A1AG2_HUMAN
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 03-AUG-2022, entry version 203.
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 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 -!- 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};
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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_000608.2.
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 PDBsum; 3APU; -.
DR PDBsum; 3APV; -.
DR PDBsum; 3APW; -.
DR PDBsum; 3APX; -.
DR PDBsum; 7OUB; -.
DR AlphaFoldDB; P19652; -.
DR SMR; P19652; -.
DR BioGRID; 111047; 20.
DR IntAct; P19652; 5.
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; DB00608; Chloroquine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB00280; Disopyramide.
DR DrugBank; DB00476; Duloxetine.
DR DrugBank; DB12466; Favipiravir.
DR DrugBank; DB00813; Fentanyl.
DR DrugBank; DB00950; Fexofenadine.
DR DrugBank; DB01195; Flecainide.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB01611; Hydroxychloroquine.
DR DrugBank; DB09053; Ibrutinib.
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; DB00598; Labetalol.
DR DrugBank; DB00281; Lidocaine.
DR DrugBank; DB08932; Macitentan.
DR DrugBank; DB01203; Nadolol.
DR DrugBank; DB11828; Neratinib.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB14582; Patisiran.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00409; Remoxipride.
DR DrugBank; DB01045; Rifampicin.
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; 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; 14; 74 N-Linked glycans (6 sites).
DR GlyGen; P19652; 7 sites, 99 N-linked glycans (7 sites).
DR iPTMnet; P19652; -.
DR PhosphoSitePlus; P19652; -.
DR BioMuta; ORM2; -.
DR DMDM; 231458; -.
DR DOSAC-COBS-2DPAGE; P19652; -.
DR SWISS-2DPAGE; P19652; -.
DR jPOST; P19652; -.
DR MassIVE; P19652; -.
DR MaxQB; P19652; -.
DR PaxDb; P19652; -.
DR PeptideAtlas; P19652; -.
DR PRIDE; P19652; -.
DR ProteomicsDB; 53685; -.
DR Antibodypedia; 29909; 262 antibodies from 28 providers.
DR DNASU; 5005; -.
DR Ensembl; ENST00000431067.4; ENSP00000394936.2; ENSG00000228278.5.
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 CTD; 5005; -.
DR DisGeNET; 5005; -.
DR GeneCards; ORM2; -.
DR HGNC; HGNC:8499; ORM2.
DR HPA; ENSG00000228278; Tissue enriched (liver).
DR MIM; 138610; gene.
DR neXtProt; NX_P19652; -.
DR OpenTargets; ENSG00000228278; -.
DR PharmGKB; PA32818; -.
DR VEuPathDB; HostDB:ENSG00000228278; -.
DR eggNOG; ENOG502S0Q2; Eukaryota.
DR GeneTree; ENSGT00390000012130; -.
DR HOGENOM; CLU_117688_0_0_1; -.
DR InParanoid; P19652; -.
DR OMA; CAPLIPV; -.
DR OrthoDB; 1257041at2759; -.
DR PhylomeDB; P19652; -.
DR TreeFam; TF343791; -.
DR PathwayCommons; P19652; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P19652; -.
DR BioGRID-ORCS; 5005; 11 hits in 1023 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 96 other tissues.
DR Genevisible; P19652; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
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; TAS:Reactome.
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: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 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; Disulfide bond; Glycoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW 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 TURN 20..23
FT /evidence="ECO:0007829|PDB:3APX"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3APU"
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
