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 02-OCT-2024, entry version 230. 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 a 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; P19652: ORM2; NbExp=4; IntAct=EBI-976767, EBI-3911979; 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}; 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; 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 SASBDB; P02763; -. DR SMR; P02763; -. DR BioGRID; 111046; 81. DR IntAct; P02763; 48. 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; DB00572; Atropine. DR DrugBank; DB06237; Avanafil. DR DrugBank; DB08903; Bedaquiline. DR DrugBank; DB16703; Belumosudil. DR DrugBank; DB01086; Benzocaine. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01156; Bupropion. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB11148; Butamben. DR DrugBank; DB08907; Canagliflozin. DR DrugBank; DB00748; Carbinoxamine. DR DrugBank; DB00608; Chloroquine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01190; Clindamycin. DR DrugBank; DB00349; Clobazam. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB05239; Cobimetinib. DR DrugBank; DB00907; Cocaine. DR DrugBank; DB08865; Crizotinib. 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; DB08930; Dolutegravir. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB00476; Duloxetine. DR DrugBank; DB01126; Dutasteride. DR DrugBank; DB12147; Erdafitinib. 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; DB08906; Fluticasone furoate. DR DrugBank; DB15149; Futibatinib. DR DrugBank; DB00317; Gefitinib. DR DrugBank; DB11978; Glasdegib. 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; DB16200; Iptacopan. 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; DB01042; Melphalan. DR DrugBank; DB00454; Meperidine. DR DrugBank; DB00333; Methadone. DR DrugBank; DB01233; Metoclopramide. DR DrugBank; DB00683; Midazolam. DR DrugBank; DB08893; Mirabegron. DR DrugBank; DB01203; Nadolol. DR DrugBank; DB00731; Nateglinide. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB11828; Neratinib. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB12005; Nirogacestat. DR DrugBank; DB04821; Nomifensine. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB09074; Olaparib. 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; DB00296; Ropivacaine. 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; DB00342; Terfenadine. DR DrugBank; DB01041; Thalidomide. DR DrugBank; DB01685; Topiroxostat. DR DrugBank; DB08867; Ulipristal. DR DrugBank; DB09076; Umeclidinium. 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; DB11739; Vonoprazan. DR DrugBank; DB00682; Warfarin. DR DrugBank; DB00246; Ziprasidone. DR DrugCentral; P02763; -. DR CarbonylDB; P02763; -. DR GlyConnect; 718; 87 N-Linked glycans (5 sites). DR GlyCosmos; P02763; 5 sites, 84 glycans. DR GlyGen; P02763; 6 sites, 89 N-linked glycans (6 sites). DR iPTMnet; P02763; -. DR PhosphoSitePlus; P02763; -. DR BioMuta; ORM1; -. DR DMDM; 112877; -. DR jPOST; P02763; -. DR MassIVE; P02763; -. DR PaxDb; 9606-ENSP00000259396; -. DR PeptideAtlas; P02763; -. DR PRIDE; P02763; -. DR ProteomicsDB; 51584; -. DR Antibodypedia; 29904; 669 antibodies from 40 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 AGR; HGNC:8498; -. 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 OMA; KTFMLAF; -. DR OrthoDB; 4563010at2759; -. 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 1125 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 107 other cell types or tissues. 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 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 1: Evidence at protein level; KW 3D-structure; Acute phase; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Proteomics identification; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; 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 //