ID A1AG2_HUMAN Reviewed; 201 AA. AC P19652; B2R5L2; Q16571; Q5T538; Q6IB74; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 02-SEP-2026, entry version 221. DE RecName: Full=Alpha-1-acid glycoprotein 2; DE Short=AGP 2; DE AltName: Full=Orosomucoid-2; DE Short=OMD 2; DE Flags: Precursor; GN Name=ORM2; Synonyms=AGP2; 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 [GENOMIC DNA]. 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2970990; DOI=10.1016/0378-1119(88)90228-4; RA Merritt C.M., Board P.G.; RT "Structure and characterisation of a duplicated human alpha 1 acid RT glycoprotein gene."; RL Gene 66:97-106(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 [8] 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 [9] 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 [10] RP PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, AND RP IDENTIFICATION BY MASS 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 [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33. 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 [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND ASN-93. 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 [13] 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 [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; 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 [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, 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 [16] 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 [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN RP COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE, FUNCTION, RP DISULFIDE BONDS, AND DOMAIN. RX PubMed=21349832; DOI=10.1074/jbc.m110.208926; RA Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H., RA Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.; RT "Structural insights into differences in drug-binding selectivity between RT two forms of human {alpha}1-acid glycoprotein genetic variants, the A and RT F1*S forms."; RL J. Biol. Chem. 286:14427-14434(2011). CC -!- FUNCTION: Functions as a transport protein in the blood stream. Binds CC various hydrophobic ligands in the interior of its beta-barrel domain. CC Also binds synthetic drugs and influences their distribution and CC availability. Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC {ECO:0000269|PubMed:21349832}. CC -!- INTERACTION: CC P19652; P02763: ORM1; NbExp=4; IntAct=EBI-3911979, EBI-976767; 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:21349832}. CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). CC {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, CC ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}. CC -!- POLYMORPHISM: Many different variants of ORM2 are known. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA29873.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAA29874.1; 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; X06675; CAA29874.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05780; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06674; CAA29873.2; ALT_SEQ; Genomic_DNA. DR EMBL; X06676; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06677; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06678; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06679; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06680; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X05784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M21540; AAA51549.1; -; Genomic_DNA. DR EMBL; AK312226; BAG35159.1; -; mRNA. DR EMBL; CR456930; CAG33211.1; -; mRNA. DR EMBL; AL356796; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87417.1; -; Genomic_DNA. DR EMBL; BC015964; AAH15964.1; -; mRNA. DR EMBL; BC056239; AAH56239.1; -; mRNA. DR CCDS; CCDS6804.1; -. DR PIR; JT0326; OMHU2. DR RefSeq; NP_000599.1; NM_000608.4. DR PDB; 3APU; X-ray; 2.10 A; A/B=19-201. DR PDB; 3APV; X-ray; 2.15 A; A/B=19-201. DR PDB; 3APW; X-ray; 2.20 A; A/B=19-201. DR PDB; 3APX; X-ray; 2.20 A; A=19-201. DR PDB; 7OUB; X-ray; 1.82 A; B=19-190. DR AlphaFoldDB; P19652; -. DR SMR; P19652; -. DR BioGRID; 111047; 22. DR FunCoup; P19652; 81. DR IntAct; P19652; 15. DR NDEx; IQUERY-CP-ORM2; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000394936; -. DR ChEMBL; CHEMBL5958; -. DR DrugBank; DB12001; Abemaciclib. DR DrugBank; DB11703; Acalabrutinib. DR DrugBank; DB00404; Alprazolam. DR DrugBank; DB00278; Argatroban. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB01072; Atazanavir. DR DrugBank; DB00289; Atomoxetine. DR DrugBank; DB01086; Benzocaine. DR DrugBank; DB00748; Carbinoxamine. DR DrugBank; DB00608; Chloroquine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00907; Cocaine. DR DrugBank; DB08865; Crizotinib. DR DrugBank; DB00280; Disopyramide. DR DrugBank; DB08930; Dolutegravir. DR DrugBank; DB00476; Duloxetine. DR DrugBank; DB12147; Erdafitinib. DR DrugBank; DB12466; Favipiravir. DR DrugBank; DB00813; Fentanyl. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB01195; Flecainide. DR DrugBank; DB11978; Glasdegib. DR DrugBank; DB00986; Glycopyrronium. DR DrugBank; DB01611; Hydroxychloroquine. DR DrugBank; DB09053; Ibrutinib. DR DrugBank; DB09262; Imidafenacin. DR DrugBank; DB00808; Indapamide. DR DrugBank; DB00332; Ipratropium. DR DrugBank; DB01029; Irbesartan. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB00598; Labetalol. DR DrugBank; DB00281; Lidocaine. DR DrugBank; DB08932; Macitentan. DR DrugBank; DB01203; Nadolol. DR DrugBank; DB11828; Neratinib. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB12005; Nirogacestat. DR DrugBank; DB00497; Oxycodone. DR DrugBank; DB14582; Patisiran. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00409; Remoxipride. DR DrugBank; DB01045; Rifampin. DR DrugBank; DB14840; Ripretinib. DR DrugBank; DB00938; Salmeterol. DR DrugBank; DB11689; Selumetinib. DR DrugBank; DB01591; Solifenacin. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB00857; Terbinafine. DR DrugBank; DB00342; Terfenadine. DR DrugBank; DB01041; Thalidomide. DR DrugBank; DB00512; Vancomycin. DR DrugBank; DB11641; Vinflunine. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR GlyConnect; P19652; 114 N-Linked glycans (6 sites). DR GlyCosmos; P19652; 6 sites, 98 glycans. DR GlyGen; P19652; 7 sites, 148 N-linked glycans (7 sites). DR iPTMnet; P19652; -. DR PhosphoSitePlus; P19652; -. DR BioMuta; ORM2; -. DR DMDM; 231458; -. DR jPOST; P19652; -. DR MassIVE; P19652; -. DR PaxDb; 9606-ENSP00000394936; -. DR PeptideAtlas; P19652; -. DR ProteomicsDB; 53685; -. DR Antibodypedia; 29909; 266 antibodies from 30 providers. DR DNASU; 5005; -. DR Ensembl; ENST00000431067.4; ENSP00000394936.2; ENSG00000228278.6. DR GeneID; 5005; -. DR KEGG; hsa:5005; -. DR MANE-Select; ENST00000431067.4; ENSP00000394936.2; NM_000608.4; NP_000599.1. DR UCSC; uc004bil.4; human. DR AGR; HGNC:8499; -. DR ClinPGx; PA32818; -. DR CTD; 5005; -. DR DisGeNET; 5005; -. DR GeneCards; ORM2; -. DR HGNC; HGNC:8499; ORM2. DR HPA; ENSG00000228278; Tissue enriched (liver). DR MIM; 138610; gene. DR OpenTargets; ENSG00000228278; -. DR VEuPathDB; HostDB:ENSG00000228278; -. DR eggNOG; ENOG502S0Q2; Eukaryota. DR GeneTree; ENSGT00390000012130; -. DR HOGENOM; CLU_117688_0_0_1; -. DR InParanoid; P19652; -. DR OMA; NWGLSFY; -. DR OrthoDB; 9448848at2759; -. DR PAN-GO; P19652; 1 GO annotation based on evolutionary models. DR PhylomeDB; P19652; -. DR PathwayCommons; P19652; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P19652; -. DR SIGNOR; P19652; -. DR Agora; ENSG00000228278; -. DR BioGRID-ORCS; 5005; 12 hits in 1100 CRISPR screens. DR ChiTaRS; ORM2; human. DR EvolutionaryTrace; P19652; -. DR GenomeRNAi; 5005; -. DR Pharos; P19652; Tbio. DR PRO; PR:P19652; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P19652; protein. DR Bgee; ENSG00000228278; Expressed in right lobe of liver and 98 other cell types or tissues. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; 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:0140104; F:molecular carrier activity; IBA:GO_Central. DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IBA:GO_Central. DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc. 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 FunFam; 2.40.128.20:FF:000012; Alpha-1-acid glycoprotein 2; 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:SF3; ALPHA-1-ACID GLYCOPROTEIN 2; 1. DR Pfam; PF00061; Lipocalin; 1. DR PIRSF; PIRSF036899; AGP; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR SUPFAM; SSF50814; Lipocalins; 1. DR PDBsum; 3APU; -. DR PDBsum; 3APV; -. DR PDBsum; 3APW; -. DR PDBsum; 3APX; -. DR PDBsum; 7OUB; -. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Disulfide bond; Glycoprotein; KW Proteomics identification; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal; Transport. FT SIGNAL 1..18 FT CHAIN 19..201 FT /note="Alpha-1-acid glycoprotein 2" FT /id="PRO_0000017861" FT MOD_RES 19 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:15253437" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) (complex) 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:19159218, 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:19159218" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952" FT CARBOHYD 93 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:15253437, ECO:0000269|PubMed:1567356, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1567356, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218" FT /id="CAR_000171" FT DISULFID 23..165 FT DISULFID 90..183 FT VARIANT 38 FT /note="R -> Q (in dbSNP:rs147969317)" FT /id="VAR_014667" FT VARIANT 99 FT /note="V -> A (in dbSNP:rs2636889)" FT /id="VAR_050172" FT VARIANT 141 FT /note="G -> R (in dbSNP:rs12685968)" FT /id="VAR_050173" FT VARIANT 167 FT /note="C -> R (in dbSNP:rs1126777)" FT /id="VAR_050174" FT VARIANT 174 FT /note="M -> V (in dbSNP:rs2636890)" FT /id="VAR_050175" FT CONFLICT 32 FT /note="T -> I (in Ref. 4; CAG33211)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="E -> D (in Ref. 3; BAG35159)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="T -> I (in Ref. 3; BAG35159)" FT /evidence="ECO:0000305" FT CONFLICT 162 FT /note="A -> V (in Ref. 3; BAG35159)" FT /evidence="ECO:0000305" FT CONFLICT 189 FT /note="Q -> H (in Ref. 3; BAG35159)" FT /evidence="ECO:0000305" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:7OUB" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:3APU" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:3APX" FT HELIX 33..39 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 41..51 FT /evidence="ECO:0007829|PDB:7OUB" FT HELIX 53..59 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 62..72 FT /evidence="ECO:0007829|PDB:7OUB" FT TURN 73..76 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 77..86 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 89..100 FT /evidence="ECO:0007829|PDB:7OUB" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 113..120 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:7OUB" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:7OUB" FT STRAND 141..150 FT /evidence="ECO:0007829|PDB:7OUB" FT HELIX 153..165 FT /evidence="ECO:0007829|PDB:7OUB" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:7OUB" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:7OUB" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:7OUB" SQ SEQUENCE 201 AA; 23603 MW; 49167ABCC22933B9 CRC64; MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK DKCEPLEKQH EKERKQEEGE S //