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P19652 (A1AG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1-acid glycoprotein 2

Short name=AGP 2
Alternative name(s):
Orosomucoid-2
Short name=OMD 2
Gene names
Name:ORM2
Synonyms:AGP2
OrganismHomo sapiens (Human) [Reference 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

Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction. Ref.17

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. Ref.17

Post-translational modification

N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). Ref.9 Ref.10 Ref.16

Polymorphism

Many different variants of ORM2 are known.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Sequence caution

The sequence CAA29873.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA29874.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 201183Alpha-1-acid glycoprotein 2
PRO_0000017861

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid
Glycosylation331N-linked (GlcNAc...) (complex) Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Glycosylation561N-linked (GlcNAc...) Ref.9 Ref.12 Ref.13 Ref.14
Glycosylation721N-linked (GlcNAc...) Ref.9 Ref.12 Ref.13
Glycosylation931N-linked (GlcNAc...) Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
Glycosylation1031N-linked (GlcNAc...) Ref.9 Ref.13 Ref.14
CAR_000171
Disulfide bond23 ↔ 165 Ref.8 Ref.17
Disulfide bond90 ↔ 183 Ref.8 Ref.17

Natural variations

Natural variant381R → Q.
Corresponds to variant rs17650 [ dbSNP | Ensembl ].
VAR_014667
Natural variant991V → A.
Corresponds to variant rs2636889 [ dbSNP | Ensembl ].
VAR_050172
Natural variant1411G → R.
Corresponds to variant rs12685968 [ dbSNP | Ensembl ].
VAR_050173
Natural variant1671C → R. Ref.17
Corresponds to variant rs1126777 [ dbSNP | Ensembl ].
VAR_050174
Natural variant1741M → V.
Corresponds to variant rs2636890 [ dbSNP | Ensembl ].
VAR_050175

Experimental info

Sequence conflict321T → I in CAG33211. Ref.4
Sequence conflict1021E → D in BAG35159. Ref.3
Sequence conflict1251T → I in BAG35159. Ref.3
Sequence conflict1621A → V in BAG35159. Ref.3
Sequence conflict1891Q → H in BAG35159. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P19652 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 49167ABCC22933B9

FASTA20123,603
        10         20         30         40         50         60 
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ 

        70         80         90        100        110        120 
EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL 

       130        140        150        160        170        180 
FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK 

       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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and characterisation of a duplicated human alpha 1 acid glycoprotein gene."
Merritt C.M., Board P.G.
Gene 66:97-106(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[8]"The disulfide bonds of alpha1-acid glycoprotein."
Schmid K., Buergi W., Collins J.H., Nanno S.
Biochemistry 13:2694-2697(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[9]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
[10]"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] [Europe PMC] [Abstract]
Cited for: PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33.
Tissue: Bile.
[12]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND ASN-93.
Tissue: Plasma.
[13]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
Tissue: Plasma.
[14]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-93 AND ASN-103.
Tissue: Liver.
[15]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[16]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Structural insights into differences in drug-binding selectivity between two forms of human {alpha}1-acid glycoprotein genetic variants, the A and F1*S forms."
Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H., Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.
J. Biol. Chem. 286:14427-14434(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE, FUNCTION, DISULFIDE BONDS, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06675 Genomic DNA. Translation: CAA29874.1. Sequence problems.
X05780 Genomic DNA. No translation available.
X06674 expand/collapse EMBL AC list , X06676, X06677, X06678, X06679, X06680 Genomic DNA. Translation: CAA29873.2. Sequence problems.
X05784 Genomic DNA. No translation available.
M21540 Genomic DNA. Translation: AAA51549.1.
AK312226 mRNA. Translation: BAG35159.1.
CR456930 mRNA. Translation: CAG33211.1.
AL356796 Genomic DNA. Translation: CAI16860.1.
CH471090 Genomic DNA. Translation: EAW87417.1.
BC015964 mRNA. Translation: AAH15964.1.
BC056239 mRNA. Translation: AAH56239.1.
CCDSCCDS6804.1.
PIROMHU2. JT0326.
RefSeqNP_000599.1. NM_000608.2.
UniGeneHs.719954.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3APUX-ray2.10A/B19-201[»]
3APVX-ray2.15A/B19-201[»]
3APWX-ray2.20A/B19-201[»]
3APXX-ray2.20A19-201[»]
ProteinModelPortalP19652.
SMRP19652. Positions 19-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111047. 3 interactions.
IntActP19652. 3 interactions.
STRING9606.ENSP00000394936.

Chemistry

ChEMBLCHEMBL5958.

PTM databases

PhosphoSiteP19652.
UniCarbKBP19652.

Polymorphism databases

DMDM231458.

2D gel databases

DOSAC-COBS-2DPAGEP19652.
SWISS-2DPAGEP19652.

Proteomic databases

MaxQBP19652.
PeptideAtlasP19652.
PRIDEP19652.

Protocols and materials databases

DNASU5005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000431067; ENSP00000394936; ENSG00000228278.
GeneID5005.
KEGGhsa:5005.
UCSCuc004bil.3. human.

Organism-specific databases

CTD5005.
GeneCardsGC09P117092.
HGNCHGNC:8499. ORM2.
HPAHPA046438.
MIM138610. gene.
neXtProtNX_P19652.
PharmGKBPA32818.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000125170.
HOVERGENHBG000035.
InParanoidP19652.
KOK17308.
OMASKEHMEE.
OrthoDBEOG7B5WXT.
PhylomeDBP19652.
TreeFamTF343791.

Gene expression databases

ArrayExpressP19652.
BgeeP19652.
GenevestigatorP19652.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR001500. A1A_glycop.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERPTHR11967. PTHR11967. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036899. AGP. 1 hit.
PRINTSPR00708. A1AGLPROTEIN.
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP19652.
GenomeRNAi5005.
NextBio19276.
PROP19652.
SOURCESearch...

Entry information

Entry nameA1AG2_HUMAN
AccessionPrimary (citable) accession number: P19652
Secondary accession number(s): B2R5L2 expand/collapse secondary AC list , Q16571, Q5T538, Q6IB74
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM