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Alpha-1-acid glycoprotein 1 (AGP 1) (Orosomucoid-1) (OMD 1)

 A1AG1_HUMAN             Reviewed;         201 AA.
P02763; B7ZKQ5; Q5T539; Q5U067; Q8TC16;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
12-SEP-2018, entry version 199.
RecName: Full=Alpha-1-acid glycoprotein 1;
Short=AGP 1;
AltName: Full=Orosomucoid-1;
Short=OMD 1;
Flags: Precursor;
Name=ORM1; Synonyms=AGP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2822385;
Dente L., Pizza M.G., Metspalu A., Cortese R.;
"Structure and expression of the genes coding for human alpha 1-acid
glycoprotein.";
EMBO J. 6:2289-2296(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3770479; DOI=10.1016/0378-1119(86)90051-X;
Board P.G., Jones I.M., Bentley A.K.;
"Molecular cloning and nucleotide sequence of human alpha 1 acid
glycoprotein cDNA.";
Gene 44:127-131(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2409529; DOI=10.1093/nar/13.11.3941;
Dente L., Ciliberto G., Cortese R.;
"Structure of the human alpha 1-acid glycoprotein gene: sequence
homology with other human acute phase protein genes.";
Nucleic Acids Res. 13:3941-3952(1985).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-38.
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-38.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-38; CYS-167
AND MET-174.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 19-129, AND PYROGLUTAMATE FORMATION AT GLN-19.
PubMed=4711474; DOI=10.1021/bi00738a026;
Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T.,
Ishiguro M., Nanno S.;
"Structure of alpha 1-acid glycoprotein. The complete amino acid
sequence, multiple amino acid substitutions, and homology with the
immunoglobulins.";
Biochemistry 12:2711-2724(1973).
[10]
PROTEIN SEQUENCE OF 129-201.
PubMed=4561179; DOI=10.1021/bi00770a022;
Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W.,
Schmid K.;
"Isolation and partial characterization of the cyanogen bromide
fragments of alpha 1-acid glycoprotein and the elucidation of the
amino acid sequence of the carboxyl-terminal cyanogen bromide
fragment.";
Biochemistry 11:3817-3829(1972).
[11]
DISULFIDE BONDS.
PubMed=4603214; DOI=10.1021/bi00710a006;
Schmid K., Buergi W., Collins J.H., Nanno S.;
"The disulfide bonds of alpha1-acid glycoprotein.";
Biochemistry 13:2694-2697(1974).
[12]
GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
PubMed=1567356; DOI=10.1042/bj2830105;
Treuheit M.J., Costello C.E., Halsall H.B.;
"Analysis of the five glycosylation sites of human alpha 1-acid
glycoprotein.";
Biochem. J. 283:105-112(1992).
[13]
GLYCOSYLATION AT ASN-33.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[14]
GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15253437; DOI=10.1021/pr034112b;
Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
"A new strategy for identification of N-glycosylated proteins and
unambiguous assignment of their glycosylation sites using HILIC
enrichment and partial deglycosylation.";
J. Proteome Res. 3:556-566(2004).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93
AND ASN-103.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93
AND ASN-103.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
FUNCTION.
PubMed=17008009; DOI=10.1016/j.bbagen.2006.08.015;
Fitos I., Visy J., Zsila F., Mady G., Simonyi M.;
"Selective binding of imatinib to the genetic variants of human
alpha1-acid glycoprotein.";
Biochim. Biophys. Acta 1760:1704-1712(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[20]
FUNCTION.
PubMed=17321687; DOI=10.1016/j.bbagen.2007.01.009;
Zsila F., Iwao Y.;
"The drug binding site of human alpha1-acid glycoprotein: insight from
induced circular dichroism and electronic absorption spectra.";
Biochim. Biophys. Acta 1770:797-809(2007).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-72, AND
STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[23]
GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[24]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, AND DISULFIDE
BONDS.
PubMed=18823996; DOI=10.1016/j.jmb.2008.09.020;
Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A.;
"The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid)
solved by UV RIP reveals the broad drug-binding activity of this human
plasma lipocalin.";
J. Mol. Biol. 384:393-405(2008).
[25]
VARIANTS ARG-38 AND MET-174.
PubMed=9050929; DOI=10.1007/s004390050378;
Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N.,
Irizawa Y.;
"Human orosomucoid polymorphism: molecular basis of the three common
ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S.";
Hum. Genet. 99:393-398(1997).
-!- FUNCTION: Functions as transport protein in the blood stream.
Binds various ligands in the interior of its beta-barrel domain.
Also binds synthetic drugs and influences their distribution and
availability in the body. Appears to function in modulating the
activity of the immune system during the acute-phase reaction.
{ECO:0000269|PubMed:17008009, ECO:0000269|PubMed:17321687}.
-!- INTERACTION:
P05121:SERPINE1; NbExp=4; IntAct=EBI-976767, EBI-953978;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- INDUCTION: Synthesis is controlled by glucocorticoids,
interleukin-1 and interleukin-6, It increases 5- to 50-fold upon
inflammation.
-!- DOMAIN: Contains a beta-barrel that binds various ligands in its
interior. {ECO:0000269|PubMed:18823996}.
-!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4
(minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
{ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15253437,
ECO:0000269|PubMed:1567356, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
-!- POLYMORPHISM: Three common alleles of ORM1 are known. ORM1*F1 has
Gln-38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg-
38/Val-174. The sequence shown is that of allele ORM1*F1.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA29229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X02544; CAA26397.1; -; mRNA.
EMBL; M13692; AAA35515.1; -; mRNA.
EMBL; X05779; CAA29229.1; ALT_SEQ; Genomic_DNA.
EMBL; X05780; CAA29229.1; JOINED; Genomic_DNA.
EMBL; X05781; CAA29229.1; JOINED; Genomic_DNA.
EMBL; X05782; CAA29229.1; JOINED; Genomic_DNA.
EMBL; X05783; CAA29229.1; JOINED; Genomic_DNA.
EMBL; X05784; CAA29229.1; JOINED; Genomic_DNA.
EMBL; X06676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X06680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BT019790; AAV38593.1; -; mRNA.
EMBL; AK312035; BAG34972.1; -; mRNA.
EMBL; AL356796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87416.1; -; Genomic_DNA.
EMBL; BC104818; AAI04819.1; -; mRNA.
EMBL; BC104820; AAI04821.1; -; mRNA.
EMBL; BC143313; AAI43314.1; -; mRNA.
EMBL; BC143314; AAI43315.1; -; mRNA.
EMBL; BC026238; AAH26238.1; -; mRNA.
CCDS; CCDS6803.1; -.
PIR; A28346; OMHU1.
RefSeq; NP_000598.2; NM_000607.2.
UniGene; Hs.522356; -.
PDB; 3KQ0; X-ray; 1.80 A; A=19-201.
PDBsum; 3KQ0; -.
ProteinModelPortal; P02763; -.
SMR; P02763; -.
BioGrid; 111046; 16.
IntAct; P02763; 7.
STRING; 9606.ENSP00000259396; -.
BindingDB; P02763; -.
ChEMBL; CHEMBL4285; -.
DrugBank; DB05812; Abiraterone.
DrugBank; DB01418; Acenocoumarol.
DrugBank; DB01426; Ajmaline.
DrugBank; DB00802; Alfentanil.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00543; Amoxapine.
DrugBank; DB01429; Aprindine.
DrugBank; DB01156; Bupropion.
DrugBank; DB08907; Canagliflozin.
DrugBank; DB00482; Celecoxib.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB01151; Desipramine.
DrugBank; DB00280; Disopyramide.
DrugBank; DB00590; Doxazosin.
DrugBank; DB01142; Doxepin.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00472; Fluoxetine.
DrugBank; DB00317; Gefitinib.
DrugBank; DB00619; Imatinib.
DrugBank; DB00458; Imipramine.
DrugBank; DB08820; Ivacaftor.
DrugBank; DB00934; Maprotiline.
DrugBank; DB08893; Mirabegron.
DrugBank; DB00731; Nateglinide.
DrugBank; DB04821; Nomifensine.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB00497; Oxycodone.
DrugBank; DB01359; Penbutolol.
DrugBank; DB00454; Pethidine.
DrugBank; DB00946; Phenprocoumon.
DrugBank; DB08860; Pitavastatin.
DrugBank; DB00457; Prazosin.
DrugBank; DB00571; Propranolol.
DrugBank; DB00908; Quinidine.
DrugBank; DB08931; Riociguat.
DrugBank; DB01232; Saquinavir.
DrugBank; DB00864; Tacrolimus.
DrugBank; DB00706; Tamsulosin.
DrugBank; DB05521; Telaprevir.
DrugBank; DB01041; Thalidomide.
DrugBank; DB00656; Trazodone.
DrugBank; DB08867; Ulipristal.
DrugBank; DB05294; Vandetanib.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB08828; Vismodegib.
DrugBank; DB00682; Warfarin.
CarbonylDB; P02763; -.
GlyConnect; 14; -.
GlyConnect; 718; -.
iPTMnet; P02763; -.
PhosphoSitePlus; P02763; -.
UniCarbKB; P02763; -.
BioMuta; ORM1; -.
DMDM; 112877; -.
SWISS-2DPAGE; P02763; -.
EPD; P02763; -.
PaxDb; P02763; -.
PeptideAtlas; P02763; -.
PRIDE; P02763; -.
ProteomicsDB; 51584; -.
DNASU; 5004; -.
Ensembl; ENST00000259396; ENSP00000259396; ENSG00000229314.
GeneID; 5004; -.
KEGG; hsa:5004; -.
UCSC; uc004bik.5; human.
CTD; 5004; -.
DisGeNET; 5004; -.
EuPathDB; HostDB:ENSG00000229314.5; -.
GeneCards; ORM1; -.
HGNC; HGNC:8498; ORM1.
HPA; CAB006265; -.
HPA; HPA046438; -.
HPA; HPA047725; -.
HPA; HPA057726; -.
MIM; 138600; gene.
neXtProt; NX_P02763; -.
PharmGKB; PA260; -.
eggNOG; ENOG410IWZI; Eukaryota.
eggNOG; ENOG4111C49; LUCA.
HOGENOM; HOG000125170; -.
HOVERGEN; HBG000035; -.
InParanoid; P02763; -.
KO; K17308; -.
OrthoDB; EOG091G0NAQ; -.
PhylomeDB; P02763; -.
TreeFam; TF343791; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; ORM1; human.
EvolutionaryTrace; P02763; -.
GeneWiki; ORM1; -.
GenomeRNAi; 5004; -.
PRO; PR:P02763; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000229314; Expressed in 95 organ(s), highest expression level in liver.
CleanEx; HS_ORM1; -.
Genevisible; P02763; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:CACAO.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:CACAO.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0050716; P:positive regulation of interleukin-1 secretion; IDA:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IDA:UniProtKB.
GO; GO:0002682; P:regulation of immune system process; IEA:InterPro.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR001500; A1A_glycop.
InterPro; IPR012674; Calycin.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11967; PTHR11967; 1.
Pfam; PF00061; Lipocalin; 1.
PIRSF; PIRSF036899; AGP; 1.
PRINTS; PR00708; A1AGLPROTEIN.
SUPFAM; SSF50814; SSF50814; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
Transport.
SIGNAL 1 18 {ECO:0000269|PubMed:4711474}.
CHAIN 19 201 Alpha-1-acid glycoprotein 1.
/FTId=PRO_0000017860.
MOD_RES 19 19 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4711474}.
CARBOHYD 33 33 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:15253437,
ECO:0000269|PubMed:1567356,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:22171320}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:1567356,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:4603214}.
CARBOHYD 72 72 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15253437,
ECO:0000269|PubMed:1567356,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19838169}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:15253437,
ECO:0000269|PubMed:1567356,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4603214}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:1567356,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
/FTId=CAR_000170.
DISULFID 23 165 {ECO:0000269|PubMed:4603214}.
DISULFID 90 183 {ECO:0000269|PubMed:4603214}.
VARIANT 38 38 Q -> R (in allele ORM1*S).
{ECO:0000269|PubMed:15164053,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9050929,
ECO:0000269|Ref.7}.
/FTId=VAR_013840.
VARIANT 167 167 R -> C (in dbSNP:rs3182034).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_056166.
VARIANT 174 174 V -> M (in allele ORM1*F2;
dbSNP:rs1126801).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9050929}.
/FTId=VAR_013841.
CONFLICT 170 170 K -> R (in Ref. 8; AAI43315).
{ECO:0000305}.
CONFLICT 182 182 Missing (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 193 193 Missing (in Ref. 10; AA sequence).
{ECO:0000305}.
HELIX 24 26 {ECO:0000244|PDB:3KQ0}.
HELIX 33 39 {ECO:0000244|PDB:3KQ0}.
STRAND 41 52 {ECO:0000244|PDB:3KQ0}.
HELIX 53 59 {ECO:0000244|PDB:3KQ0}.
STRAND 62 72 {ECO:0000244|PDB:3KQ0}.
TURN 73 76 {ECO:0000244|PDB:3KQ0}.
STRAND 77 86 {ECO:0000244|PDB:3KQ0}.
STRAND 89 100 {ECO:0000244|PDB:3KQ0}.
TURN 101 104 {ECO:0000244|PDB:3KQ0}.
STRAND 105 110 {ECO:0000244|PDB:3KQ0}.
STRAND 113 121 {ECO:0000244|PDB:3KQ0}.
STRAND 127 132 {ECO:0000244|PDB:3KQ0}.
HELIX 137 139 {ECO:0000244|PDB:3KQ0}.
STRAND 141 149 {ECO:0000244|PDB:3KQ0}.
TURN 153 156 {ECO:0000244|PDB:3KQ0}.
HELIX 157 166 {ECO:0000244|PDB:3KQ0}.
HELIX 170 172 {ECO:0000244|PDB:3KQ0}.
HELIX 178 180 {ECO:0000244|PDB:3KQ0}.
HELIX 184 192 {ECO:0000244|PDB:3KQ0}.
SEQUENCE 201 AA; 23512 MW; 63292233AD6EAD8B CRC64;
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF RNEEYNKSVQ
EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL
ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK
DKCEPLEKQH EKERKQEEGE S


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