DrugBank; DB05294; Vandetanib.
DR DrugBank; DB08881; Vemurafenib.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB11641; Vinflunine.
DR DrugBank; DB08828; Vismodegib.
DR DrugBank; DB00682; Warfarin.
DR DrugBank; DB00246; Ziprasidone.
DR DrugCentral; P02763; -.
DR CarbonylDB; P02763; -.
DR GlyConnect; 718; 87 N-Linked glycans (5 sites).
DR GlyGen; P02763; 6 sites, 82 N-linked glycans (6 sites).
DR iPTMnet; P02763; -.
DR PhosphoSitePlus; P02763; -.
DR BioMuta; ORM1; -.
DR DMDM; 112877; -.
DR SWISS-2DPAGE; P02763; -.
DR EPD; P02763; -.
DR jPOST; P02763; -.
DR MassIVE; P02763; -.
DR PaxDb; P02763; -.
DR PeptideAtlas; P02763; -.
DR PRIDE; P02763; -.
DR ProteomicsDB; 51584; -.
DR Antibodypedia; 29904; 630 antibodies from 39 providers.
DR DNASU; 5004; -.
DR Ensembl; ENST00000259396.9; ENSP00000259396.8; ENSG00000229314.6.
DR GeneID; 5004; -.
DR KEGG; hsa:5004; -.
DR MANE-Select; ENST00000259396.9; ENSP00000259396.8; NM_000607.4; NP_000598.2.
DR UCSC; uc004bik.5; human.
DR CTD; 5004; -.
DR DisGeNET; 5004; -.
DR GeneCards; ORM1; -.
DR HGNC; HGNC:8498; ORM1.
DR HPA; ENSG00000229314; Tissue enriched (liver).
DR MIM; 138600; gene.
DR neXtProt; NX_P02763; -.
DR OpenTargets; ENSG00000229314; -.
DR PharmGKB; PA260; -.
DR VEuPathDB; HostDB:ENSG00000229314; -.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR GeneTree; ENSGT00390000012130; -.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; P02763; -.
DR OrthoDB; 1025450at2759; -.
DR PhylomeDB; P02763; -.
DR TreeFam; TF343791; -.
DR PathwayCommons; P02763; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P02763; -.
DR BioGRID-ORCS; 5004; 23 hits in 1047 CRISPR screens.
DR ChiTaRS; ORM1; human.
DR EvolutionaryTrace; P02763; -.
DR GeneWiki; ORM1; -.
DR GenomeRNAi; 5004; -.
DR Pharos; P02763; Tbio.
DR PRO; PR:P02763; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P02763; protein.
DR Bgee; ENSG00000229314; Expressed in right lobe of liver and 105 other tissues.
DR Genevisible; P02763; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:CACAO.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:CACAO.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acute phase; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:4711474"
FT CHAIN 19..201
FT /note="Alpha-1-acid glycoprotein 1"
FT /id="PRO_0000017860"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4711474"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:22171320"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:4603214"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437,
FT ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:4603214"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT /id="CAR_000170"
FT DISULFID 23..165
FT /evidence="ECO:0000269|PubMed:4603214"
FT DISULFID 90..183
FT /evidence="ECO:0000269|PubMed:4603214"
FT VARIANT 38
FT /note="R -> Q (in allele ORM1*S; dbSNP:rs17650)"
FT /evidence="ECO:0000269|PubMed:15164053,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9050929,
FT ECO:0000269|Ref.7"
FT /id="VAR_013840"
FT VARIANT 167
FT /note="R -> C (in dbSNP:rs3182034)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_056166"
FT VARIANT 174
FT /note="V -> M (in allele ORM1*F2; dbSNP:rs1126801)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9050929"
FT /id="VAR_013841"
FT CONFLICT 170
FT /note="K -> R (in Ref. 8; AAI43315)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:3KQ0"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:3KQ0"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3KQ0"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3KQ0"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3KQ0"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3KQ0"
SQ SEQUENCE 201 AA; 23540 MW; CC2AD1FD9C8CBFA4 CRC64;
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ
EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL
ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK
DKCEPLEKQH EKERKQEEGE S
