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Reviewed, UniProtKB/Swiss-Prot P02763 (A1AG1_HUMAN)

Last modified October 13, 2009. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-1-acid glycoprotein 1
      Short name=AGP 1
Alternative name(s):
    Orosomucoid-1
      Short name=OMD 1
Gene names
Name: ORM1
Synonyms: AGP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Appears to function in modulating the activity of the immune system during the acute-phase reaction.

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.

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.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processAcute phase
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processacute-phase response Ref.1

Traceable author statement. Source: ProtInc

regulation of immune system process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SERPINE1P051211EBI-976767,EBI-953978

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.7
Chain19 – 201183Alpha-1-acid glycoprotein 1
PRO_0000017860

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid Ref.7
Glycosylation331N-linked (GlcNAc...) Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.9
Glycosylation561N-linked (GlcNAc...) Ref.10 Ref.14 Ref.15 Ref.9
Glycosylation721N-linked (GlcNAc...) Ref.10 Ref.12 Ref.14 Ref.15 Ref.9
Glycosylation931N-linked (GlcNAc...) Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.9
Glycosylation1031N-linked (GlcNAc...) Ref.10 Ref.14 Ref.15 Ref.17
CAR_000170
Disulfide bond23 ↔ 165 Ref.9
Disulfide bond90 ↔ 183 Ref.9

Natural variations

Natural variant381Q → R in allele ORM1*S. Ref.6 Ref.19
VAR_013840
Natural variant1671R → C: dbSNP rs3182034.
VAR_056166
Natural variant1741V → M in allele ORM1*F2. dbSNP rs1126801. Ref.19
VAR_013841

Experimental info

Sequence conflict1821Missing AA sequence Ref.8
Sequence conflict1931Missing AA sequence Ref.8

Secondary structure

................................... 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02763-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 63292233AD6EAD8B

FASTA20123,512
        10         20         30         40         50         60 
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF RNEEYNKSVQ 

        70         80         90        100        110        120 
EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL 

       130        140        150        160        170        180 
ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK 

       190        200 
DKCEPLEKQH EKERKQEEGE S 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the genes coding for human alpha 1-acid glycoprotein."
Dente L., Pizza M.G., Metspalu A., Cortese R.
EMBO J. 6:2289-2296(1987) [PubMed: 2822385] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning and nucleotide sequence of human alpha 1 acid glycoprotein cDNA."
Board P.G., Jones I.M., Bentley A.K.
Gene 44:127-131(1986) [PubMed: 3770479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the human alpha 1-acid glycoprotein gene: sequence homology with other human acute phase protein genes."
Dente L., Ciliberto G., Cortese R.
Nucleic Acids Res. 13:3941-3952(1985) [PubMed: 2409529] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-38.
Tissue: Liver.
[7]"Structure of alpha 1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins."
Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T., Ishiguro M., Nanno S.
Biochemistry 12:2711-2724(1973) [PubMed: 4711474] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-129.
[8]"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."
Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W., Schmid K.
Biochemistry 11:3817-3829(1972) [PubMed: 4561179] [Abstract]
Cited for: PROTEIN SEQUENCE OF 129-201.
[9]"The disulfide bonds of alpha1-acid glycoprotein."
Schmid K., Buergi W., Collins J.H., Nanno S.
Biochemistry 13:2694-2697(1974) [PubMed: 4603214] [Abstract]
Cited for: DISULFIDE BONDS.
[10]"Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein."
Treuheit M.J., Costello C.E., Halsall H.B.
Biochem. J. 283:105-112(1992) [PubMed: 1567356] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
[11]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33.
[12]"A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation."
Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.
J. Proteome Res. 3:556-566(2004) [PubMed: 15253437] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, MASS SPECTROMETRY.
[13]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed: 15084671] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93, MASS SPECTROMETRY.
Tissue: Bile.
[14]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103, MASS SPECTROMETRY.
Tissue: Plasma.
[15]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103, MASS SPECTROMETRY.
Tissue: Plasma.
[16]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed: 16740002] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, MASS SPECTROMETRY.
Tissue: Saliva.
[17]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103, MASS SPECTROMETRY.
Tissue: Liver.
[18]"Three-dimensional modeling of the protein moiety of human alpha1-acid glycoprotein, a lipocalin-family member."
Rojo-Dominguez A., Hernandez-Arana A.
Protein Seq. Data Anal. 5:349-355(1993)
Cited for: 3D-STRUCTURE MODELING.
[19]"Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S."
Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., Irizawa Y.
Hum. Genet. 99:393-398(1997) [PubMed: 9050929] [Abstract]
Cited for: VARIANTS ARG-38 AND MET-174.
+Additional computationally mapped references.

Cross-references

Sequence databases

X02544 mRNA. Translation: CAA26397.1.
M13692 mRNA. Translation: AAA35515.1.
X05779 expand/collapse EMBL AC list , X05780, X05781, X05782, X05783, X05784 Genomic DNA. Translation: CAA29229.1. Sequence problems.
X06676 Genomic DNA. No translation available.
X06680 Genomic DNA. No translation available.
BT019790 mRNA. Translation: AAV38593.1.
AK312035 mRNA. Translation: BAG34972.1.
BC026238 mRNA. Translation: AAH26238.1.
IPIIPI00022429.
PIROMHU1. A28346.
RefSeqNP_000598.2.
UniGeneHs.522356

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3BX6X-ray1.80A19-201[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP02763. 2 interactions.
STRINGP02763.

PTM databases

GlycoSuiteDBP02763.

2-D gel databases

SWISS-2DPAGEP02763.
Siena-2DPAGEP02763.

Proteomic databases

PeptideAtlasP02763.
PRIDEP02763.

Genome annotation databases

EnsemblENST00000259396; ENSP00000259396; ENSG00000229314; Homo sapiens. [Genome view]
ENST00000438927; ENSP00000388265; ENSG00000229314; Homo sapiens. [Genome view]
GeneID5004.
KEGGhsa:5004.

Organism-specific databases

CTD5004.
GeneCardsGC09P116125.
HGNCHGNC:8498. ORM1.
HPACAB006265.
MIM138600. gene.
PharmGKBPA260.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP02763.
HOVERGENP02763.

Gene expression databases

ArrayExpressP02763.
BgeeP02763.
CleanExHS_ORM1.
GenevestigatorP02763.
GermOnlineENSG00000187681. Homo sapiens.

Family and domain databases

InterProIPR001500. A1A_glycop.
IPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11967. A1A_glycop. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036899. AGP. 1 hit.
PRINTSPR00708. A1AGLPROTEIN.
PROSITEPS00213. LIPOCALIN. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01418. Acenocoumarol.
DB00802. Alfentanil.
DB01429. Aprindine.
DB00280. Disopyramide.
DB01359. Penbutolol.
DB00946. Phenprocoumon.
DB00908. Quinidine.
DB00706. Tamsulosin.
NextBio19272.
SOURCESearch...

Entry information

Entry nameA1AG1_HUMAN
AccessionPrimary (citable) accession number: P02763
Secondary accession number(s): Q5U067, Q8TC16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: October 13, 2009
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents