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O95445 (APOM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein M

Short name=Apo-M
Short name=ApoM
Alternative name(s):
Protein G3a
Gene names
Name:APOM
Synonyms:G3A, NG20
ORF Names:HSPC336
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. Ref.11 Ref.17

Subcellular location

Secreted. Note: Present in high density lipoprotein (HDL) and to a lesser extent in triglyceride-rich lipoproteins (TGRLP) and low density lipoproteins (LDL). Ref.11 Ref.12 Ref.13

Tissue specificity

Plasma protein. Expressed in liver and kidney.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family. Highly divergent.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentHDL
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol efflux

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

cholesterol homeostasis

Inferred by curator PubMed 15793583. Source: BHF-UCL

high-density lipoprotein particle assembly

Inferred from sequence or structural similarity PubMed 15793583. Source: BHF-UCL

high-density lipoprotein particle clearance

Inferred from sequence or structural similarity PubMed 15793583. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 18006500. Source: BHF-UCL

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of plasma lipoprotein particle oxidation

Inferred from direct assay PubMed 16682745PubMed 22204862. Source: BHF-UCL

response to glucose

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from sequence or structural similarity PubMed 15793583. Source: BHF-UCL

   Cellular_componentdiscoidal high-density lipoprotein particle

Inferred from direct assay PubMed 15793583. Source: BHF-UCL

high-density lipoprotein particle

Inferred from direct assay PubMed 22204862. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

low-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

spherical high-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 17154273. Source: BHF-UCL

   Molecular_functionantioxidant activity

Inferred from direct assay PubMed 22204862. Source: BHF-UCL

lipid transporter activity

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 22204862. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95445-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95445-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Apolipoprotein M
PRO_0000223278
Signal peptide1 – ?2222Not cleaved Ref.1

Sites

Binding site1361Fatty acid
Binding site1431Fatty acid

Amino acid modifications

Glycosylation1351N-linked (GlcNAc...) Ref.10 Ref.14
Disulfide bond23 ↔ 167 Ref.17
Disulfide bond95 ↔ 183 Ref.17
Disulfide bond128 ↔ 157 Ref.17

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_045586

Experimental info

Mutagenesis221Q → A: Introduces a signal cleavage site. Abolishes interaction with lipoprotein particles. Leads to rapid elimination from plasma. Ref.11 Ref.12 Ref.13
Mutagenesis1351N → Q: Loss of glycosylation.
Mutagenesis1481N → Q: No loss of glycosylation.
Sequence conflict1 – 3838MFHQI…VDGKE → RFPDSIWGSRSDTSGSPQVP KLYFCGARRESPQPQT in AAF29014. Ref.3
Sequence conflict175 – 18814LTPRN…ELSNN → VDS in CAB51604. Ref.2

Secondary structure

......................... 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: E4C35FEC32B7CB86

FASTA18821,253
        10         20         30         40         50         60 
MFHQIWAALL YFYGIILNSI YQCPEHSQLT TLGVDGKEFP EVHLGQWYFI AGAAPTKEEL 

        70         80         90        100        110        120 
ATFDPVDNIV FNMAAGSAPM QLHLRATIRM KDGLCVPRKW IYHLTEGSTD LRTEGRPDMK 

       130        140        150        160        170        180 
TELFSSSCPG GIMLNETGQG YQRFLLYNRS PHPPEKCVEE FKSLTSCLDS KAFLLTPRNQ 


EACELSNN 

« Hide

Isoform 2 [UniParc].

Checksum: F78244DE4A76A382
Show »

FASTA11613,051

References

« Hide 'large scale' references
[1]"A novel human apolipoprotein (apoM)."
Xu N., Dahlbaeck B.
J. Biol. Chem. 274:31286-31290(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-15.
Tissue: Liver.
[2]"Characterisation of the novel gene G3a located in the class III region of the human major histocompatibility complex."
Thomson W., Campbell R.D.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Human partial CDS from CD34+ stem cells."
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[4]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation."
Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y., Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J., Stanton L.W.
Nat. Biotechnol. 22:707-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic stem cell.
[7]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"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] (ISOFORM 1).
Tissue: Liver.
[10]"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-135.
Tissue: Plasma.
[11]"Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M."
Ahnstrom J., Faber K., Axler O., Dahlback B.
J. Lipid Res. 48:1754-1762(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-22.
[12]"Apolipoprotein M associates to lipoproteins through its retained signal peptide."
Axler O., Ahnstrom J., Dahlback B.
FEBS Lett. 582:826-828(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-22.
[13]"The signal peptide anchors apolipoprotein M in plasma lipoproteins and prevents rapid clearance of apolipoprotein M from plasma."
Christoffersen C., Ahnstrom J., Axler O., Christensen E.I., Dahlback B., Nielsen L.B.
J. Biol. Chem. 283:18765-18772(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-22.
[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-135.
Tissue: Liver.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis."
Duan J., Dahlbaeck B., Villoutreix B.O.
FEBS Lett. 499:127-132(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, MUTAGENESIS.
[17]"Serendipitous fatty acid binding reveals the structural determinants for ligand recognition in apolipoprotein M."
Sevvana M., Ahnstrom J., Egerer-Sieber C., Lange H.A., Dahlback B., Muller Y.A.
J. Mol. Biol. 393:920-936(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-188 IN COMPLEX WITH FATTY ACIDS, DISULFIDE BONDS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118393 mRNA. Translation: AAD11443.2.
AJ245434 mRNA. Translation: CAB51604.1.
AF161454 mRNA. Translation: AAF29014.1.
AF129756 Genomic DNA. Translation: AAD18084.1.
CN428415 mRNA. No translation available.
BA000025 Genomic DNA. Translation: BAB63389.1.
AL662801 Genomic DNA. Translation: CAI18319.1.
AL670886 Genomic DNA. Translation: CAI17788.1.
AL805934 Genomic DNA. Translation: CAI18511.1.
AL805934 Genomic DNA. Translation: CAI18513.1.
BX511262 Genomic DNA. Translation: CAM45814.1.
BX511262 Genomic DNA. Translation: CAM45816.1.
CR753842 Genomic DNA. Translation: CAQ06561.1.
CR753842 Genomic DNA. Translation: CAQ06563.1.
CR354443 Genomic DNA. Translation: CAQ06991.1.
CR354443 Genomic DNA. Translation: CAQ06993.1.
CR759761 Genomic DNA. Translation: CAQ10868.1.
CR759761 Genomic DNA. Translation: CAQ10870.1.
CH471081 Genomic DNA. Translation: EAX03461.1.
CH471081 Genomic DNA. Translation: EAX03463.1.
BC020683 mRNA. Translation: AAH20683.1.
CCDSCCDS4710.1. [O95445-1]
CCDS59004.1. [O95445-2]
RefSeqNP_001243098.1. NM_001256169.1. [O95445-2]
NP_061974.2. NM_019101.2. [O95445-1]
UniGeneHs.534468.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WEWX-ray1.95A22-188[»]
2WEXX-ray2.00A22-188[»]
2YG2X-ray1.70A/B22-188[»]
ProteinModelPortalO95445.
SMRO95445. Positions 22-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121006. 2 interactions.
IntActO95445. 2 interactions.
MINTMINT-1379248.
STRING9606.ENSP00000365081.

Proteomic databases

MaxQBO95445.
PaxDbO95445.
PeptideAtlasO95445.
PRIDEO95445.

Protocols and materials databases

DNASU55937.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375916; ENSP00000365081; ENSG00000204444. [O95445-1]
ENST00000375920; ENSP00000365085; ENSG00000204444. [O95445-2]
ENST00000383438; ENSP00000372930; ENSG00000206409. [O95445-1]
ENST00000400157; ENSP00000383021; ENSG00000206409. [O95445-2]
ENST00000416324; ENSP00000393581; ENSG00000224290. [O95445-2]
ENST00000422771; ENSP00000392021; ENSG00000226215. [O95445-2]
ENST00000425177; ENSP00000403062; ENSG00000235754. [O95445-2]
ENST00000426800; ENSP00000405730; ENSG00000227567. [O95445-1]
ENST00000430282; ENSP00000401684; ENSG00000224290. [O95445-1]
ENST00000432598; ENSP00000389591; ENSG00000235754. [O95445-1]
ENST00000436931; ENSP00000394610; ENSG00000231974. [O95445-1]
ENST00000439902; ENSP00000413446; ENSG00000227567. [O95445-2]
ENST00000441436; ENSP00000398944; ENSG00000226215. [O95445-1]
ENST00000443975; ENSP00000416335; ENSG00000231974. [O95445-2]
GeneID55937.
KEGGhsa:55937.
UCSCuc003nvk.4. human. [O95445-1]

Organism-specific databases

CTD55937.
GeneCardsGC06P031620.
GC06Pj31607.
GC06Pk31602.
GC06Pl31659.
GC06Pm31696.
GC06Pn31610.
GC06Po31610.
HGNCHGNC:13916. APOM.
HPACAB034086.
HPA051006.
MIM606907. gene.
neXtProtNX_O95445.
PharmGKBPA38370.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40194.
HOGENOMHOG000034009.
HOVERGENHBG018735.
InParanoidO95445.
OMAPRNQEAC.
PhylomeDBO95445.
TreeFamTF330771.

Gene expression databases

ArrayExpressO95445.
BgeeO95445.
CleanExHS_APOM.
GenevestigatorO95445.

Family and domain databases

InterProIPR022734. ApoM.
IPR011038. Calycin-like.
[Graphical view]
PfamPF11032. ApoM. 1 hit.
[Graphical view]
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO95445.
GeneWikiAPOM.
GenomeRNAi55937.
NextBio61349.
PROO95445.
SOURCESearch...

Entry information

Entry nameAPOM_HUMAN
AccessionPrimary (citable) accession number: O95445
Secondary accession number(s): B0UX98 expand/collapse secondary AC list , Q5SRP4, Q9P046, Q9UMP6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 129 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 chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM